|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1511 |
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: 2400.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 7 CSPNSSEPFWDWSRSWNTSNPDLTPCFQNTVLVWVPCFYLWICAPFYLMYMRSHNRGYICMSHLNKAKTAVGFLLWIICW 86
Cdd:TIGR00957 1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 87 LDVFYTFWERSHSSnITAAVHLVSPTLLGLTMLLATLIVQYERMKGVQSSGVMLIFWLLALLCATVTFRSKILQAQDQPE 166
Cdd:TIGR00957 81 ADLFYSFWERSHGR-APAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 167 SVSVWRYTTFYIYYTLLLLALILSGLSDQMPLFSQAVKDSNPCPEPGASFLSRITFWWISGMMVSGYKRPLEEKDLWSLN 246
Cdd:TIGR00957 160 IVDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 247 PEDQSHCVVPQLLRRWSAECHKVKRTEGKMVYSPKQP--PRGESKEDrAVEESEILIVKTPKKSREASLLWALCLTFAPY 324
Cdd:TIGR00957 240 KEDTSEMVVPVLVENWKKECKKTRKQPVSAVYGKKDPskPKGSSQLD-ANEEVEALIVKSPHKPRKPSLFKVLYKTFGPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 325 FLVSCLYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVY 404
Cdd:TIGR00957 319 FLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 405 RKALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIA 484
Cdd:TIGR00957 399 RKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 485 MKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALST 564
Cdd:TIGR00957 479 MKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALIT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 565 FSVYVLSNDQNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRLRVFLSHEELQEDSVEH-PAAGCSAYSIS 643
Cdd:TIGR00957 559 FAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERrTIKPGEGNSIT 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 644 IEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQNATLKNN 723
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLREN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFGQKRKESWYQRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKH 803
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 804 IFDQVIGPQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFLRTYASSEQTDGSE------ 877
Cdd:TIGR00957 799 IFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEdswtal 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 878 -PVPNSPSKPMENG------VGPGFTGSSQSASNNSKGPASELNKEEKKSKS---AEAGKLTDADKASTGRVKLSVFCSY 947
Cdd:TIGR00957 879 vSGEGKEAKLIENGmlvtdvVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAeakEETWKLMEADKAQTGQVELSVYWDY 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 948 LKAIGVLLSAISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPDRLMRLGVYGGLGVSQGVAVFGYSLSVSIGGILASR 1027
Cdd:TIGR00957 959 MKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASR 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1028 FLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLY 1107
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLY 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1108 FFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFV 1187
Cdd:TIGR00957 1119 FFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECV 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1188 GNCIVSFAALFAVLARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYSDTEKEAEWRHEPPTVPPD 1267
Cdd:TIGR00957 1199 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSG 1278
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1268 WPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHEL 1347
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL 1358
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1348 RSRITIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLR 1427
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1428 KTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRMAK 1507
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
....
gi 1357684105 1508 DAGL 1511
Cdd:TIGR00957 1519 DAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
209-1510 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1048.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 209 CPEPGASFLSRITFWWISGMMVSGYKRPLEEKDLWSLNPEDQSHCVVPQLLRRWSAECHKVKrtegkmvyspkqpPRges 288
Cdd:PLN03130 227 CPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPK-------------PW--- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 289 kedraveeseilivktpkksreasLLWALCLTFAPYFLVSCLYKFIQDILMFAGPEILRLLIKFVNDPDaPPWQGYFYTA 368
Cdd:PLN03130 291 ------------------------LLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGE-PAWIGYIYAF 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 369 LLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAP 448
Cdd:PLN03130 346 SIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAP 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 449 LQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKV 528
Cdd:PLN03130 426 FRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 529 SQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTFSVYVLSNdqNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQ 608
Cdd:PLN03130 506 QTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLG--GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVN 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 609 ASVSLKRLRVFLSHEE--LQEDSVEHPaaGCSAysISIEDGVFSW-SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSL 685
Cdd:PLN03130 584 ANVSLKRLEELLLAEErvLLPNPPLEP--GLPA--ISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSL 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 686 LSALLGEMDKME-GSVAVKGSVAYVPQQAWIQNATLKNNIIFGQKRKESWYQRVVEACALQQDLDILPAGDETEIGEKGV 764
Cdd:PLN03130 660 ISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGV 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 765 NLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIgpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEI 844
Cdd:PLN03130 740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 845 TEIGSYLQLKEEEGAFAEFLRTYASSEQTD---GSEPVPNSPSKPMENGVGPGFTGSSqSASNNSKGPASELNKEEKKSk 921
Cdd:PLN03130 818 KEEGTYEELSNNGPLFQKLMENAGKMEEYVeenGEEEDDQTSSKPVANGNANNLKKDS-SSKKKSKEGKSVLIKQEERE- 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 922 saeagkltdadkasTGRVKLSVFCSYLKAIG-VLLSAISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPdrLMRLGVY 1000
Cdd:PLN03130 896 --------------TGVVSWKVLERYKNALGgAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKTHGP--LFYNLIY 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1001 GGLGVSQGVAVFGYSLSVSIGGILASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLF 1080
Cdd:PLN03130 960 ALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIF 1039
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1081 NVLGSCVII-LVATPMVAFIIPFLgLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHES 1159
Cdd:PLN03130 1040 QLLSTFVLIgIVSTISLWAIMPLL-VLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEIN 1118
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1160 DQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIVSFAALFAVLARENLS-----PGIMGLSISYALQLTASLTWLVRMSSD 1234
Cdd:PLN03130 1119 GRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAEnqaafASTMGLLLSYALNITSLLTAVLRLASL 1198
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1235 VETNIVAVERVKEYSDTEKEAEWRHEPPTVPPDWPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGK 1314
Cdd:PLN03130 1199 AENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGK 1278
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1315 SSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVS 1394
Cdd:PLN03130 1279 SSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIR 1358
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1395 GLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMD 1474
Cdd:PLN03130 1359 RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID 1438
|
1290 1300 1310
....*....|....*....|....*....|....*..
gi 1357684105 1475 YTRVLVLDKGQMAEFDSPSSLIAQKG-AFYRMAKDAG 1510
Cdd:PLN03130 1439 CDRILVLDAGRVVEFDTPENLLSNEGsAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
207-1510 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 958.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 207 NPCPEPGASFLSRITFWWISGMMVSGYKRPLEEKDLWSLNPEDQSHCVVPQLLRRWsaechkvkrtegkmvyspkqpprg 286
Cdd:PLN03232 225 NICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCW------------------------ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 287 eskedraVEESeilivKTPKksreASLLWALCLTFAPYFLVSCLYKFIQDILMFAGPEILRLLIKFVNDPDaPPWQGYFY 366
Cdd:PLN03232 281 -------TEES-----RRPK----PWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGYVY 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 367 TALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWS 446
Cdd:PLN03232 344 AFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWS 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 447 APLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRD 526
Cdd:PLN03232 424 APFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFES 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 527 KVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTFSVYVLSNDQnvLDAQKAFVSLALFNILRFPLNMLPMVISSM 606
Cdd:PLN03232 504 RIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQV 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 607 VQASVSLKRLR-VFLSHEELQedsVEHPAAGCSAYSISIEDGVFSW-SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSS 684
Cdd:PLN03232 582 VNANVSLQRIEeLLLSEERIL---AQNPPLQPGAPAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTS 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 685 LLSALLGEMDKME-GSVAVKGSVAYVPQQAWIQNATLKNNIIFGQKRKESWYQRVVEACALQQDLDILPAGDETEIGEKG 763
Cdd:PLN03232 659 LISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERG 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 764 VNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPQglLKDKTRILVTHGLSYLPQADLVLVMVDGE 843
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGM 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 844 ITEIGSYLQLKEEEGAFaeflrtyasseqtdgsepvpnspSKPMENGvgpGFTGSSQSASNNS-----KGPASELNKEEK 918
Cdd:PLN03232 817 IKEEGTFAELSKSGSLF-----------------------KKLMENA---GKMDATQEVNTNDenilkLGPTVTIDVSER 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 919 KSKSAEAGK-----LTDADKASTGRVKLSVFCSYLKAIG-VLLSAISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPD 992
Cdd:PLN03232 871 NLGSTKQGKrgrsvLVKQEERETGIISWNVLMRYNKAVGgLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPG 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 993 rlMRLGVYGGLGVSQGVAVFGYSLSVSIGGILASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMIL 1072
Cdd:PLN03232 951 --FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLM 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1073 KMFMGSLFNVLGSCVII-LVATPMVAFIIPFLgLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGE 1151
Cdd:PLN03232 1029 NMFMNQLWQLLSTFALIgTVSTISLWAIMPLL-ILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKA 1107
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1152 QERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIVSFAALFAVLARENLS-----PGIMGLSISYALQLTASLT 1226
Cdd:PLN03232 1108 YDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLS 1187
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1227 WLVRMSSDVETNIVAVERVKEYSDTEKEAEWRHEPPTVPPDWPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGI 1306
Cdd:PLN03232 1188 GVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGV 1267
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1307 VGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEF 1386
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALER 1347
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1387 SHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIA 1466
Cdd:PLN03232 1348 AHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA 1427
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*
gi 1357684105 1467 HRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKG-AFYRMAKDAG 1510
Cdd:PLN03232 1428 HRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
302-1496 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 770.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 302 VKTPKKsreASLLWALCLTFAPYFLVSCLYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQGYFYTALLFVCTCVQSLIL 381
Cdd:PTZ00243 226 PPTPKR---LSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 382 QRYFHVCFVSGMRLRTAVIGAVYRKALVIS--SAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLW 459
Cdd:PTZ00243 303 HRFYYISIRCGLQYRSALNALIFEKCFTISskSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 460 ENLGPSVLAGVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVL 539
Cdd:PTZ00243 383 RLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 540 KKAAYLGAVSTFTWVCAPFLVALSTFSVYVLSNdqNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRLRVF 619
Cdd:PTZ00243 463 RDVQLARVATSFVNNATPTLMIAVVFTVYYLLG--HELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTF 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 620 LS-----------HEELQEDSVEHPAAgC--------------------------------------------------- 637
Cdd:PTZ00243 541 LEcdnatcstvqdMEEYWREQREHSTA-Cqlaavlenvdvtafvpvklprapkvktsllsralrmlcceqcrptkrhpsp 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 638 ------------SAYSISIEDGVFSWSRSESPT-----------------------LKRLNVRVPEGSLVAVVGHVGSGK 682
Cdd:PTZ00243 620 svvvedtdygspSSASRHIVEGGTGGGHEATPTsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGK 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 683 SSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQNATLKNNIIFGQKRKESWYQRVVEACALQQDLDILPAGDETEIGEK 762
Cdd:PTZ00243 700 STLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEK 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 763 GVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIgpQGLLKDKTRILVTHGLSYLPQADLVLVMVDG 842
Cdd:PTZ00243 780 GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 843 EITEIGSYlqlkeeegafAEFLRT--YAS-----SEQTDGSEPVPNSPSKPMEngVGPGFTGSSQSASNNSKGPASElnk 915
Cdd:PTZ00243 858 RVEFSGSS----------ADFMRTslYATlaaelKENKDSKEGDADAEVAEVD--AAPGGAVDHEPPVAKQEGNAEG--- 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 916 EEKKSKSAEAGKLTDADKASTGRVKLSVFCSYLKAIGVLLSAISLLF-FLSHNLLSMFANYWLSLWTDDPVVNGTQPDRL 994
Cdd:PTZ00243 923 GDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLAtFAVTELVTVSSGVWLSMWSTRSFKLSAATYLY 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 995 MRLGVygglgVSQGVAVFGYSLSVSIGGI-LASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILK 1073
Cdd:PTZ00243 1003 VYLGI-----VLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYL 1077
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1074 MFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQE 1153
Cdd:PTZ00243 1078 YLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAH 1157
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1154 RFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIVSFAALFAV------LARENLspGIMGLSISYALQLTASLTW 1227
Cdd:PTZ00243 1158 LVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVigtmlrATSQEI--GLVSLSLTMAMQTTATLNW 1235
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1228 LVRMSSDVETNIVAVERVKEYSD-TEKEA--EWRHE----------------PPTVPPDWPTEGCIHITNFG-------- 1280
Cdd:PTZ00243 1236 LVRQVATVEADMNSVERLLYYTDeVPHEDmpELDEEvdalerrtgmaadvtgTVVIEPASPTSAAPHPVQAGslvfegvq 1315
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1281 LRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVL 1360
Cdd:PTZ00243 1316 MRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVL 1395
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1361 FSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVL-DEATA 1439
Cdd:PTZ00243 1396 FDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATA 1475
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1440 AVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLI 1496
Cdd:PTZ00243 1476 NIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
327-616 |
1.20e-178 |
|
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: 533.97 E-value: 1.20e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 327 VSCLYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRK 406
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 407 ALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMK 486
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 487 TKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTFS 566
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 567 VYVLSNDQNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
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, ... |
956-1249 |
8.89e-163 |
|
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: 492.38 E-value: 8.89e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 956 SAISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQP--DRLMRLGVYGGLGVSQGVAVFGYSLSVSIGGILASRFLHQSM 1033
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDteQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPM-VAFIIPfLGLLYFFVQR 1112
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIfLVVIIP-LAILYFFIQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1113 FYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIV 1192
Cdd:cd18603 160 FYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1193 SFAALFAVLARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18603 240 LFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
210-1502 |
7.67e-162 |
|
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: 528.71 E-value: 7.67e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 210 PEPGASFLSRITFWWISGMMVSGYKRPLEEKDLWSLNPEDQSHCVVPQLLRRWSAEchkvkrtegkmVYSPKQPPRgesk 289
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRE-----------LASAKKNPK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 290 edraveeseilivktpkksreasLLWALCLTFAPYFLVSCLYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQGYFYTA- 368
Cdd:TIGR01271 70 -----------------------LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLAl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 369 ---LLFVctcVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIW 445
Cdd:TIGR01271 127 glcLLFI---VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVW 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 446 SAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFR 525
Cdd:TIGR01271 204 IAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAME 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 526 DKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTFSVYVLSNDqnvLDAQKAFVSLALFNILRFPLN-MLPMVIS 604
Cdd:TIGR01271 284 KIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKG---IILRRIFTTISYCIVLRMTVTrQFPGAIQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 605 SMVQASVSLKRLRVFLSHEEL---------------------------------QEDSVEHPAAGcsaysisiEDGVF-- 649
Cdd:TIGR01271 361 TWYDSLGAITKIQDFLCKEEYktleynltttevemvnvtaswdegigelfekikQNNKARKQPNG--------DDGLFfs 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 650 SWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQNATLKNNIIFGQK 729
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLS 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 730 RKESWYQRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVI 809
Cdd:TIGR01271 513 YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 810 GPqgLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFL-----------------------RT 866
Cdd:TIGR01271 593 CK--LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrnsiltetlrRV 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 867 YASSEQTDGSEP-----------------------------------VPNSPSKPMENGV-------------------- 891
Cdd:TIGR01271 671 SIDGDSTVFSGPetikqsfkqpppefaekrkqsiilnpiasarkfsfVQMGPQKAQATTIedavrepserkfslvpedeq 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 892 -------------GPGFTGSSQSA-----SNNSKGP----ASELNKEEKKSKSAEAGKLTDADKASTGRVKLSVF----- 944
Cdd:TIGR01271 751 geeslprgnqyhhGLQHQAQRRQSvlqlmTHSNRGEnrreQLQTSFRKKSSITQQNELASELDIYSRRLSKDSVYeisee 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 945 --------C---------------SYLKAIGVLLSAISLLFFLSHNLLSMFANYWLSLW--TDDPVVNGTQ--------- 990
Cdd:TIGR01271 831 ineedlkeCfaderenvfetttwnTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWliTDNPSAPNYVdqqhanass 910
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 991 PDRLMRLGVYGG---------LGVSQGVAVFGY--SLSVSIGGILASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAK 1059
Cdd:TIGR01271 911 PDVQKPVIITPTsayyifyiyVGTADSVLALGFfrGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTK 990
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1060 EMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNET 1139
Cdd:TIGR01271 991 DMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITS 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1140 LLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVgncIVSF--AALFAVLARENLSPGIMGLSISY 1217
Cdd:TIGR01271 1071 LKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGIILTL 1147
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1218 ALQLTASLTWLVRMSSDVETNIVAVERVKEYSDT---EKEAEWRHEP-----------PTVPPDWPTEGCIHITNFGLRY 1283
Cdd:TIGR01271 1148 AMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLpqeEPRPSGGGGKyqlstvlvienPHAQKCWPSGGQMDVQGLTAKY 1227
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1284 RSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEpAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSG 1363
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 TLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDL 1443
Cdd:TIGR01271 1307 TFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1444 ETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAF 1502
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
327-616 |
1.45e-124 |
|
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: 389.92 E-value: 1.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 327 VSCLYKFIQDILMFAGPEILRLLIKFVND-PDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYR 405
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 406 KALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAM 485
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 486 KTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTF 565
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 566 SVYVLSNdqNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18579 241 ATYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1272-1492 |
2.72e-120 |
|
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: 375.29 E-value: 2.72e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1272 GCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRI 1351
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1352 TIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKV 1431
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1432 LVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSP 1492
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
642-843 |
7.80e-115 |
|
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: 359.48 E-value: 7.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSE---SPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQNA 718
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIFGQKRKESWYQRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDA 798
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1357684105 799 HVGKHIFDQVIGPqGLLKDKTRILVTHGLSYLPQADLVLVMVDGE 843
Cdd:cd03250 161 HVGRHIFENCILG-LLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
956-1249 |
2.78e-114 |
|
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: 361.82 E-value: 2.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 956 SAISLLFFLSHNLLSMFANYWLSLWTDDpVVNGTQPDRLMRLGVYGGLGV-SQGVAVFGYSLSVSIGGILASRFLHQSML 1034
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD-WSSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1035 FDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQRFY 1114
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1115 VASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIVSF 1194
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1195 AALFAVLARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18580 240 VALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
330-616 |
5.13e-113 |
|
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: 358.45 E-value: 5.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 330 LYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKALV 409
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 410 ISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMKTKT 489
Cdd:cd18559 84 SPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 490 YQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTFSVYV 569
Cdd:cd18559 164 LKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1357684105 570 LSNDQNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18559 244 SRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
957-1507 |
1.47e-109 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 359.86 E-value: 1.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 957 AISLLFFLSHNLLSMFANYWLSLWTDDpVVNGTQPDRLMRL-GVYGGLGVSQGVAVFGYSLsvsIGGILASRFLHQ--SM 1033
Cdd:COG1132 24 ILALLLLLLSALLELLLPLLLGRIIDA-LLAGGDLSALLLLlLLLLGLALLRALLSYLQRY---LLARLAQRVVADlrRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQR 1112
Cdd:COG1132 100 LFEhLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1113 FYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIV 1192
Cdd:COG1132 180 LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1193 SFAALFAVL--ARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYSDTEKEAEwrhEPPTVPPDWPT 1270
Cdd:COG1132 260 ALVLLVGGLlvLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP---DPPGAVPLPPV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1271 EGCIHITNFGLRYRSDlDLAIRNINVDISGGEKVGIVGRTGAGKSSLT-LgLFRIIEPAEGQISIDGVDIAKLGLHELRS 1349
Cdd:COG1132 337 RGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVnL-LLRFYDPTSGRILIDGVDIRDLTLESLRR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1350 RITIIPQDPVLFSGTLRMNL---DPfdSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQllclarall 1426
Cdd:COG1132 415 QIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQriaiarall 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1427 rKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRMA 1506
Cdd:COG1132 493 kDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLY 572
|
.
gi 1357684105 1507 K 1507
Cdd:COG1132 573 R 573
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
969-1249 |
1.39e-103 |
|
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: 332.13 E-value: 1.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 969 LSMFANYWLSLWTDDpvvngtQPDRLMR--LGVYGGLGVSQGVAVFGYSLSVSIGGILASRFLHQSMLFDVLRSPMSFFE 1046
Cdd:cd18606 14 AQVFTNLWLSFWTED------FFGLSQGfyIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1047 RTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQRFYVASSRQLKRLES 1126
Cdd:cd18606 88 TTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLES 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1127 VSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIVSFAALFAVLARENL 1206
Cdd:cd18606 168 ILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFSI 247
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1357684105 1207 SPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18606 248 SPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
959-1249 |
4.00e-94 |
|
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: 305.68 E-value: 4.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 959 SLLFFLSHNLL--SMFANYWLSLWTDDPVvNGTQPDRLMRLGVYGGLGVSQGVAVFGYSLSVSIGGILASRFLHQSMLFD 1036
Cdd:cd18559 2 FLLIKLVLCNHvfSGPSNLWLLLWFDDPV-NGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPfLGLLYFFVQRFYVA 1116
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIP-LGLLYVPVNRVYAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1117 SSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDhNQKAYYPSIVANRWLAIRLEFVGNCIVSFAA 1196
Cdd:cd18559 160 SSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1197 LFAVLARENLSpGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18559 239 FFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
957-1249 |
6.54e-93 |
|
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: 302.46 E-value: 6.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 957 AISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPDRLMR----LGVYGGLGVSQGVAVFGYSLSVSIGGILASRFLHQS 1032
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSvlyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1033 MLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPmvAFIIP--FLGLLYFFV 1110
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSP--AFLLPavVLAALYVYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1111 QRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNC 1190
Cdd:cd18604 160 GRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1191 IVSFAALFAVLAReNLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18604 240 FSFATAALLVYGP-GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1268-1492 |
4.91e-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: 296.25 E-value: 4.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1268 WPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHEL 1347
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1348 RSRITIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFshlktfvsglpdklshecSEGGENLSVGQRQLLCLARALLR 1427
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1428 KTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSP 1492
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
329-616 |
2.15e-88 |
|
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: 290.17 E-value: 2.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 329 CLYKFIQDILMFAGPEILRLLIKFV-NDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKA 407
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 408 LVI-------------------SSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLA 468
Cdd:cd18596 83 LRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 469 GVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAV 548
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 549 STFTWVCAPFLVALSTFSVYVLSNDQNvLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLVMGQE-LTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
329-616 |
2.75e-87 |
|
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: 286.37 E-value: 2.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 329 CLYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKAL 408
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 409 VISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMKTK 488
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 489 TYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTFSVY 568
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1357684105 569 VLSNDQnvLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18598 243 VLMGNT--LTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
959-1248 |
1.23e-85 |
|
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: 282.11 E-value: 1.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 959 SLLFFLSHNLL---SMFANYWLSLWTD---DPVVNGTQPDRLMRLGVYGGLGVSQGVAVFGYSLSVSIGGILASRFLHQS 1032
Cdd:cd18605 1 LILILLSLILMqasRNLIDFWLSYWVShsnNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1033 MLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQR 1112
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1113 FYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIV 1192
Cdd:cd18605 161 YYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1193 SFAALFAVLAR---ENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEY 1248
Cdd:cd18605 241 TFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1016-1507 |
1.24e-84 |
|
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: 293.28 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1016 LSVSIGGILASRFLHQsmlfdVLRSPMSFFERTPSGNLVNRFaKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPM 1095
Cdd:COG2274 223 LGQRIDLRLSSRFFRH-----LLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1096 VAFI----IPFLGLLYFFVQRFYVASSRQLKRLESVSRSpiytHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYY 1171
Cdd:COG2274 297 LALVvlllIPLYVLLGLLFQPRLRRLSREESEASAKRQS----LLVETLRGIETIKALGAESRFRRRWENLLAKYLNARF 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1172 psivANRWLAIRLEFVGNCI--VSFAALFAVLA----RENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:COG2274 373 ----KLRRLSNLLSTLSGLLqqLATVALLWLGAylviDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1246 KEYSDTEKEAEwRHEPPTVPPdwPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRII 1325
Cdd:COG2274 449 DDILDLPPERE-EGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1326 EPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL---DPfdSYSDEDIWKALEFSHLKTFVSGLPDKLSH 1402
Cdd:COG2274 526 EPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDT 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1403 ECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLD 1482
Cdd:COG2274 604 VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLD 683
|
490 500
....*....|....*....|....*
gi 1357684105 1483 KGQMAEFDSPSSLIAQKGAFYRMAK 1507
Cdd:COG2274 684 KGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
327-616 |
9.65e-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: 273.56 E-value: 9.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 327 VSCLYKFIQDILMFAGPEILRLLIKFV-----NDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIG 401
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVedaylGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 402 AVYRKALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNA 481
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 482 VIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVA 561
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 562 LSTFSVYVLSNdqNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18597 241 MLSFITYYATG--HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
327-616 |
1.34e-79 |
|
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: 265.25 E-value: 1.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 327 VSCLYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQ------------------GYFYTALLFVCTCVQSLILQRYFHVC 388
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 389 FVSGMRLRTAVIGAVYRKALVISSAARRTS--TVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSV 466
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGsmTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 467 LAGVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLG 546
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 547 AVSTFTWVCAPFLVALSTFSVYVLSNDQNvLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
957-1249 |
8.43e-78 |
|
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: 259.84 E-value: 8.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 957 AISLLFFLSHNLLSMFANYWLSLWTD-----DPVVNGTQPDRLMR------LGVYGGLGVSQGVAVFGYSLSVSIGGILA 1025
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEanhdvASVVFNITSSSLEDdevsyyISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1026 SRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGL 1105
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1106 LYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLE 1185
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1186 FVGNCIVSFAALFAVLA--RENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18602 242 YLGAVIVFLAALSSLTAalAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1272-1503 |
2.20e-75 |
|
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: 250.98 E-value: 2.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1272 GCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRI 1351
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1352 TIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKV 1431
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1432 LVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFY 1503
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
314-871 |
2.16e-74 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 259.71 E-value: 2.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 314 LWALCLTFAPYFLVSCLYKFIQDILMFAGPEILRLLI-KFVNDPDAPPWqgYFYTALLFVCTCVQSLI--LQRYFHvcFV 390
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSAL--LLLLLLLLGLALLRALLsyLQRYLL--AR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 391 SGMRLRTAVIGAVYRKALVISSAARRTSTVGEIVNLMSVDAQRFMDLV-TYINMIWSAPLQVVLALYFLWeNLGPSV-LA 468
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLF-VIDWRLaLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 469 GVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYA---WEMA-FRDKVSQIRENELQVLKKAAY 544
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 545 LGAVSTFTWVCAPFLVALstFSVY-VLSNDQNVLDAQkAFVSLALFniLRFPLNMLPMVISSMVQASVSLKRLRVFLSHE 623
Cdd:COG1132 247 FFPLMELLGNLGLALVLL--VGGLlVLSGSLTVGDLV-AFILYLLR--LFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 624 ELQEDSVEHPAAGCSAYSISIEDGVFSWsRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVK 703
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 704 G-------------SVAYVPQQAWIQNATLKNNIIFGqkRKESWYQRVVEACALQQ---DLDILPAGDETEIGEKGVNLS 767
Cdd:COG1132 401 GvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYG--RPDATDEEVEEAAKAAQaheFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 768 GGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEI 847
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570 580
....*....|....*....|....
gi 1357684105 848 GSYLQLKEEEGAFAEFLRTYASSE 871
Cdd:COG1132 556 GTHEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
952-1249 |
4.32e-72 |
|
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: 244.01 E-value: 4.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 952 GVLLSAISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQ---------------PDRLMRLGVYGGLGVSQGVAVFGYSL 1016
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNnvdnstvdsgnisdnPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1017 SVSIGGILASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMV 1096
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1097 AFIIPFLGLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVA 1176
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1177 NRWLAIRLEFVGNCIVSFAALFAVLARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
329-616 |
4.08e-69 |
|
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: 234.45 E-value: 4.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 329 CLYKFIQDILMFAGPEILRLLIK-FVNDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKA 407
Cdd:cd18594 3 GILLFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 408 LVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMKT 487
Cdd:cd18594 83 LKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 488 KTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTFSV 567
Cdd:cd18594 163 AKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVP 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 568 YVLSNdqNVLDAQKAFVSLALFNILRFPLNM-LPMVISSMVQASVSLKRL 616
Cdd:cd18594 243 YVLTG--NTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
960-1249 |
8.11e-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: 222.97 E-value: 8.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 960 LLFFLSHNLLSMFANYWLSLW---------TDDPVVNGTQ-----PDRLMR--LGVYGGLGVSQGVAVFGYSLSVSIGGI 1023
Cdd:cd18601 9 VLLNIAAQVLYVLSDWWLSYWanleeklndTTDRVQGENStnvdiEDLDRDfnLGIYAGLTAATFVFGFLRSLLFFHVAV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1024 LASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFL 1103
Cdd:cd18601 89 SASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1104 GLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIR 1183
Cdd:cd18601 169 VILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLATSRWLAVR 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1184 LEFVGNCIVSFAALFAVLARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS 1249
Cdd:cd18601 249 LDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
642-842 |
2.49e-64 |
|
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: 217.97 E-value: 2.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSrSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV-----------------AVKG 704
Cdd:cd03290 1 VQVTNGYFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 705 SVAYVPQQAWIQNATLKNNIIFGQKRKESWYQRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDR 784
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDQviGPQGLLKD--KTRILVTHGLSYLPQADLVLVMVDG 842
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE--GILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
333-616 |
6.64e-64 |
|
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: 219.40 E-value: 6.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 333 FIQDILMFAGPEILRLLIKFV--NDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYRKALVI 410
Cdd:cd18593 7 FLEEAIRVVQPIFLGKLIRYFegNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 411 SSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAmktktY 490
Cdd:cd18593 87 SQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-----K 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 491 QVAQMKNK-----DSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALSTF 565
Cdd:cd18593 162 LFSKLRRKtaartDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTF 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 566 SVYVLSNdqNVLDAQKAFVSLALFNILRFPLNM-LPMVISSMVQASVSLKRL 616
Cdd:cd18593 242 LAYILLG--NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
227-865 |
1.91e-62 |
|
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: 227.79 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 227 GMMVSGYKRPLEEKDLWSLnP----EDQSHCVVpqLLRRwsaechkvkRTEGKMVYSPKQPPRGESKEDRAVEESEILIV 302
Cdd:COG2274 60 GLRARGVRLDLEELAELPL-PailhWDGNHFVV--LEGV---------DGDKVTIADPATGRRKLSLEEFAESWTGVALL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 303 KTP--------KKSREASLLWALCLTFAPYFLVSCLYKFIQDILMFAGPeilrLLIKFVND---PDAPPWQGYFYTALLF 371
Cdd:COG2274 128 LEPtpefdkrgEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATP----LFTQVVIDrvlPNQDLSTLWVLAIGLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 372 VCTCVQSLI--LQRYF--HVcfvsGMRLRTAVIGAVYRKALVISSAARRTSTVGEIVNlmsvdaqRFMDLVTYINMIWSA 447
Cdd:COG2274 204 LALLFEGLLrlLRSYLllRL----GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIREFLTGS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 448 PLQVVLALyflwenlgPSVLAGVAVM-----------ILMVPVNAVIAM----KTKTYQVAQMKNKDSRIKLMNEMLNGI 512
Cdd:COG2274 273 LLTALLDL--------LFVLIFLIVLffyspplalvvLLLIPLYVLLGLlfqpRLRRLSREESEASAKRQSLLVETLRGI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 513 KVLKLYAWEMAFRDK----VSQIRENELQVLKKAAYLGAVSTFtwvcapfLVALSTFSVY------VLSNDQNVldaqKA 582
Cdd:COG2274 345 ETIKALGAESRFRRRwenlLAKYLNARFKLRRLSNLLSTLSGL-------LQQLATVALLwlgaylVIDGQLTL----GQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 583 FVSlalFNIL--RF--PLNMLPMVISSMVQASVSLKRLRVFLSHEELQEDSVEHPAAGCSAYSISIEDGVFSWSRSESPT 658
Cdd:COG2274 414 LIA---FNILsgRFlaPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPV 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNII 725
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENIT 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 726 FGqkRKESWYQRVVEAC---ALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGK 802
Cdd:COG2274 571 LG--DPDATDEEIIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 803 HIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFLR 865
Cdd:COG2274 649 IILENL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1290-1500 |
5.30e-61 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 208.62 E-value: 5.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL 1369
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 DPFDSYS-DEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNL 1448
Cdd:cd03254 98 RLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1449 IQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKG 1500
Cdd:cd03254 178 IQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1002-1505 |
2.70e-60 |
|
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: 218.05 E-value: 2.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1002 GLGVSQGVAVFG--YSLSVSIGGILasRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSL 1079
Cdd:TIGR02203 62 GLAVLRGICSFVstYLLSWVSNKVV--RDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1080 FNVLGSCVIIL----VATPMVAFIIPFLGLLyffVQRFyvasSRQLKRLES---VSRSPIYTHFNETLLGTSVIRAFG-- 1150
Cdd:TIGR02203 140 LTVIGLFIVLLyyswQLTLIVVVMLPVLSIL---MRRV----SKRLRRISKeiqNSMGQVTTVAEETLQGYRVVKLFGgq 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1151 --EQERFIHESDQRVDHNQKayypSIVANRWLAIRLEFVGN---CIVSFAALFAVLArENLSPGIMGLSISYALQLTASL 1225
Cdd:TIGR02203 213 ayETRRFDAVSNRNRRLAMK----MTSAGSISSPITQLIASlalAVVLFIALFQAQA-GSLTAGDFTAFITAMIALIRPL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1226 TWLVRMSSDVETNIVAVERVKEYSDTEKEA-EWRHEPPTVppdwptEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKV 1304
Cdd:TIGR02203 288 KSLTNVNAPMQRGLAAAESLFTLLDSPPEKdTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1305 GIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL---DPfDSYSDEDIW 1381
Cdd:TIGR02203 362 ALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1382 KALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCT 1461
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1357684105 1462 VLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAF---YRM 1505
Cdd:TIGR02203 521 TLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYaqlHNM 567
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
946-1500 |
9.93e-60 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 216.16 E-value: 9.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 946 SYLKAIGVLLSAISLLFFLShnLLSMFANYWLSLWTDDPVVNGTQPDR--LMRLGVYGGLGVSQGVAVFGYSLSVSIGGI 1023
Cdd:COG4988 10 RLARGARRWLALAVLLGLLS--GLLIIAQAWLLASLLAGLIIGGAPLSalLPLLGLLLAVLLLRALLAWLRERAAFRAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1024 LASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFakeMDTIDSLIPMILKmFMGSLFNVLGSCVIILVAT----PMVAFI 1099
Cdd:COG4988 88 RVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEALDGYFAR-YLPQLFLAALVPLLILVAVfpldWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1100 I----PFLGLLYFFVQRFY-VASSRQLKRLESVSrspiyTHFNETLLGTSVIRAFG----EQERFIHESDQ--------- 1161
Cdd:COG4988 164 LlvtaPLIPLFMILVGKGAaKASRRQWRALARLS-----GHFLDRLRGLTTLKLFGrakaEAERIAEASEDfrkrtmkvl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1162 RVdhnqkAYYPSIVanrwlairLEFvgncivsFAALF-AVLArenlspGIMGLSISYA-LQLTASLTWLV---------- 1229
Cdd:COG4988 239 RV-----AFLSSAV--------LEF-------FASLSiALVA------VYIGFRLLGGsLTLFAALFVLLlapefflplr 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1230 RMSS---DVETNIVAVERVKEYSDTEKEAewrHEPPTVPPDWPTEGCIHITNFGLRYRSDlDLAIRNINVDISGGEKVGI 1306
Cdd:COG4988 293 DLGSfyhARANGIAAAEKIFALLDAPEPA---APAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVAL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1307 VGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL---DPfdSYSDEDIWKA 1383
Cdd:COG4988 369 VGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1384 LEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVL 1463
Cdd:COG4988 447 LEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVI 526
|
570 580 590
....*....|....*....|....*....|....*..
gi 1357684105 1464 TIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKG 1500
Cdd:COG4988 527 LITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1034-1507 |
4.58e-58 |
|
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: 211.55 E-value: 4.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFDVL-RSPMSFFERTPSGNLVNRFAKEMDTIDSLipmilkmFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYF---- 1108
Cdd:COG4987 94 LYRRLePLAPAGLARLRSGDLLNRLVADVDALDNL-------YLRVLLPLLVALLVILAAVAFLAFFSPALALVLAlgll 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1109 --------FVQRFYVASSRQLKRLesvsRSPIYTHFNETLLGTSVIRAFGEQERF---IHESDQRVDHNQKAyypsivAN 1177
Cdd:COG4987 167 laglllplLAARLGRRAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRAlarLDAAEARLAAAQRR------LA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1178 RWLAIRlEFVGNCIVSFAALFAVL------ARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYSDT 1251
Cdd:COG4987 237 RLSALA-QALLQLAAGLAVVAVLWlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1252 EKEAEwrhEPPTvPPDWPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQ 1331
Cdd:COG4987 316 PPAVT---EPAE-PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1332 ISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL---DPfDSySDEDIWKALEFSHLKTFVSGLPDKLSHECSEGG 1408
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP-DA-TDEELWAALERVGLGDWLAALPDGLDTWLGEGG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1409 ENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAE 1488
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
490
....*....|....*....
gi 1357684105 1489 FDSPSSLIAQKGAFYRMAK 1507
Cdd:COG4987 550 QGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
327-616 |
1.89e-57 |
|
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: 200.87 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 327 VSCLYKFIQDILMFAGPEIL-RLLIKFVNDPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAVYR 405
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 406 KALVISSAarRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAM 485
Cdd:cd18592 81 KILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 486 KTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQVLKKAAYLGAVSTftwVCAPFLVALS-- 563
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISI---SLAPIVPVIAsv 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 564 -TFSVYVLSNdqNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18592 236 vTFLAHVALG--NDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
451-865 |
6.11e-57 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 208.08 E-value: 6.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 451 VVLALYFLWENLGPSVLAGVAVMILMVPVNAVIAMKTKTYQVAQMKNkDSRIKLMnEMLNGIKVLKLY-AWEmAFRDKVS 529
Cdd:COG4987 146 AVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYgALD-RALARLD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 530 QIRENELQVLKKAAYLGAVSTFTwvcAPFLVALSTFSVYVLSNDQ-------NVLDAQKAFVSLALFNILrfplNMLPMV 602
Cdd:COG4987 223 AAEARLAAAQRRLARLSALAQAL---LQLAAGLAVVAVLWLAAPLvaagalsGPLLALLVLAALALFEAL----APLPAA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 603 ISSMVQASVSLKRLRVfLSHEELQEDSVEHPAAGCSAYSISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGK 682
Cdd:COG4987 296 AQHLGRVRAAARRLNE-LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 683 SSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNIIFGqkRKESWYQRVVEACA---LQQ 746
Cdd:COG4987 375 STLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLA--RPDATDEELWAALErvgLGD 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 747 DLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIgpqGLLKDKTRILVTHG 826
Cdd:COG4987 453 WLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHR 529
|
410 420 430
....*....|....*....|....*....|....*....
gi 1357684105 827 LSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFLR 865
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1274-1505 |
3.78e-55 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 192.06 E-value: 3.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPVLFSGTLRMNLdpfdSY-----SDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRK 1428
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1429 TKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRM 1505
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
977-1505 |
3.73e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 200.71 E-value: 3.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 977 LSLWTDDPVVNGTQPdrlmrLGVYGGLGVSqgvavfgyslsvSIGGILASRFLH--QSMLF-------------DV---- 1037
Cdd:PRK10790 46 ISYFIDNMVAKGNLP-----LGLVAGLAAA------------YVGLQLLAAGLHyaQSLLFnraavgvvqqlrtDVmdaa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1038 LRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKmfmgslfNVLGSCVII---LVAT-------PMVAFII-PFLGLL 1106
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVA-------TVLRSAALIgamLVAMfsldwrmALVAIMIfPAVLVV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1107 YFFVQRFyvaSSRQLKRLESVsRSPIYTHFNETLLGTSVIRAFGEQERFihesDQRVDHNQKAYYPSivanRWLAIRLE- 1185
Cdd:PRK10790 182 MVIYQRY---STPIVRRVRAY-LADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSHYMA----RMQTLRLDg 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1186 FVGNCIVS-FAA--------LFAVLARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYSDTEKEAE 1256
Cdd:PRK10790 250 FLLRPLLSlFSAlilcgllmLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1257 WRHEPPTvppdwpTEGCIHITNFGLRYRSDlDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG 1336
Cdd:PRK10790 330 GNDDRPL------QSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1337 VDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQR 1416
Cdd:PRK10790 403 RPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1417 QLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLI 1496
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
....*....
gi 1357684105 1497 AQKGAFYRM 1505
Cdd:PRK10790 563 AAQGRYWQM 571
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1291-1505 |
1.54e-52 |
|
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: 184.74 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL- 1369
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 --DPfdSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDN 1447
Cdd:cd03253 97 ygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1448 LIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRM 1505
Cdd:cd03253 175 EIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
656-872 |
2.23e-52 |
|
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: 185.83 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 656 SPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQNATLKNNIIFGQKRKESWY 735
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 736 QRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPqgLL 815
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LM 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 816 KDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFLRTYASSEQ 872
Cdd:cd03291 208 ANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQ 264
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1274-1485 |
1.43e-51 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 179.12 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPVLFSGTLRMNLdpfdsysdediwkalefshlktfvsglpdklshecseggenLSVGQRQLLCLARALLRKTKVLV 1433
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1434 LDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQ 1485
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
357-858 |
2.21e-50 |
|
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: 188.43 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 357 DAPPWQGYFYTALLFVCTCVQSLI--LQRyfHVCFVSGMRLRTAVIGAVYRKALVISSAARRTSTVGEIVNLMS--VDA- 431
Cdd:COG4988 51 GAPLSALLPLLGLLLAVLLLRALLawLRE--RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTegVEAl 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 432 ----QRFmdLVTYINMIWsAPLQVVLALYFLwenlgpSVLAGV--AVMILMVPVNAVIAMKtktyqVAQMKNKDSRIKLM 505
Cdd:COG4988 129 dgyfARY--LPQLFLAAL-VPLLILVAVFPL------DWLSGLilLVTAPLIPLFMILVGK-----GAAKASRRQWRALA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 506 N------EMLNGIKVLKLYAWEMAFRDKVSQI----RENELQVLKKA----------AYLGAVstftwvcapfLVAlstf 565
Cdd:COG4988 195 RlsghflDRLRGLTTLKLFGRAKAEAERIAEAsedfRKRTMKVLRVAflssavleffASLSIA----------LVA---- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 566 sVYV---LSNDQnvLDAQKAFVSLAL----FNilrfPLNMLpmviSSMVQASVS----LKRLRVFLSHEELQEDSVEHPA 634
Cdd:COG4988 261 -VYIgfrLLGGS--LTLFAALFVLLLapefFL----PLRDL----GSFYHARANgiaaAEKIFALLDAPEPAAPAGTAPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 635 AGCSAYSISIEDGVFSWSrSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG---------- 704
Cdd:COG4988 330 PAAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpas 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 705 ---SVAYVPQQAWIQNATLKNNIIFGQKR-KESWYQRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAV 780
Cdd:COG4988 409 wrrQIAWVPQNPYLFAGTIRENLRLGRPDaSDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARAL 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 781 YCDRSVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEG 858
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1272-1502 |
1.17e-49 |
|
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: 177.74 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1272 GCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEpAEGQISIDGVDIAKLGLHELRSRI 1351
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1352 TIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKV 1431
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1432 LVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAF 1502
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1274-1507 |
3.25e-49 |
|
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: 175.04 E-value: 3.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAI-RNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRIT 1352
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1353 IIPQDPVLFSGTLRMNL---DPfdSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKT 1429
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygKP--DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1430 KVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRMAK 1507
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
958-1225 |
2.17e-48 |
|
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: 173.98 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 958 ISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPDR--LMRLGVYGGLGVSQGVAVFGYSLSVSIGGILASRFLHQSMLF 1035
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1036 DVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQRFYV 1115
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1116 ASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIVSFA 1195
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 1357684105 1196 ALFAVL--ARENLSPGIMGLSISYALQLTASL 1225
Cdd:pfam00664 243 LWFGAYlvISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1290-1486 |
3.77e-47 |
|
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: 168.54 E-value: 3.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL 1369
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 DPFDSY-SDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNL 1448
Cdd:cd03245 99 TLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1357684105 1449 IQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQM 1486
Cdd:cd03245 179 LKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1292-1505 |
6.56e-47 |
|
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: 179.25 E-value: 6.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLdp 1371
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI-- 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1372 fdSY-----SDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETD 1446
Cdd:COG5265 453 --AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1447 NLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRM 1505
Cdd:COG5265 531 RAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
993-1505 |
8.14e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 178.29 E-value: 8.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 993 RLMRLGVYGgLGVSQGVAVF--GYSLSVSIGGILAS--RFLHQSMLFdvlrSPMSFFERTPSGNLVNRFAKEMDTIDS-- 1066
Cdd:PRK11176 65 KWMPLVVIG-LMILRGITSFisSYCISWVSGKVVMTmrRRLFGHMMG----MPVSFFDKQSTGTLLSRITYDSEQVASss 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1067 ---LIPM------ILKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGllyffvQRFyvassRQLKRLESVSRSPIYTHFN 1137
Cdd:PRK11176 140 sgaLITVvregasIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVS------KRF-----RNISKNMQNTMGQVTTSAE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1138 ETLLGTSVIRAFG----EQERFIHESDQRVDHNQKAYYPSIVANRwlairlefVGNCIVSFAaLFAVL-------ARENL 1206
Cdd:PRK11176 209 QMLKGHKEVLIFGgqevETKRFDKVSNRMRQQGMKMVSASSISDP--------IIQLIASLA-LAFVLyaasfpsVMDTL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1207 SPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYSDTEKEA-EWRHEPPTVppdwptEGCIHITNFGLRYRS 1285
Cdd:PRK11176 280 TAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKdEGKRVIERA------KGDIEFRNVTFTYPG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1286 DLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTL 1365
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTI 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1366 RMNLD--PFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDL 1443
Cdd:PRK11176 434 ANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1444 ETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAF---YRM 1505
Cdd:PRK11176 514 ESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYaqlHKM 578
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1037-1505 |
7.86e-46 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 177.61 E-value: 7.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATP---MVAFI-IPFLGLLYFFVQR 1112
Cdd:TIGR00958 244 LLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltMVTLInLPLVFLAEKVFGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1113 FYVASSRQLKrlESVSRSpiyTHFNETLLGT-SVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCI 1191
Cdd:TIGR00958 324 RYQLLSEELQ--EAVAKA---NQVAEEALSGmRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLI 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1192 ---VSFAALFAVLAREnLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYSDtekeaewrhEPPTVPPD- 1267
Cdd:TIGR00958 399 qvlVLYYGGQLVLTGK-VSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLD---------RKPNIPLTg 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1268 ----WPTEGCIHITNFGLRYRSDLDLAI-RNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKL 1342
Cdd:TIGR00958 469 tlapLNLEGLIEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1343 GLHELRSRITIIPQDPVLFSGTLRMNLD-PFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCL 1421
Cdd:TIGR00958 549 DHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAI 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1422 ARALLRKTKVLVLDEATAAVDLETDNLIQSTirSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGA 1501
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
....
gi 1357684105 1502 FYRM 1505
Cdd:TIGR00958 707 YKHL 710
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1274-1505 |
2.43e-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: 161.11 E-value: 2.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPVLFSGTLRMNLDPFDSYSD-EDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVL 1432
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1433 VLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRM 1505
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
357-839 |
1.30e-41 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 161.69 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 357 DAPPWQG-YFYTALLFVCTCVQSLILQRYFHVCFVSGMR----LRTAVIGAVYR---KALVISSAARRTSTVGEIVNLMS 428
Cdd:TIGR02857 36 AGEPLAElLPALGALALVLLLRALLGWLQERAAARAAAAvksqLRERLLEAVAAlgpRWLQGRPSGELATLALEGVEALD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 429 VDAQRFmdLVTYINMIwSAPLQVVLALYFLwenlgpSVLAGVAVMI--LMVPV-NAVIAMKTKTYQVAQMKNKDSRIKLM 505
Cdd:TIGR02857 116 GYFARY--LPQLVLAV-IVPLAILAAVFPQ------DWISGLILLLtaPLIPIfMILIGWAAQAAARKQWAALSRLSGHF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 506 NEMLNGIKVLKLYAWEMAFRDKVSQI----RENELQVLKkAAYLgavSTFTwvcAPFLVALST--FSVYV-LSNDQNVLD 578
Cdd:TIGR02857 187 LDRLRGLPTLKLFGRAKAQAAAIRRSseeyRERTMRVLR-IAFL---SSAV---LELFATLSValVAVYIgFRLLAGDLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 579 AQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRLRVFLSHEElQEDSVEHPAAGCSAYSISIEDGVFSWsRSESPT 658
Cdd:TIGR02857 260 LATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAP-RPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNII 725
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 726 FGQK-RKESWYQRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHI 804
Cdd:TIGR02857 418 LARPdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
490 500 510
....*....|....*....|....*....|....*
gi 1357684105 805 FDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVM 839
Cdd:TIGR02857 498 LEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1031-1507 |
1.44e-41 |
|
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: 164.36 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1031 QSMLFD-VLRSPMSFFERTPSGNLVNRfAKEMDTIDSLIP-MILKMFMGSLFNVLG-------SCVIILVATPMVAF--- 1098
Cdd:TIGR03797 212 QAAVWDrLLRLPVSFFRQYSTGDLASR-AMGISQIRRILSgSTLTTLLSGIFALLNlglmfyySWKLALVAVALALVaia 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1099 IIPFLGLLyffvQRFYVassRQLKRLESVSRSPIYTHFNetllGTSVIRAFGEQERFIHesdqrvdhnqkAYYPSIVANR 1178
Cdd:TIGR03797 291 VTLVLGLL----QVRKE---RRLLELSGKISGLTVQLIN----GISKLRVAGAENRAFA-----------RWAKLFSRQR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1179 WLAIRLEFVGNCIVSF---------AALFAV----LARENLSPGIMgLSISYAL-QLTASLTWLVRMSSDVETNIVAVER 1244
Cdd:TIGR03797 349 KLELSAQRIENLLTVFnavlpvltsAALFAAaislLGGAGLSLGSF-LAFNTAFgSFSGAVTQLSNTLISILAVIPLWER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1245 VKEYSDTEKEAEWRheppTVPPDwPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRI 1324
Cdd:TIGR03797 428 AKPILEALPEVDEA----KTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1325 I----EPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKL 1400
Cdd:TIGR03797 499 LlgfeTPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGM 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1401 SHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLI-QSTIRSQfedCTVLTIAHRLNTIMDYTRVL 1479
Cdd:TIGR03797 579 HTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVsESLERLK---VTRIVIAHRLSTIRNADRIY 655
|
490 500
....*....|....*....|....*...
gi 1357684105 1480 VLDKGQMAEFDSPSSLIAQKGAFYRMAK 1507
Cdd:TIGR03797 656 VLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1011-1505 |
6.49e-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: 162.60 E-value: 6.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1011 VFGYSLSVSIggILAsrFLHQsmLFDVlrsPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMF-------MGSLFNVL 1083
Cdd:TIGR01193 222 VLGQRLSIDI--ILS--YIKH--LFEL---PMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFldmwilvIVGLFLVR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1084 GSC---VIILVATPMVAFIIpflgllYFFVQRFYVASSRQLKRLESVSRSPIythfnETLLGTSVIRAFG-EQERFIHES 1159
Cdd:TIGR01193 293 QNMllfLLSLLSIPVYAVII------ILFKRTFNKLNHDAMQANAVLNSSII-----EDLNGIETIKSLTsEAERYSKID 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1160 DQRVDHNQKAYYPSIVANRWLAIR--LEFVGNCIVSFAALFAVLaRENLSpgiMGLSISYALQLTASLTWL---VRMSSD 1234
Cdd:TIGR01193 362 SEFGDYLNKSFKYQKADQGQQAIKavTKLILNVVILWTGAYLVM-RGKLT---LGQLITFNALLSYFLTPLeniINLQPK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1235 VETNIVAVERVKEYSDTEKEAEWRHEPPTVPPdwpTEGCIHITNFGLRYRSDlDLAIRNINVDISGGEKVGIVGRTGAGK 1314
Cdd:TIGR01193 438 LQAARVANNRLNEVYLVDSEFINKKKRTELNN---LNGDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1315 SSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL--DPFDSYSDEDIWKALEFSHLKTF 1392
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1393 VSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSqFEDCTVLTIAHRLNTI 1472
Cdd:TIGR01193 594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVA 672
|
490 500 510
....*....|....*....|....*....|...
gi 1357684105 1473 MDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRM 1505
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
642-862 |
4.21e-40 |
|
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: 148.92 E-value: 4.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQNATLKNNIIFGqKRKESWYQ--RVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSV 786
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYG-RPGATREEveEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 787 YLLDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAE 862
Cdd:cd03251 160 LILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
642-862 |
4.81e-40 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 148.53 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSrSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQNATLKNNIIFGqkRKESWYQRVVEACALQQDLDI---LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRS 785
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYG--RPDATDEEVIEAAKAAQIHDKimrFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 786 VYLLDDPLSAVDAHVGKHIFDQVIgpqGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAE 862
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALR---DVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
325-596 |
1.72e-39 |
|
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: 148.56 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 325 FLVSCLYKFIQDILMFAGPEILRLLIKFVNDPDAPPWQ-GYFYTALLFVCTCVQSLILQRYFHVCFVSGMRLRTAVIGAV 403
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 404 YRKALVISSAARRTSTVGEIVNLMSVDAQRFMDLVTYINMIWSAPLQVVLALYFLWENLGPSV-LAGVAVMILMVPVNAV 482
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 483 IAMKTKTYQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMAFRDKVSQIRENELQV-LKKAAYLGAVSTFTWVCAPFLVA 561
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1357684105 562 LSTFSVYVLSnDQNVLDAQKAFVSLALFNILRFPL 596
Cdd:pfam00664 241 LALWFGAYLV-ISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
642-843 |
2.73e-39 |
|
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: 144.06 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQNATLKNNIifgqkrkeswyqrvveacalqqdldilpagdeteigekgvnLSGGQKQRVSLARAVYCDRSVYL 788
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 789 LDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGE 843
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
997-1512 |
3.01e-39 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 155.89 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 997 LGVYGGLGVSQGVAvfgySLSVSIGgilASRFLH---QSMLFD----VLRSPMSFFERTPSGNLVnrfaKEM-DTIDSLI 1068
Cdd:PRK13657 59 LAAWAGFGLFNIIA----GVLVARH---ADRLAHrrrLAVLTEyferIIQLPLAWHSQRGSGRAL----HTLlRGTDALF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1069 PMILKMFMGSLFNVLGSCVIILVATPM---VAFIIPFLGLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSV 1145
Cdd:PRK13657 128 GLWLEFMREHLATLVALVVLLPLALFMnwrLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1146 IRAFGEQERFIHESDQRVDHNQKAYYPsiVANRWlaiRLEFVGNCIVSFAALFAVL-------ARENLSPGIMGLSISYA 1218
Cdd:PRK13657 208 VQSYNRIEAETQALRDIADNLLAAQMP--VLSWW---ALASVLNRAASTITMLAILvlgaalvQKGQLRVGEVVAFVGFA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1219 LQLTASLTwlvRMSSDVETNIVAVERVKEYSDTEKEAEWRHEPPTVPPDWPTEGCIHITNFGLRY---RSdldlAIRNIN 1295
Cdd:PRK13657 283 TLLIGRLD---QVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYdnsRQ----GVEDVS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1296 VDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL---DPf 1372
Cdd:PRK13657 356 FEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRP- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1373 dSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQST 1452
Cdd:PRK13657 435 -DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1453 IRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRMAKDAGLI 1512
Cdd:PRK13657 514 LDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGML 573
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
642-858 |
4.10e-39 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 145.83 E-value: 4.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWsRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:cd03254 3 IEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQNATLKNNIIFGqkRKESWYQRVVEACALQQDLDI---LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRS 785
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLG--RPNATDEEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 786 VYLLDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEG 858
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
641-844 |
1.50e-38 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 143.88 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 641 SISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVA 707
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 708 YVPQQAWIQNATLKNNIIFGqkRKESWYQRVVEAC---ALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDR 784
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLG--APLADDERILRAAelaGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEI 844
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1034-1469 |
3.35e-38 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 151.36 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFDVL-RSPMSFFERTPSGNLVNRFAKEMDTIDSLI-----PMILKMFMGSLFnVLGSCVI------ILVATPMVA-FII 1100
Cdd:TIGR02868 92 VYERLaRQALAGRRRLRRGDLLGRLGADVDALQDLYvrvivPAGVALVVGAAA-VAAIAVLsvpaalILAAGLLLAgFVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1101 PFLGLLyffvqrfyvaSSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESdQRVDHnqkayypsivanRWL 1180
Cdd:TIGR02868 171 PLVSLR----------AARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQV-EEADR------------ELT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1181 AI-----RLEFVGNCIVSFAALFAVL----------ARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:TIGR02868 228 RAerraaAATALGAALTLLAAGLAVLgalwaggpavADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1246 KEYSDTE---KEAEwRHEPPTVPPDWPTegcihITNFGLRYRSDLD-LAIRNINVDISGGEKVGIVGRTGAGKSSLTLGL 1321
Cdd:TIGR02868 308 VEVLDAAgpvAEGS-APAAGAVGLGKPT-----LELRDLSAGYPGApPVLDGVSLDLPPGERVAILGPSGSGKSTLLATL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1322 FRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL---DPfdSYSDEDIWKALEFSHLKTFVSGLPD 1398
Cdd:TIGR02868 382 AGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLRALPD 459
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1399 KLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRL 1469
Cdd:TIGR02868 460 GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
619-865 |
9.68e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.07 E-value: 9.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 619 FLSHEELQEDSVEHPAAGCSAYSISIEDGVFSwSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMdKMEG 698
Cdd:PRK11174 327 FLETPLAHPQQGEKELASNDPVTIEAEDLEIL-SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 699 SVAVKG------SVAYVPQQ-AWI-QN-----ATLKNNIIFGQKR-KESWYQRVVEACALQQDLDILPAGDETEIGEKGV 764
Cdd:PRK11174 405 SLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNPDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAA 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 765 NLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFdqvigpQGLLK---DKTRILVTHGLSYLPQADLVLVMVD 841
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM------QALNAasrRQTTLMVTHQLEDLAQWDQIWVMQD 558
|
250 260
....*....|....*....|....
gi 1357684105 842 GEITEIGSYLQLKEEEGAFAEFLR 865
Cdd:PRK11174 559 GQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
642-865 |
2.23e-36 |
|
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: 138.06 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSW-SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-------------VA 707
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 708 YVPQQAWIQNATLKNNIIFGQKRKESwyQRVVEACALQQDLDI---LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDR 784
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFimsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHI---FDQVIgpqgllKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFA 861
Cdd:cd03249 159 KILLLDEATSALDAESEKLVqeaLDRAM------KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
....
gi 1357684105 862 EFLR 865
Cdd:cd03249 233 KLVK 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1254-1481 |
4.25e-36 |
|
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: 145.12 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1254 EAEWRHEPPTVPPDWPTEGCIHITNFGLRYRsDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQIS 1333
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1334 IDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDPFDSY-SDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLS 1412
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1413 VGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVL 1481
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1293-1505 |
1.98e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 144.22 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1293 NINVDISGGEKVGIVGRTGAGKSSLT---LGLFriiePAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL 1369
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLnalLGFL----PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 ---DPfdSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETD 1446
Cdd:PRK11174 444 llgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1447 NLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGAFYRM 1505
Cdd:PRK11174 522 QLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1279-1486 |
2.48e-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: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1279 FGLRYRSDLdLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDP 1358
Cdd:cd03248 19 FAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1359 VLFSGTLRMNLD-PFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEA 1437
Cdd:cd03248 98 VLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1357684105 1438 TAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQM 1486
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
642-865 |
1.73e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 138.23 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQNATLKNNIIFGQKRKESWYQrVVEACALQQDLDI---LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRS 785
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYARTEQYSREQ-IEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 786 VYLLDDPLSAVDAHVGKHI---FDQvigpqgLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAE 862
Cdd:PRK11176 501 ILILDEATSALDTESERAIqaaLDE------LQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
...
gi 1357684105 863 FLR 865
Cdd:PRK11176 575 LHK 577
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
383-827 |
4.29e-33 |
|
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: 135.95 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 383 RYF------HVCFVSGMRLRTAVIGAVYRKALVISSAARRTSTVGEIVNlmSVDAQRFMDLVTYINMIWSAPL---QVVL 453
Cdd:TIGR02868 70 RYLerlvghDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGA--DVDALQDLYVRVIVPAGVALVVgaaAVAA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 454 ALYFLWEnLGPSVLAGVAVMILMVPVNAVIAMKTKTYQVAQMKNKDSRiKLMnEMLNGIKVLKLYAWEMAFRDKVSQIRE 533
Cdd:TIGR02868 148 IAVLSVP-AALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAA-QLT-DALDGAAELVASGALPAALAQVEEADR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 534 NELQVLKKAAYLGAVSTftwvCAPFLVA-LSTFSVYVLSNDQnVLDAQKAFVSLALFNILRFPL----NMLPMVISSMVQ 608
Cdd:TIGR02868 225 ELTRAERRAAAATALGA----ALTLLAAgLAVLGALWAGGPA-VADGRLAPVTLAVLVLLPLAAfeafAALPAAAQQLTR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 609 ASVSLKRLrvflshEELQEDS-----VEHPAAGCSA---YSISIEDGVFSWSRSEsPTLKRLNVRVPEGSLVAVVGHVGS 680
Cdd:TIGR02868 300 VRAAAERI------VEVLDAAgpvaeGSAPAAGAVGlgkPTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 681 GKSSLLSALLGEMDKMEGSVAVKGS-------------VAYVPQQAWIQNATLKNNIIFGQKR---KESWyqRVVEACAL 744
Cdd:TIGR02868 373 GKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARPDatdEELW--AALERVGL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 745 QQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPqglLKDKTRILVT 824
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLIT 527
|
...
gi 1357684105 825 HGL 827
Cdd:TIGR02868 528 HHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
417-862 |
2.28e-32 |
|
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: 136.02 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 417 TSTVGEIVNlmsvdaqRFMDLVTYINMIWSAPLQVVLALYFLwenLGPSVLAGVAVMILM------VPVNAVI------- 483
Cdd:TIGR01193 249 TRRTGEIVS-------RFTDASSIIDALASTILSLFLDMWIL---VIVGLFLVRQNMLLFllsllsIPVYAVIiilfkrt 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 484 --AMKTKTYQVAQMKNkdSRIKlmnEMLNGIKVLKLYAWEMAFRDKVSQIRENELQ---VLKKAAYL-GAVSTFTWVcap 557
Cdd:TIGR01193 319 fnKLNHDAMQANAVLN--SSII---EDLNGIETIKSLTSEAERYSKIDSEFGDYLNksfKYQKADQGqQAIKAVTKL--- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 558 flvalsTFSVYVL-SNDQNVLDAQKAFVSLALFN-ILRFPLNMLPMVIS---SMVQASVSLKRL-RVFLSHEELqEDSVE 631
Cdd:TIGR01193 391 ------ILNVVILwTGAYLVMRGKLTLGQLITFNaLLSYFLTPLENIINlqpKLQAARVANNRLnEVYLVDSEF-INKKK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 632 HPAAGCSAYSISIEDGVFSWSRSeSPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV----------- 700
Cdd:TIGR01193 464 RTELNNLNGDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfslkdid 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 701 --AVKGSVAYVPQQAWIQNATLKNNIIFGQKRKESwYQRVVEACAL---QQDLDILPAGDETEIGEKGVNLSGGQKQRVS 775
Cdd:TIGR01193 543 rhTLRQFINYLPQEPYIFSGSILENLLLGAKENVS-QDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIA 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 776 LARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGpqglLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKE 855
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
....*..
gi 1357684105 856 EEGAFAE 862
Cdd:TIGR01193 698 RNGFYAS 704
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
610-865 |
3.17e-32 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 134.07 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 610 SVSLKRLRVFLSHEELQEDSVEHPAAGCSAYSISIEDgvFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL 689
Cdd:PRK10789 284 SAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQ--FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 690 LGEMDKMEGSV-------------AVKGSVAYVPQQAWIQNATLKNNIIFGqkRKESWYQRVVEACAL---QQDLDILPA 753
Cdd:PRK10789 362 QRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIALG--RPDATQQEIEHVARLasvHDDILRLPQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 754 GDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQA 833
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL---RQWGEGRTVIISAHRLSALTEA 516
|
250 260 270
....*....|....*....|....*....|..
gi 1357684105 834 DLVLVMVDGEITEIGSYLQLKEEEGAFAEFLR 865
Cdd:PRK10789 517 SEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
605-848 |
4.58e-32 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 133.33 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 605 SMVQASVSLKRLRVFLSHEELQEDSVEHPAAgcsAYSISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSS 684
Cdd:COG4618 297 QFVSARQAYRRLNELLAAVPAEPERMPLPRP---KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKST 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 685 LLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNII-FGQKRKEswyqRVVEACALQQ--DL 748
Cdd:COG4618 374 LARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAENIArFGDADPE----KVVAAAKLAGvhEM 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 749 dI--LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAhvgkhifdqvIGPQGL------LKD--K 818
Cdd:COG4618 450 -IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD----------EGEAALaaairaLKArgA 518
|
250 260 270
....*....|....*....|....*....|
gi 1357684105 819 TRILVTHGLSYLPQADLVLVMVDGEITEIG 848
Cdd:COG4618 519 TVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
641-849 |
4.98e-31 |
|
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: 122.22 E-value: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 641 SISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVA 707
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 708 YVPQQAWIQNATLKNNI-IFGQKR-KESWyqRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRS 785
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSdEELW--QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 786 VYLLDDPLSAVDAHVGKHIFdQVIgpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGS 849
Cdd:cd03244 160 ILVLDEATASVDPETDALIQ-KTI--REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1274-1499 |
7.17e-31 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 122.06 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDlDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPV--LFSGTLR-------MNLDpfdsYSDEDIWK----ALEFSHLktfvSGLPDKLSHEcseggenLSVGQRQLLC 1420
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENLG----LPREEIRErveeALELVGL----EHLADRPPHE-------LSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1421 LARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREVFSD 224
|
.
gi 1357684105 1499 K 1499
Cdd:COG1122 225 Y 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1239-1505 |
1.54e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.79 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1239 IVAVERVKEYSDTEKEAEWrhepPTVPPDWPTEGCIHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLT 1318
Cdd:PRK11160 308 IASARRINEITEQKPEVTF----PTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1319 LGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL---DPfdSYSDEDIWKALEFSHLKTFVSG 1395
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1396 lPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTI--M 1473
Cdd:PRK11160 462 -DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqF 540
|
250 260 270
....*....|....*....|....*....|..
gi 1357684105 1474 DytRVLVLDKGQMAEFDSPSSLIAQKGAFYRM 1505
Cdd:PRK11160 541 D--RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
394-861 |
3.38e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.99 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 394 RLRTAVIGAVYRKAL----------VISSAARRTSTVGEIVNLMSVDAQRF--MDLVTYINMIWSAPLQVVLALYFLwen 461
Cdd:TIGR00958 235 RIREDLFRSLLRQDLgffdenktgeLTSRLSSDTQTMSRSLSLNVNVLLRNlvMLLGLLGFMLWLSPRLTMVTLINL--- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 462 lgPSVLA-----GVAVMILMVPVNAVIAmktKTYQVAQmknkdsriklmnEMLNGIKVLKLYAWE----MAFRDKVSQIR 532
Cdd:TIGR00958 312 --PLVFLaekvfGKRYQLLSEELQEAVA---KANQVAE------------EALSGMRTVRSFAAEegeaSRFKEALEETL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 533 enelQVLKKAAYlgAVSTFTW---VCAPFLValstfsVYVLS-NDQNVLDAQKAFVSLALFNILRFPLN----MLPMVIS 604
Cdd:TIGR00958 375 ----QLNKRKAL--AYAGYLWttsVLGMLIQ------VLVLYyGGQLVLTGKVSSGNLVSFLLYQEQLGeavrVLSYVYS 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 605 SMVQASVSLKRLRVFLSheelQEDSVEHPaaGCSAYS-----ISIEDGVFSW-SRSESPTLKRLNVRVPEGSLVAVVGHV 678
Cdd:TIGR00958 443 GMMQAVGASEKVFEYLD----RKPNIPLT--GTLAPLnleglIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 679 GSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNIIFGQKRKE-SWYQRVVEACAL 744
Cdd:TIGR00958 517 GSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENIAYGLTDTPdEEIMAAAKAANA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 745 QQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVgkhifDQVIGPQGLLKDKTRILVT 824
Cdd:TIGR00958 597 HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRASRTVLLIA 671
|
490 500 510
....*....|....*....|....*....|....*..
gi 1357684105 825 HGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFA 861
Cdd:TIGR00958 672 HRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1276-1485 |
5.22e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 116.03 E-value: 5.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1276 ITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIP 1355
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1356 QDP------------VLFSgtLRmNLdpfdSYSDEDIWKALEFShLKTFvsGLPDKLSHECSEggenLSVGQRQLLCLAR 1423
Cdd:cd03225 82 QNPddqffgptveeeVAFG--LE-NL----GLPEEEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1424 ALLRKTKVLVLDEATAAVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQ 1485
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1023-1245 |
3.59e-28 |
|
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: 117.21 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1023 ILASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFIIPF 1102
Cdd:cd18600 99 ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1103 LGLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAI 1182
Cdd:cd18600 179 VIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 258
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1183 RLEFVGNCIVSFAALFAVLARENlSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18600 259 RIEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
595-862 |
5.87e-28 |
|
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: 121.08 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 595 PLNMLPMVISSMVQASVSLKRLRVFLS-HEELQeDSVEHPAAGCSAYSISIEDGVFSWSrSESPTLKRLNVRVPEGSLVA 673
Cdd:COG5265 311 PLNFLGFVYREIRQALADMERMFDLLDqPPEVA-DAPDAPPLVVGGGEVRFENVSFGYD-PERPILKGVSFEVPAGKTVA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 674 VVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNIIFGqkRKESWYQRVVE 740
Cdd:COG5265 389 IVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQDTVLFNDTIAYNIAYG--RPDASEEEVEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 741 ACALQQDLDI---LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIfdqvigpQGLL-- 815
Cdd:COG5265 467 AARAAQIHDFiesLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI-------QAALre 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1357684105 816 --KDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAE 862
Cdd:COG5265 540 vaRGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
642-861 |
5.98e-28 |
|
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: 113.74 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQNATLKNNIIFGqkRKESWYQRVVEACALQQDLDI---LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRS 785
Cdd:cd03252 81 VLQENVLFNRSIRDNIALA--DPGMSMERVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 786 VYLLDDPLSAVDAHVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFA 861
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1274-1488 |
6.06e-28 |
|
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: 112.02 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGlHELRSRITI 1353
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPVLFSGTLRMNLdpfdsysdediwkalefshlktfvsglpdklshecsegGENLSVGQRQLLCLARALLRKTKVLV 1433
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1434 LDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAE 1488
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1274-1486 |
8.19e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.15 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPVLFSGTLRMNLdpfdsysdediwkalefshlktfvsglpdklshecseggenLSVGQRQLLCLARALLRKTKVLV 1433
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1434 LDEATAAVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDYTRVLVLDKGQM 1486
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
637-844 |
9.23e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 9.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 637 CSAYSISIEDGVFSWSRSesPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------SVAY 708
Cdd:COG1121 2 MMMPAIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQA---WIQNAT--------LKNNIIFGQKRKESWYQRVVEacALQQdLDILPAGDETeIGEkgvnLSGGQKQRVSLA 777
Cdd:COG1121 80 VPQRAevdWDFPITvrdvvlmgRYGRRGLFRRPSRADREAVDE--ALER-VGLEDLADRP-IGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 778 RAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKD-----KTRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRElrregKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
626-865 |
2.63e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.77 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 626 QEDSVEHPAAG---CSAYSISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAV 702
Cdd:PRK11160 320 QKPEVTFPTTStaaADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 703 KG-------------SVAYVPQQAWIQNATLKNNIIFGQKRKESwyQRVVEacALQQ-DLDILPAGDE---TEIGEKGVN 765
Cdd:PRK11160 400 NGqpiadyseaalrqAISVVSQRVHLFSATLRDNLLLAAPNASD--EALIE--VLQQvGLEKLLEDDKglnAWLGEGGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 766 LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLL----KDKTRILVTHGLSYLPQADLVLVMVD 841
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDN 548
|
250 260
....*....|....*....|....
gi 1357684105 842 GEITEIGSYLQLKEEEGAFAEFLR 865
Cdd:PRK11160 549 GQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
394-884 |
3.91e-27 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 118.67 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 394 RLRTAVIGAVYRKALvissAARRTSTVGEIVNLMSVDAQRFMDLvtYINMI----WSAPL--QVVLALYFL-WEnlgpsv 466
Cdd:PRK10790 99 QLRTDVMDAALRQPL----SAFDTQPVGQLISRVTNDTEVIRDL--YVTVVatvlRSAALigAMLVAMFSLdWR------ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 467 LAGVAVMIL-MVPVNAVIAMKTKTYQVAQMKNKDSRIKL-MNEMLNGIKVLKLYAWEMAFRDKVSQIR----ENELQVLK 540
Cdd:PRK10790 167 MALVAIMIFpAVLVVMVIYQRYSTPIVRRVRAYLADINDgFNEVINGMSVIQQFRQQARFGERMGEASrshyMARMQTLR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 541 KAAYL--GAVSTFTWVCAPFLVALSTFS------VYVLSndqnvldaqkAFVSLalFNILRFPLNMLPMVISSMVQASVS 612
Cdd:PRK10790 247 LDGFLlrPLLSLFSALILCGLLMLFGFSasgtieVGVLY----------AFISY--LGRLNEPLIELTTQQSMLQQAVVA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 613 LKRLRVFLSHEELQEDSVEHPAAGCSaysISIEDGVFSWsRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGE 692
Cdd:PRK10790 315 GERVFELMDGPRQQYGNDDRPLQSGR---IDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 693 MDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNIIFGQKRKESWYQRVVEACALQQDLDILPAGDETEI 759
Cdd:PRK10790 391 YPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 760 GEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVgkhifDQVIgPQGL--LKDKTRILV-THGLSYLPQADLV 836
Cdd:PRK10790 471 GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAI-QQALaaVREHTTLVViAHRLSTIVEADTI 544
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1357684105 837 LVMVDGEITEIGSYLQLKEEEGAFAEFLRTYASSEQTDGSEPVPNSPS 884
Cdd:PRK10790 545 LVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1291-1439 |
9.18e-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: 107.35 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSG-TLRMNL 1369
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1370 -------DPFDSYSDEDIWKALEfsHLktfvsGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATA 1439
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALE--KL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
643-828 |
2.86e-26 |
|
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: 108.39 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 643 SIEDGVFSWSRSesPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------SVAYVPQQA- 713
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 714 --WIQNATLKN--------NIIFGQKRKESWYQRVVEAcalqqdLDILPAGD--ETEIGEkgvnLSGGQKQRVSLARAVY 781
Cdd:cd03235 79 idRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEA------LERVGLSElaDRQIGE----LSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 782 CDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKD-----KTRILVTHGLS 828
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYE-------LLRElrregMTILVVTHDLG 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
652-1482 |
8.93e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 116.28 E-value: 8.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 652 SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--------------VAYVPQQAWIQN 717
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskIGVVSQDPLLFS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 ATLKNNIIFG----------------------------------------------------QKRKEswYQRV------- 738
Cdd:PTZ00265 474 NSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKN--YQTIkdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 739 VEACALQQD-LDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDaHVGKHIFDQVIGPQGLLKD 817
Cdd:PTZ00265 552 VSKKVLIHDfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNEN 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 818 KTRILVTHGLSYLPQADLVLVM------------VDGE----------------------------ITEIGSYL------ 851
Cdd:PTZ00265 631 RITIIIAHRLSTIRYANTIFVLsnrergstvdvdIIGEdptkdnkennnknnkddnnnnnnnnnnkINNAGSYIieqgth 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 852 --QLKEEEGAFAEFLRTYASSEQT------DGSEPVPNSPSKPMENGVGPG-FTGSSQSASNNSKGPASELNKEEKKSKS 922
Cdd:PTZ00265 711 daLMKNKNGIYYTMINNQKVSSKKssnndnDKDSDMKSSAYKDSERGYDPDeMNGNSKHENESASNKKSCKMSDENASEN 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 923 AEAGKLT-------DADKASTG-RVKLSVFCSYLKAIGVLLSAISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPDRL 994
Cdd:PTZ00265 791 NAGGKLPflrnlfkRKPKAPNNlRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSL 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 995 MRLGVYGGLGVSQGVAVFgYSlsvSIGGILASRFLHQSMLFDVLRSPMSFFER---TPsGNLVNRFAKEMDTIDSLIPMI 1071
Cdd:PTZ00265 871 YILVIAIAMFISETLKNY-YN---NVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNN 945
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1072 LKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGLLYF--FVQRFYVASSRQLKRLESVSRSPIYTHFN------------ 1137
Cdd:PTZ00265 946 IVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMrvFAIRARLTANKDVEKKEINQPGTVFAYNSddeifkdpsfli 1025
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1138 -ETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNCIVSFAALFA--VLARENLSPGIMGLS 1214
Cdd:PTZ00265 1026 qEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGsfLIRRGTILVDDFMKS 1105
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1215 IsYALQLTASLTW-LVRMSSDVETNIVAVERV------KEYSDTEKEAEWRhepptVPPDWPTEGCIHITNFGLRYRSDL 1287
Cdd:PTZ00265 1106 L-FTFLFTGSYAGkLMSLKGDSENAKLSFEKYypliirKSNIDVRDNGGIR-----IKNKNDIKGKIEIMDVNFRYISRP 1179
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1288 DLAI-RNINVDISGGEKVGIVGRTGAGKSSLTLGLFR---------IIEPAE---------------------------- 1329
Cdd:PTZ00265 1180 NVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhIVFKNEhtndmtneqdyqgdeeqnvgmknvnefs 1259
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1330 -----------------GQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDpF--DSYSDEDIWKALEFSHLK 1390
Cdd:PTZ00265 1260 ltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FgkEDATREDVKRACKFAAID 1338
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1391 TFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHR 1468
Cdd:PTZ00265 1339 EFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHR 1418
|
1050
....*....|....
gi 1357684105 1469 LNTIMDYTRVLVLD 1482
Cdd:PTZ00265 1419 IASIKRSDKIVVFN 1432
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
659-794 |
2.09e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 103.50 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV-------------AVKGSVAYVPQQAWIQNA-TLKNNI 724
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltdderkSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 725 IFG---QKRKESWYQRVVEAcALQQdLDILPAGDETeIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:pfam00005 81 RLGlllKGLSKREKDARAEE-ALEK-LGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1274-1489 |
3.02e-25 |
|
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: 105.67 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDL--AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHEL---R 1348
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1349 SRITIIPQDPvlFSgtlrmNLDP---------------FDSYSDEDIWKALEfshLKTFVSGLP----DKLSHEcsegge 1409
Cdd:cd03257 82 KEIQMVFQDP--MS-----SLNPrmtigeqiaeplrihGKLSKKEARKEAVL---LLLVGVGLPeevlNRYPHE------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1410 nLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETD----NLIQsTIRSQFeDCTVLTIAHRLNTIMDYT-RVLVLDKG 1484
Cdd:cd03257 146 -LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLK-KLQEEL-GLTLLFITHDLGVVAKIAdRVAVMYAG 222
|
....*
gi 1357684105 1485 QMAEF 1489
Cdd:cd03257 223 KIVEE 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1280-1485 |
3.85e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 103.09 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1280 GLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQdpv 1359
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1360 lfsgtlrmnldpfdsysdediwkalefshlktfvsglpdklshecseggenLSVGQRQLLCLARALLRKTKVLVLDEATA 1439
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1357684105 1440 AVDLETDNLIQSTIRSQFED-CTVLTIAHRLNTIMDYT-RVLVLDKGQ 1485
Cdd:cd00267 110 GLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1274-1498 |
4.02e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.53 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPA---EGQISIDGVDIAKLGLHELRSR 1350
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1351 ITIIPQDP--VLFSGTLR-------MNLDPFDSYSDEDIWKALEFSHLKTFVSGLPdklsHEcseggenLSVGQRQLLCL 1421
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYP----HQ-------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1422 ARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS--QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEILAA 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
648-839 |
4.52e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.33 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 648 VFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------SVAYVPQQA----Wi 715
Cdd:COG1116 16 RFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPallpW- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 716 qnATLKNNIIFGQK----RKESWYQRVVEACA---LQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYL 788
Cdd:COG1116 95 --LTVLDNVALGLElrgvPKAERRERARELLElvgLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 789 LDDPLSAVDAHVGKHIfdqvigpQGLL------KDKTRILVTHGLS---YLpqADLVLVM 839
Cdd:COG1116 162 MDEPFGALDALTRERL-------QDELlrlwqeTGKTVLFVTHDVDeavFL--ADRVVVL 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
643-843 |
5.07e-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: 104.47 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 643 SIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYV 709
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 710 PQQAWIQ--NATLKNNIIFG---QKRKESWYQRVVEACALQQDLDILpagDETEIGEkgvnLSGGQKQRVSLARAVYCDR 784
Cdd:cd03225 81 FQNPDDQffGPTVEEEVAFGlenLGLPEEEIEERVEEALELVGLEGL---RDRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKD-----KTRILVTHGLSYL-PQADLVLVMVDGE 843
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLE-------LLKKlkaegKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1291-1489 |
6.37e-25 |
|
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: 111.29 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLD 1370
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1371 PFDSYSD-EDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDN-L 1448
Cdd:TIGR01842 414 RFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQaL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1357684105 1449 IQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEF 1489
Cdd:TIGR01842 494 ANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1290-1504 |
1.41e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 110.19 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL 1369
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 ---DPfdSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETD 1446
Cdd:PRK10789 410 algRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1447 NLIQSTIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGaFYR 1504
Cdd:PRK10789 488 HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG-WYR 544
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
642-844 |
1.70e-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: 101.91 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGsvayVPQQAWiqnatlk 721
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQW------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 nniifgqkRKESWYQRVveaCALQQDlDILPAGDETEigekgvN-LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDaHV 800
Cdd:cd03246 70 --------DPNELGDHV---GYLPQD-DELFSGSIAE------NiLSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1357684105 801 GKHIFDQVIgpQGL-LKDKTRILVTHGLSYLPQADLVLVMVDGEI 844
Cdd:cd03246 131 GERALNQAI--AALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
649-848 |
2.58e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.60 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 649 FSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------SVAYVPQQ-AWIQ 716
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 NATLKNNIIFGQKR----KESWYQRVVEACALqqdldilpAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:cd03259 86 HLTVAENIAFGLKLrgvpKAEIRARVRELLEL--------VGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 793 LSAVDAHVGKHIFDQVigpQGLLK--DKTRILVTHGLS-YLPQADLVLVMVDGEITEIG 848
Cdd:cd03259 158 LSALDAKLREELREEL---KELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
582-866 |
3.60e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 109.28 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 582 AFVSLALFNILRfplnmLPMVISSMVQASVSLKRLRVFLSHEELQEDSVEHPAAGCSAY---SISIEDGVFSWSRSeSPT 658
Cdd:PRK13657 277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRvkgAVEFDDVSFSYDNS-RQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNII 725
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 726 FGqkRKESWYQRVVEACALQQDLDIL---PAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGK 802
Cdd:PRK13657 431 VG--RPDATDEEMRAAAERAQAHDFIerkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 803 HIFDQVigpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFLRT 866
Cdd:PRK13657 509 KVKAAL---DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
642-848 |
7.25e-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: 100.08 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS------------VAYV 709
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 710 PQQAWIQNATLKNNIifgqkrkeswyqrvveacalqqdldilpagdeteigekGVNLSGGQKQRVSLARAVYCDRSVYLL 789
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 790 DDPLSAVDAHVGKHIFDQVIgpqGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIG 848
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
645-844 |
1.19e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 101.01 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 645 EDGVFSW-SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-------------VAYVP 710
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 711 QQAWIQNATLKNNIIFGQKRKEswYQRVVEACALQQDLDI---LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVY 787
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCS--FECVKEAAQKAHAHSFiseLASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 788 LLDDPLSAVDAHvGKHIFDQVIgpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEI 844
Cdd:cd03248 173 ILDEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
655-844 |
2.59e-23 |
|
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: 99.87 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSaLLGEMDK-MEGSVAVKG-----------------SVAYVPQQ-AWI 715
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRpTSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 716 QNATLKNNI----IFGQKRKESWYQRVVEACA---LQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYL 788
Cdd:cd03255 95 PDLTALENVelplLLAGVPKKERRERAEELLErvgLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 789 LDDPLSAVDAHVGKHIFDqvigpqgLLKD------KTRILVTHGLSYLPQADLVLVMVDGEI 844
Cdd:cd03255 164 ADEPTGNLDSETGKEVME-------LLRElnkeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1274-1507 |
3.22e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.22 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDP------------VLFsGTLRMNLDPfdsysdEDIWKALEFSHLKTfvsGLPDKLSHEcsegGENLSVGQRQLLCL 1421
Cdd:PRK13632 88 IFQNPdnqfigatveddIAF-GLENKKVPP------KKMKDIIDDLAKKV---GMEDYLDKE----PQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1422 ARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS--QFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
....*...
gi 1357684105 1500 gAFYRMAK 1507
Cdd:PRK13632 234 -EILEKAK 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
642-853 |
4.17e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 105.37 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMD---KMEGSVAVKG-------------S 705
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGrdllelsealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 706 VAYVPQQAWIQ--NATLKNNIIFG----QKRKESWYQRVVEACALqqdldilpAGDETEIGEKGVNLSGGQKQRVSLARA 779
Cdd:COG1123 85 IGMVFQDPMTQlnPVTVGDQIAEAlenlGLSRAEARARVLELLEA--------VGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 780 VYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPQGLLkDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGSYLQL 853
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRER-GTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEI 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
642-844 |
4.43e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 98.73 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDgvFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:COG4619 1 LELEG--LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQ-AWIQNaTLKNNIIFGQKRKESWYQRVVEACALQQ---DLDILpagdETEIGEkgvnLSGGQKQRVSLARAVYCDR 784
Cdd:COG4619 79 VPQEpALWGG-TVRDNLPFPFQLRERKFDRERALELLERlglPPDIL----DKPVER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 785 SVYLLDDPLSAVDAHvGKHIFDQVIgpQGLLKDKTR--ILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:COG4619 150 DVLLLDEPTSALDPE-NTRRVEELL--REYLAEEGRavLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
659-839 |
9.55e-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: 98.31 E-value: 9.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------SVAYVPQQA----WiqnATLKNNIIF 726
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 727 GQK----RKESWYQRV---VEACALQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAH 799
Cdd:cd03293 97 GLElqgvPKAEARERAeelLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1357684105 800 VGKHIfdqvigpQGLLKD------KTRILVTHGLS---YLpqADLVLVM 839
Cdd:cd03293 166 TREQL-------QEELLDiwretgKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1274-1494 |
3.06e-22 |
|
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: 97.25 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDlDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG---LHELRSR 1350
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1351 ITIIPQDP-----------VLfSGTL-RMNLDP--FDSYSDEDIWKALEFshLKTFvsGLPDKLSHECSEggenLSVGQR 1416
Cdd:cd03256 80 IGMIFQQFnlierlsvlenVL-SGRLgRRSTWRslFGLFPKEEKQRALAA--LERV--GLLDKAYQRADQ----LSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1417 QLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS--QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAeFDSPS 1493
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYAdRIVGLKDGRIV-FDGPP 229
|
.
gi 1357684105 1494 S 1494
Cdd:cd03256 230 A 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
658-848 |
4.02e-22 |
|
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: 96.17 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 658 TLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------SVAYVPQQ-AWIQNATLKNNII 725
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 726 FGQK----RKESWYQRVVEACALqqdLDIlpagdETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVG 801
Cdd:cd03301 95 FGLKlrkvPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1357684105 802 KHIFDQVIGPQGLLKdKTRILVTHG-LSYLPQADLVLVMVDGEITEIG 848
Cdd:cd03301 167 VQMRAELKRLQQRLG-TTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1274-1496 |
5.03e-22 |
|
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: 97.04 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPVL-FSGTLR----M----NLDPFDSYSDED---IWKALEfshlKTFVSGLPDKLSHEcseggenLSVGQRQLLCL 1421
Cdd:COG1120 80 VPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALE----RTGLEHLADRPVDE-------LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1422 ARALLRKTKVLVLDEATAAVDL----ETDNLIQSTIRSQfeDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLI 1496
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
642-849 |
8.14e-22 |
|
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: 95.86 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRsESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQ--NATLKNNIIFG-----QKRKESWyQRVVEACALqqdLDIlpagdeTEIGEKGV-NLSGGQKQRVSLARAV 780
Cdd:COG1122 80 VFQNPDDQlfAPTVEEDVAFGpenlgLPREEIR-ERVEEALEL---VGL------EHLADRPPhELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 781 YCDRSVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKD-KTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELL---KRLNKEgKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
659-865 |
8.68e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.90 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV------------AVKGSVAYVPQQAWI-QNATLKNNI- 724
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvardpaEVRRRIGYVPQEPALyPDLTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 ----IFGQKRKESWyQRVVEACALqqdLDILPAGDEteigeKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAhV 800
Cdd:COG1131 96 ffarLYGLPRKEAR-ERIDELLEL---FGLTDAADR-----KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-E 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 801 GKHIFDQVIgpQGLLKD-KTRILVTHglsYLPQA----DLVLVMVDGEITEIGSYLQLKEE--EGAFAEFLR 865
Cdd:COG1131 166 ARRELWELL--RELAAEgKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKARllEDVFLELTG 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
642-846 |
2.36e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.34 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPT--LKRLNVRVPEGSLVAVVGHVGSGKSSLLSaLLGEMDKM-EGSVAVKG-------------- 704
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 705 ---SVAYVPQQA-WIQNATLKNNI-----IFGQKRKESwYQRVVEACA---LQQDLDILPAgdeteigekgvNLSGGQKQ 772
Cdd:COG1136 84 rrrHIGFVFQFFnLLPELTALENValpllLAGVSRKER-RERARELLErvgLGDRLDHRPS-----------QLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 773 RVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKD------KTRILVTHGLSYLPQADLVLVMVDGEITE 846
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRElnrelgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
659-849 |
2.51e-21 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 94.17 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL-----LGEMDKMEGSVAVKGS---------------VAYVPQQAWIQNA 718
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIFGQK----RKESWYQRVVEACALQQDLDilpagDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:cd03260 96 SIYDNVAYGLRlhgiKLKEELDERVEEALRKAALW-----DEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 795 AVDAhVGKHIFDQVIgpQGLLKDKTRILVTHGlsyLPQA----DLVLVMVDGEITEIGS 849
Cdd:cd03260 171 ALDP-ISTAKIEELI--AELKKEYTIVIVTHN---MQQAarvaDRTAFLLNGRLVEFGP 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
649-848 |
3.21e-21 |
|
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: 94.11 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 649 FSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------------SVAYVPQQ 712
Cdd:cd03257 11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 713 A-----------WIQNATLKnniIFGQKRKESWYQRVVEACALQ-----QDLDILPAGdeteigekgvnLSGGQKQRVSL 776
Cdd:cd03257 91 PmsslnprmtigEQIAEPLR---IHGKLSKKEARKEAVLLLLVGvglpeEVLNRYPHE-----------LSGGQRQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 777 ARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKD------KTRILVTHGLS---YLpqADLVLVMVDGEITEI 847
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILD-------LLKKlqeelgLTLLFITHDLGvvaKI--ADRVAVMYAGKIVEE 227
|
.
gi 1357684105 848 G 848
Cdd:cd03257 228 G 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1290-1498 |
3.31e-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: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG---LHELRSRITIIPQDPV--LFSgt 1364
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNP-- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 lRMN--------LDPFDSYSDEDIWK----ALEFSHLKTfvsGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKVL 1432
Cdd:COG1123 358 -RMTvgdiiaepLRLHGLLSRAERRErvaeLLERVGLPP---DLADRYPHE-------LSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1433 VLDEATAAVDLetdnLIQSTIRSQFED------CTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:COG1123 427 ILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIAdRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1275-1484 |
3.74e-21 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 93.37 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1275 HITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLT---LGLfriIEPAEGQISIDGVDIAKlglheLRSRI 1351
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLkaiLGL---LKPTSGSIRVFGKPLEK-----ERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1352 TIIPQ----D---PVLFSGTLRMNLDP----FDSYSDEDIWKALEFshLKtFVsGLPDKLSHECSEggenLSVGQRQLLC 1420
Cdd:cd03235 71 GYVPQrrsiDrdfPISVRDVVLMGLYGhkglFRRLSKADKAKVDEA--LE-RV-GLSELADRQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1421 LARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDYT-RVLVLDKG 1484
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1290-1498 |
4.81e-21 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 93.80 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtLGLFRIIE-PAEGQISIDGVDIAKL---GLHELRSRITIIPQDPVLFSG-T 1364
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 LRMNLD-PF--DSYSDEDIWKALEfsHLKTFVsGLPDKLSHECSeggeNLSVGQRQLLCLARALLRKTKVLVLDEATAAV 1441
Cdd:cd03258 99 VFENVAlPLeiAGVPKAEIEERVL--ELLELV-GLEDKADAYPA----QLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1442 DLE-TDNLIQ--STIRSQFeDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:cd03258 172 DPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1276-1486 |
6.14e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 91.73 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1276 ITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIP 1355
Cdd:cd03214 2 VENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1356 QdpVLfsgtlrmnldpfdsysdediwKALEFSHLKtfvsglpDKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVLD 1435
Cdd:cd03214 80 Q--AL---------------------ELLGLAHLA-------DRPFNE-------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1436 EATAAVDL----ETDNLIQSTIRSqfEDCTVLTIAHRLNTIMDY-TRVLVLDKGQM 1486
Cdd:cd03214 123 EPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
657-839 |
1.28e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--SVAYVPQQ---AWIQNATLKNNIIFGQKRK 731
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 732 ESWYQR-------VVEACALQQDLDILpagDETEIGEkgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHI 804
Cdd:NF040873 86 RGLWRRltrddraAVDDALERVGLADL---AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1357684105 805 FDqvigpqgLLKDKTR-----ILVTHGLSYLPQADLVLVM 839
Cdd:NF040873 159 IA-------LLAEEHArgatvVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
643-843 |
1.96e-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: 89.61 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 643 SIEDGVFSWSrsESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAyvpqqAWIQNATLKN 722
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-----AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 723 NIIFgqkrkeswyqrvveacaLQQdldilpagdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHvGK 802
Cdd:cd00267 74 RIGY-----------------VPQ-------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1357684105 803 HIFDQVIgpQGLLKD-KTRILVTHGLSYLPQA-DLVLVMVDGE 843
Cdd:cd00267 117 ERLLELL--RELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
650-848 |
3.61e-20 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 89.42 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 650 SWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-------------VAYVPQqawiq 716
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 natlknniifgqkrkeswyqrvveacALQQdLDIlpagdeTEIGEKGVN-LSGGQKQRVSLARAVYCDRSVYLLDDPLSA 795
Cdd:cd03214 81 --------------------------ALEL-LGL------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 796 VDAHVGKHIFDqvigpqgLLKD------KTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:cd03214 128 LDIAHQIELLE-------LLRRlarergKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
642-857 |
5.18e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.59 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSS---LLSALL----GEMdKMEGSVAVKGSVAYVPQQAW 714
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsGEI-KIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 I--QN-------ATLKNNIIFG-----QKRKESWyqRVVEACALQqdldilpAGDETEIGEKGVNLSGGQKQRVSLARAV 780
Cdd:PRK13632 87 IifQNpdnqfigATVEDDIAFGlenkkVPPKKMK--DIIDDLAKK-------VGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 781 YCDRSVYLLDDPLSAVDAHvGKHIFDQVIGPQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQ-LKEEE 857
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEiLNNKE 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
642-848 |
5.20e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.00 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVaYVPQQAW------- 714
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 --IQN-------ATLKNNIIFGQKR----KESWYQRVVEACAL---QQDLDILPAgdeteigekgvNLSGGQKQRVSLAR 778
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFGLENigvpREEMVERVDQALRQvgmEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 779 AVYCDRSVYLLDDPLSAVDAhVGKhifDQVIGPQGLLKDKTRILV---THGLSYLPQADLVLVMVDGEITEIG 848
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1274-1495 |
5.27e-20 |
|
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: 90.70 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIE-----PAEGQISIDGVDIAKLGLH--E 1346
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1347 LRSRITIIPQDPVLFSGTLRMNLD---PFDSYSDEDIWKALEFSHLKTfvSGLPDKLSHECSEGGenLSVGQRQLLCLAR 1423
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglRLHGIKLKEELDERVEEALRK--AALWDEVKDRLHALG--LSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1424 ALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNT---IMDYTrvLVLDKGQMAEFDSPSSL 1495
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRT--AFLLNGRLVEFGPTEQI 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
641-849 |
5.29e-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: 89.78 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 641 SISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVA 707
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 708 YVPQQAWIQNATLKNNI-IFGQkrkeswyqrvveacalQQDLDILPAgdeTEIGEKGVNLSGGQKQRVSLARAVYCDRSV 786
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDE----------------YSDEEIYGA---LRVSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 787 YLLDDPLSAVDAHVgKHIFDQVIgpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGS 849
Cdd:cd03369 147 LVLDEATASIDYAT-DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
648-849 |
5.98e-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: 91.02 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 648 VFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-------------VAYVPQQ-- 712
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQDpy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 713 ---------AWIQNATLKnniIFGQKRKEswyQRVVEACA---LQQD-LDILPAgdeteigekgvNLSGGQKQRVSLARA 779
Cdd:COG1124 90 aslhprhtvDRILAEPLR---IHGLPDRE---ERIAELLEqvgLPPSfLDRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 780 VYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGL---SYLpqADLVLVMVDGEITEIGS 849
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILN-------LLKDLREergltyLFVSHDLavvAHL--CDRVAVMQNGRIVEELT 222
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
985-1245 |
7.67e-20 |
|
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: 91.84 E-value: 7.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 985 VVNGTQPDRLMRLGVYGGLGVsqGVAVFGYSLSVSIGGILASRfLHQSMLFD--------VLRSPMSFFERTPSGNLVNR 1056
Cdd:cd07346 25 LIDDVIPAGDLSLLLWIALLL--LLLALLRALLSYLRRYLAAR-LGQRVVFDlrrdlfrhLQRLSLSFFDRNRTGDLMSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1057 FAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATP----MVAFIIPFLGLLYFFVQRFYVASSRQLKrlESVSRspI 1132
Cdd:cd07346 102 LTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRRRIRKASREVR--ESLAE--L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1133 YTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNciVSFAALFAVLA----RENLSP 1208
Cdd:cd07346 178 SAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA--LGTALVLLYGGylvlQGSLTI 255
|
250 260 270
....*....|....*....|....*....|....*..
gi 1357684105 1209 GIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd07346 256 GELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1291-1489 |
8.97e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 95.20 E-value: 8.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLD 1370
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1371 PFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQ 1450
Cdd:COG4618 428 RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1357684105 1451 STIRSQFED-CTVLTIAHRLNTIMDYTRVLVLDKGQMAEF 1489
Cdd:COG4618 508 AAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
657-849 |
9.72e-20 |
|
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: 90.09 E-value: 9.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------SVAYVPQQ-AWIQNATLKNNI 724
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 IFG---QKRKESW-----YQRVVEACALQQdLDIL----PAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:cd03296 96 AFGlrvKPRSERPpeaeiRAKVHELLKLVQ-LDWLadryPA-----------QLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 793 LSAVDAHVGKHIFDQVigpqGLLKDK---TRILVTHGLS-YLPQADLVLVMVDGEITEIGS 849
Cdd:cd03296 164 FGALDAKVRKELRRWL----RRLHDElhvTTVFVTHDQEeALEVADRVVVMNKGRIEQVGT 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1290-1500 |
9.88e-20 |
|
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: 90.30 E-value: 9.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLhELRSRITIIPQDPVLFSG-TLRMN 1368
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1369 LDPF----DSYSDEDIWKALEFSHLktFvsGLPDKLSHECSEggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLE 1444
Cdd:COG4555 95 IRYFaelyGLFDEELKKRIEELIEL--L--GLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1445 TDNLIQSTIRSQF-EDCTVLTIAHrlntIMD-----YTRVLVLDKGQMAEFDSPSSLIAQKG 1500
Cdd:COG4555 167 ARRLLREILRALKkEGKTVLFSSH----IMQevealCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
657-853 |
1.07e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.44 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLG--EMDkmEGSVAVKG-----------SVAYVPQQ-AWIQNATLKN 722
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDPT--SGEILIGGrdvtdlppkdrNIAMVFQSyALYPHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 723 NIIFGQKR----KESWYQRVVEACA---LQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSA 795
Cdd:COG3839 95 NIAFPLKLrkvpKAEIDRRVREAAEllgLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 796 VDAHvgkhifdqvigpqglLKDKTR--------------ILVTHGlsylpQ------ADLVLVMVDGEITEIGSYLQL 853
Cdd:COG3839 164 LDAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QveamtlADRIAVMNDGRIQQVGTPEEL 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
652-809 |
1.47e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 88.69 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 652 SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------------SVAYVPQQ-AWIQNA 718
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAdGLKPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIF-----GQKRKESWYQRVVEACALQQDLDiLPAGdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:COG4133 91 TVRENLRFwaalyGLRADREAIDEALEAVGLAGLAD-LPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170
....*....|....*.
gi 1357684105 794 SAVDAHvGKHIFDQVI 809
Cdd:COG4133 160 TALDAA-GVALLAELI 174
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1269-1488 |
1.66e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 89.38 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1269 PTEGCIHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSL---TLGLfriIEPAEGQISIDGVDIAKLglh 1345
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLlkaILGL---LPPTSGTVRLFGKPPRRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1346 elRSRITIIPQ----DP--------VLFSGTL-RMNLdpFDSYSDED---IWKALEFSHLktfvSGLPDKLSHEcsegge 1409
Cdd:COG1121 74 --RRRIGYVPQraevDWdfpitvrdVVLMGRYgRRGL--FRRPSRADreaVDEALERVGL----EDLADRPIGE------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1410 nLSVGQRQllclarallrKT----------KVLVLDEATAAVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDY-TR 1477
Cdd:COG1121 140 -LSGGQQQ----------RVllaralaqdpDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDR 208
|
250
....*....|.
gi 1357684105 1478 VLVLDKGQMAE 1488
Cdd:COG1121 209 VLLLNRGLVAH 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
642-849 |
2.16e-19 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 89.80 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSL---LSALLgemDKMEGSVAVKGSVAYVPQQAW---- 714
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLL---LPTSGKVTVDGLDTLDEENLWeirk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 -----IQN-------ATLKNNIIFGQ-----KRKESWyQRVVEACALQQDLDIL---PAgdeteigekgvNLSGGQKQRV 774
Cdd:TIGR04520 78 kvgmvFQNpdnqfvgATVEDDVAFGLenlgvPREEMR-KRVDEALKLVGMEDFRdrePH-----------LLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 775 SLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKD--KTRILVTHGLSYLPQADLVLVMVDGEITEIGS 849
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETI---RKLNKEegITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1274-1486 |
2.65e-19 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 86.68 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGlHELRS 1349
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIIlgllKPDSGEIKVLGKDIKKEP-EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1350 RITIIPQDPVLFSG-TLRMNLDpfdsysdediwkalefshlktfvsglpdklshecseggenLSVGQRQLLCLARALLRK 1428
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1429 TKVLVLDEATAAVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQM 1486
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1290-1485 |
3.15e-19 |
|
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: 86.86 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLH--ELRSRITIIPQDPVLFSG-TLR 1366
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNLdpfdsysdediwkalefshlktfvsGLPdklshecseggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETD 1446
Cdd:cd03229 95 ENI-------------------------ALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1357684105 1447 NLIQSTIRSQFED--CTVLTIAHRLNTIMDYT-RVLVLDKGQ 1485
Cdd:cd03229 137 REVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1274-1485 |
3.28e-19 |
|
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: 87.52 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRY---RSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGvdiaklglhelrsR 1350
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1351 ITIIPQDPVLFSGTLRMNL---DPFDSysdEDIWKALEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLR 1427
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1428 KTKVLVLDEATAAVDLETDNLIqstirsqFEDC---------TVLTIAHRLNTIMDYTRVLVLDKGQ 1485
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1281-1499 |
3.79e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1281 LRYR-SDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG--VDIAKLGLHELRSRITIIPQD 1357
Cdd:PRK13636 11 LNYNySDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 P--VLFSGTLR-------MNLdpfdSYSDEDIWKALEFSHLKTFVSGLPDKLSHEcseggenLSVGQRQLLCLARALLRK 1428
Cdd:PRK13636 91 PdnQLFSASVYqdvsfgaVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1429 TKVLVLDEATAAVDLETDNLIQSTIRSQFE--DCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCdNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1220-1489 |
4.08e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1220 QLTASLTWLVRMSSDVeTNIVA-VERVKEYSDTEKEAEwRHEPPTVPPDWPTEGCIHITNFGLRyRSDLDLAIRNINVDI 1298
Cdd:COG4178 310 QVQGALSWFVDNYQSL-AEWRAtVDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1299 SGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISI-DGVDIAklglhelrsritIIPQDPVLFSGTLRMNL---D 1370
Cdd:COG4178 387 KPGERLLITGPSGSGKSTL----LRAIaglwPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREALlypA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1371 PFDSYSDEDIWKALEFSHLKTFVSGLpdklsHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQ 1450
Cdd:COG4178 451 TAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1357684105 1451 STIRSQFEDCTVLTIAHRlNTIMDY-TRVLVLDKGQMAEF 1489
Cdd:COG4178 526 QLLREELPGTTVISVGHR-STLAAFhDRVLELTGDGSWQL 564
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
642-849 |
4.21e-19 |
|
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: 88.56 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDgvFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:COG1120 2 LEAEN--LSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQawiqnatlkNNIIFG--------------QKRKESW----YQRVVEACALqqdLDIlpagdeTEIGEKGVN-LSGG 769
Cdd:COG1120 80 VPQE---------PPAPFGltvrelvalgryphLGLFGRPsaedREAVEEALER---TGL------EHLADRPVDeLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 770 QKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKD--KTRILVTHGLS----YlpqADLVLVMVDGE 843
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELL---RRLARErgRTVVMVLHDLNlaarY---ADRLVLLKDGR 215
|
....*.
gi 1357684105 844 ITEIGS 849
Cdd:COG1120 216 IVAQGP 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1274-1490 |
5.53e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 93.94 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAI-RNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISI-DGVDIAKLGLHELRSRI 1351
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1352 TIIPQDPVLFSGTLRMNL-------------------DPFDSYSDEDIWKAL------------------EFSHLKT--- 1391
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQENKNKRNSCrakcagdlndmsnttdsnELIEMRKnyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1392 ------------------FVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTI 1453
Cdd:PTZ00265 543 tikdsevvdvskkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1357684105 1454 RS--QFEDCTVLTIAHRLNTIMDYTRVLVL---DKGQMAEFD 1490
Cdd:PTZ00265 623 NNlkGNENRITIIIAHRLSTIRYANTIFVLsnrERGSTVDVD 664
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
333-616 |
6.33e-19 |
|
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: 89.15 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 333 FIQDILMFAGPEILRLLIKFVndPDAPPWQGYFYTALLFVCTCVQSLILQRYFHVCFV-SGMRLRTAVIGAVYRKALVIS 411
Cdd:cd07346 9 LLATALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAArLGQRVVFDLRRDLFRHLQRLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 412 SAARRTSTVGEIVNLMSVDAQRFMDLVTY-INMIWSAPLQVVLALYFLWeNLGPSV-LAGVAVMILMVPVNAVIAMKTKT 489
Cdd:cd07346 87 LSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILF-YLNWKLtLVALLLLPLYVLILRYFRRRIRK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 490 YQVAQMKNKDSRIKLMNEMLNGIKVLKLYAWEMA----FRDKVSQIRENELQVLKKAAYLGAVSTFTWVCAPFLVALstF 565
Cdd:cd07346 166 ASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL--Y 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 566 SVYVLSndQNVLDAQKAFVSLALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd07346 244 GGYLVL--QGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1274-1497 |
9.02e-19 |
|
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: 87.55 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDL--AIRNINVDISGGEKVGIVGRTGAGKSSLT---LGLFRiiePAEGQISIDGVDIAKLGLHELR 1348
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLralAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1349 SRITIIPQDPvlfSGTL--RMNLD-----PFDSY----SDEDIWKALEFshlktfVsGLP----DKLSHEcseggenLSV 1413
Cdd:COG1124 79 RRVQMVFQDP---YASLhpRHTVDrilaePLRIHglpdREERIAELLEQ------V-GLPpsflDRYPHQ-------LSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1414 GQRQLLCLARALLRKTKVLVLDEATAAVDL----ETDNLIQStIRSQfEDCTVLTIAHRLNTImDY--TRVLVLDKGQMA 1487
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKD-LREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIV 218
|
250
....*....|
gi 1357684105 1488 EFDSPSSLIA 1497
Cdd:COG1124 219 EELTVADLLA 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
642-866 |
1.12e-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: 87.66 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVP---------- 710
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPlhtlrsrlsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 711 --QQAWIQNATLKNNIIFGQKRKESWYQRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYL 788
Cdd:cd03288 100 ilQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 789 LDDPLSAVDAHVgKHIFDQVIgpQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQL-KEEEGAFAEFLRT 866
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASLVRT 255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
652-854 |
1.34e-18 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 86.40 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 652 SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------------SVAYVPQqawiqnat 719
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 lKNNI-----------IFGQKRKESWYQRVVEACALQQDLDILPAGDeTEIGekgvNLSGGQKQRVSLARAVYCDRSVYL 788
Cdd:cd03263 83 -FDALfdeltvrehlrFYARLKGLPKSEIKEEVELLLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 789 LDDPLSAVDaHVGKHIFDQVIgpQGLLKDKTRILVTHGL---SYLpqADLVLVMVDGEITEIGSYLQLK 854
Cdd:cd03263 157 LDEPTSGLD-PASRRAIWDLI--LEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKLRCIGSPQELK 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
659-849 |
1.67e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 90.73 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------------SVAYVPQQAWIQ-NA--T 719
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDPYSSlNPrmT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNI-----IFGQKRKESWYQRVVEA---CALQQD-LDILPAGdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:COG1123 361 VGDIIaeplrLHGLLSRAERRERVAELlerVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 791 DPLSAVDAHVGKHIFDqvigpqgLLKD------KTRILVTHGLS---YLpqADLVLVMVDGEITEIGS 849
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRDlqrelgLTYLFISHDLAvvrYI--ADRVAVMYDGRIVEDGP 488
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1271-1485 |
2.70e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1271 EGCIHITNFGLRYRSDldlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIA--KLGLHELR 1348
Cdd:PRK13637 6 ENLTHIYMEGTPFEKK---ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1349 SRITIIPQDP--VLFSGTL---------RMNLdpfdsySDEDI----WKALEFSHLKtfVSGLPDKLSHEcseggenLSV 1413
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIekdiafgpiNLGL------SEEEIenrvKRAMNIVGLD--YEDYKDKSPFE-------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1414 GQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFE--DCTVLTIAHRLNTIMDY-TRVLVLDKGQ 1485
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGK 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
642-853 |
3.09e-18 |
|
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: 85.71 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIED--GVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGeMDK-MEGSVAVKG-------------- 704
Cdd:cd03258 2 IELKNvsKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 705 --SVAYVPQQ-AWIQNATLKNNI-----IFGQKRKESwYQRVVEACA---LQQDLDILPAgdeteigekgvNLSGGQKQR 773
Cdd:cd03258 81 rrRIGMIFQHfNLLSSRTVFENValpleIAGVPKAEI-EERVLELLElvgLEDKADAYPA-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 774 VSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGLSYLPQ-ADLVLVMVDGEITE 846
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILA-------LLRDINRelgltiVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
....*..
gi 1357684105 847 IGSYLQL 853
Cdd:cd03258 222 EGTVEEV 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
655-858 |
4.71e-18 |
|
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: 85.29 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------------SVAYVPQQAWI-QNATLK 721
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLyDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNI-----IFGQKRKE--SWYQRVVEACALQQDLDilpagdeteigEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:COG4555 93 ENIryfaeLYGLFDEElkKRIEELIELLGLEEFLD-----------RRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 795 AVDAhVGKHIFDQVIgpQGLLKDKTRILVThglSYLPQ-----ADLVLVMVDGEITEIGSYLQLKEEEG 858
Cdd:COG4555 162 GLDV-MARRLLREIL--RALKKEGKTVLFS---SHIMQevealCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
659-856 |
7.69e-18 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 84.21 E-value: 7.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVP----------QQ-AWIQNATLKNNIIF 726
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 727 G----QKRKESWYQRVVEACALQQdLDILPAGDETEigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGK 802
Cdd:cd03300 96 GlrlkKLPKAEIKERVAEALDLVQ-LEGYANRKPSQ-------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 803 HIfdqvigpQGLLKD------KTRILVTHGLS-YLPQADLVLVMVDGEITEIGSYLQLKEE 856
Cdd:cd03300 168 DM-------QLELKRlqkelgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
643-845 |
9.15e-18 |
|
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: 83.46 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 643 SIEDGVFSWSRSESpTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------SVAYVPQQ 712
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 713 AWIQ--NATLKNNIIFGQKRKESWYQRVveACALQqDLDILPAGDETEIgekgvNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:cd03226 80 VDYQlfTDSVREELLLGLKELDAGNEQA--ETVLK-DLDLYALKERHPL-----SLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 791 DPLSAVDAH----VGKhIFDQVIGpqgllKDKTRILVTHGLSYLPQ-ADLVLVMVDGEIT 845
Cdd:cd03226 152 EPTSGLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
649-843 |
1.15e-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: 82.23 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 649 FSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG---------------SVAYVPQQ- 712
Cdd:cd03229 6 VSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 713 AWIQNATLKNNIIFGqkrkeswyqrvveacalqqdldilpagdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:cd03229 86 ALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 793 LSAVDAHVGKHIfdqvigpQGLLKD------KTRILVTHGLSYLPQ-ADLVLVMVDGE 843
Cdd:cd03229 128 TSALDPITRREV-------RALLKSlqaqlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
638-870 |
1.38e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.55 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 638 SAYSISIEDGVFSWsRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS----------VA 707
Cdd:PRK15056 3 QQAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 708 YVPQQA---WIQNATLKNNIIFGQKRKESWYQR--------VVEACALQQDLDIlpagDETEIGEkgvnLSGGQKQRVSL 776
Cdd:PRK15056 82 YVPQSEevdWSFPVLVEDVVMMGRYGHMGWLRRakkrdrqiVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 777 ARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVigpqGLLKD--KTRILVTHGLSYLPQADLVLVMVDGEITEIG---SYL 851
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLL----RELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGpteTTF 229
|
250
....*....|....*....
gi 1357684105 852 QLKEEEGAFAEFLRTYASS 870
Cdd:PRK15056 230 TAENLELAFSGVLRHVALN 248
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
668-848 |
1.88e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 82.73 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 668 EGSLVAVVGHVGSGKSSLLSALLGeMDKMEGSVAVKGSVAYV---------PQQAWI----QNATL------KNNIIFGQ 728
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG-LEKPDGGTIVLNGTVLFdsrkkinlpPQQRKIglvfQQYALfphlnvRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 729 KRKESWYQR-----VVEACALQQDLDILPAGdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKH 803
Cdd:cd03297 101 KRKRNREDRisvdeLLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 804 IFDQVigpQGLLKD--KTRILVTHGLS---YLpqADLVLVMVDGEITEIG 848
Cdd:cd03297 170 LLPEL---KQIKKNlnIPVIFVTHDLSeaeYL--ADRIVVMEDGRLQYIG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
659-844 |
4.90e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGeMDKMEGSVAVKGSvayvpqqAWIQNATLKNNIIFGQKRKESWyQRV 738
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGT-------APLAEAREDTRLMFQDARLLPW-KKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 739 VEACAL-------QQDLDILPA-GDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGkhifdqvIG 810
Cdd:PRK11247 99 IDNVGLglkgqwrDAALQALAAvGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR-------IE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1357684105 811 PQGLLKDK------TRILVTHGLS-YLPQADLVLVMVDGEI 844
Cdd:PRK11247 172 MQDLIESLwqqhgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
659-844 |
6.54e-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: 79.75 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGsvayvpQQAWIQNATLKNNIIFgqkrkeswyqrV 738
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGY-----------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 739 VEACALQQDLdilpagdeTeiGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAhVGKHIFDQVIgpQGLLKD- 817
Cdd:cd03230 79 PEEPSLYENL--------T--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKKEg 145
|
170 180
....*....|....*....|....*...
gi 1357684105 818 KTRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:cd03230 146 KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
659-849 |
9.81e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 83.61 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------SVAYVPQQAwiqnA-----TLKN 722
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVGMVFQDY----AlfphlTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 723 NIIFGQKR----KESWYQRVVEACALqqdldilpagdeTEIGEKG----VNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:COG3842 97 NVAFGLRMrgvpKAEIRARVAELLEL------------VGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 795 AVDAHVGKHIfdqvigpQGLLKD------KTRILVTH----GLSYlpqADLVLVMVDGEITEIGS 849
Cdd:COG3842 165 ALDAKLREEM-------REELRRlqrelgITFIYVTHdqeeALAL---ADRIAVMNDGRIEQVGT 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1274-1508 |
9.92e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 82.37 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDP-VLFSGT---------LRMNLDPFDSYSdEDIWKALEFSHLKTFvsglpdkLSHECSeggeNLSVGQRQLLCLAR 1423
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddvafgLENIGVPREEMV-ERVDQALRQVGMEDF-------LNREPH----RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1424 ALLRKTKVLVLDEATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKGA 1501
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
....*..
gi 1357684105 1502 FYRMAKD 1508
Cdd:PRK13635 234 LQEIGLD 240
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
659-849 |
1.02e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 83.66 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLG-EM-DkmEGSVAVKGSVAYV---PQQAWI----QNATL-KN-----N 723
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETpD--SGRIVLNGRDLFTnlpPRERRVgfvfQHYALfPHmtvaeN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFG-QKRKESwyQRVVEACALQQdLDIL---------PAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:COG1118 96 IAFGlRVRPPS--KAEIRARVEEL-LELVqlegladryPS-----------QLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 794 SAVDAHVGKHIFDQVIgpqGLLKD--KTRILVTHGLS-YLPQADLVLVMVDGEITEIGS 849
Cdd:COG1118 162 GALDAKVRKELRRWLR---RLHDElgGTTVFVTHDQEeALELADRVVVMNQGRIEQVGT 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1290-1487 |
1.20e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 79.01 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHE-LRSRITIIPQdpvlfsgtlrmn 1368
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1369 ldpfdsysdediwkalefshlktfvsglpdklshecseggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVDL-ETDN 1447
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1357684105 1448 LIQsTIRS-QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMA 1487
Cdd:cd03216 121 LFK-VIRRlRAQGVAVIFISHRLDEVFEIAdRVTVLRDGRVV 161
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
642-854 |
1.30e-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: 81.01 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSwsRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS---------------- 705
Cdd:cd03261 1 IELRGLTKS--FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 706 VAYVPQQawiqNA-----TLKNNIIFG----QKRKESWYQRVV----EACALQQDLDILPAgdeteigekgvNLSGGQKQ 772
Cdd:cd03261 79 MGMLFQS----GAlfdslTVFENVAFPlrehTRLSEEEIREIVleklEAVGLRGAEDLYPA-----------ELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 773 RVSLARAVYCDRSVYLLDDPLSAVDAhVGKHIFDQVIgpqGLLKDK---TRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDP-IASGVIDDLI---RSLKKElglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
|
....*.
gi 1357684105 849 SYLQLK 854
Cdd:cd03261 220 TPEELR 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
642-849 |
1.49e-16 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 80.81 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWsRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWI-QNATLKNNII-------FGQKRKEswyQRVVEACALqqdLDILPAG------DEteigekgvnLSGGQKQRV 774
Cdd:cd03295 80 VIQQIGLfPHMTVEENIAlvpkllkWPKEKIR---ERADELLAL---VGLDPAEfadrypHE---------LSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 775 SLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPQGLLKdKTRILVTHGL-SYLPQADLVLVMVDGEITEIGS 849
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELG-KTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGT 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
642-849 |
1.49e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSS---LLSALLGEMDKMEGSVAVKGsVAYVPQQAW---- 714
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 -----IQN-------ATLKNNIIFGQK-----RKE--SWYQRVVEACALQQDLDILPAgdeteigekgvNLSGGQKQRVS 775
Cdd:PRK13640 85 kvgivFQNpdnqfvgATVGDDVAFGLEnravpRPEmiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 776 LARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIgpqGLLKDK--TRILVTHGLSYLPQADLVLVMVDGEITEIGS 849
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIR---KLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1290-1485 |
1.77e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGLHElRSR-ITIIPQDPVLfsGT 1364
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL----LNAIagslPPDSGSILIDGKDVTKLPEYK-RAKyIGRVFQDPMM--GT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 ---------------------LRMNLDPfdsySDEDIWKALefshLKTFVSGLPDKLSHECseggENLSVGQRQLLCLAR 1423
Cdd:COG1101 94 apsmtieenlalayrrgkrrgLRRGLTK----KRRELFREL----LATLGLGLENRLDTKV----GLLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1424 ALLRKTKVLVLDEATAAVD-------LE-TDNLIQStirsqfEDCTVLTIAHRLNTIMDY-TRVLVLDKGQ 1485
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEGR 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1274-1485 |
3.07e-16 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 79.46 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLD--LAIRNINVDISGGEKVGIVGRTGAGKSSL--TLGLfrIIEPAEGQISIDGVDIAKLGLHEL-- 1347
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVRVDGTDISKLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1348 --RSRITIIPQD---------------PVLFSGTLRmnldpfdsysDEDIWKALEFshLKTFvsGLPDKLSHECSEggen 1410
Cdd:cd03255 79 frRRHIGFVFQSfnllpdltalenvelPLLLAGVPK----------KERRERAEEL--LERV--GLGDRLNHYPSE---- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1411 LSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS--QFEDCTVLTIAHRLNTIMDYTRVLVLDKGQ 1485
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1290-1490 |
9.07e-16 |
|
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: 77.96 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLH-----ELRSRitiipqDPVLFSGT 1364
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGggfnpELTGR------ENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 LrMNLDP--FDSYSDEdIWkalEFSHLKTFVSgLPDKlshecseggeNLSVGQRQLLCLARALLRKTKVLVLDEATAAVD 1442
Cdd:cd03220 111 L-LGLSRkeIDEKIDE-II---EFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1443 LETDNLIQSTIRSQFEDC-TVLTIAHRLNTIMDY-TRVLVLDKGQMAEFD 1490
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1292-1497 |
9.91e-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: 78.31 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSLT---LGLFRiiePAEGQISIDGVDIAKLG---LHELRSRITIIPQDPVLFSGT- 1364
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLrliVGLLR---PDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFDSLt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 --------LRMNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLShecseGGENLSVG-QRqllclarALLRKTKVLVLD 1435
Cdd:cd03261 94 vfenvafpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELS-----GGMKKRVAlAR-------ALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1436 EATAAVD----LETDNLIQSTIRSQfeDCTVLTIAHRLNTIM---DytRVLVLDKGQMAEFDSPSSLIA 1497
Cdd:cd03261 162 EPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFaiaD--RIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1290-1497 |
1.19e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG-LHELRSRITIIPQDPV--------- 1359
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPEtqfvgrtve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1360 --LFSGTLRMNLDPFDSYSDEDiwKALEFSHLKTFVSGLPdklshecseggENLSVGQRQLLCLARALLRKTKVLVLDEA 1437
Cdd:PRK13644 97 edLAFGPENLCLPPIEIRKRVD--RALAEIGLEKYRHRSP-----------KTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1438 TAAVDLETDNLIQSTIRSQFEDC-TVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIA 1497
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
954-1221 |
1.40e-15 |
|
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: 78.97 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 954 LLSAISLLFFLShnLLSMFANYWLSLWTDDPVVNGTQP-DRLMRL-GVYGGLGVSQGVAVFGYSLSVSIGGilasrflhQ 1031
Cdd:cd18544 1 FILALLLLLLAT--ALELLGPLLIKRAIDDYIVPGQGDlQGLLLLaLLYLGLLLLSFLLQYLQTYLLQKLG--------Q 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1032 SMLFD--------VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFI---- 1099
Cdd:cd18544 71 RIIYDlrrdlfshIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALIsllv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1100 IPFLGLLYFFVQRFYVASSRQLKrlESVSRspIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRW 1179
Cdd:cd18544 151 LPLLLLATYLFRKKSRKAYREVR--EKLSR--LNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFAL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1357684105 1180 LAIRLEFVGNciVSFAALFAVLAR----ENLSPGIMGLSISYALQL 1221
Cdd:cd18544 227 FRPLVELLSS--LALALVLWYGGGqvlsGAVTLGVLYAFIQYIQRF 270
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
659-864 |
1.46e-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: 77.76 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-----------VAYVPQQ-AWIQNATLKNNIIF 726
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 727 G-QKRKESWYQRVVEACALQQDLDIlpagdETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIF 805
Cdd:cd03299 95 GlKKRKVDKKEIERKVLEIAEMLGI-----DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 806 DqvigpqgLLK------DKTRILVTHGLS-YLPQADLVLVMVDGEITEIGSYLQL--KEEEGAFAEFL 864
Cdd:cd03299 170 E-------ELKkirkefGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVfkKPKNEFVAEFL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
659-846 |
2.03e-15 |
|
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: 77.47 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------------SVAYVpQQAW--IQNAT 719
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNI-----IFG----QKRKESWYQRVveacALQQDLDILPAGdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:COG4181 107 ALENVmlpleLAGrrdaRARARALLERV----GLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 791 DPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGLSYLPQADLVLVMVDGEITE 846
Cdd:COG4181 172 EPTGNLDAATGEQIID-------LLFELNRergttlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1289-1486 |
2.66e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 76.68 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1289 LAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKL---GLHELRSRITIIPQDPVLFSgtl 1365
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQDFRLLP--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1366 rmNLDPFdsysdEDIWKALEfshlktfVSGLPDK--------------LSHECSEGGENLSVGQRQLLCLARALLRKTKV 1431
Cdd:cd03292 92 --DRNVY-----ENVAFALE-------VTGVPPReirkrvpaalelvgLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1432 LVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMDYT--RVLVLDKGQM 1486
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTrhRVIALERGKL 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1274-1490 |
3.85e-15 |
|
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: 76.02 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGLHelRS 1349
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIagleRPDSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1350 RITIIPQDPVLF----------SGtLRMNLDPFDSySDEDIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLL 1419
Cdd:cd03259 73 NIGMVFQDYALFphltvaeniaFG-LKLRGVPKAE-IRARVRELLELVGLEGLLNRYPHELSG-----------GQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1420 CLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFE--DCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFD 1490
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1274-1489 |
4.33e-15 |
|
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: 75.69 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGeKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGlHELRSRITI 1353
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDPVLFSG-TLRMNLDPF-------DSYSDEDIWKALEFSHLKTFVSGLPDKLShecsegGenlsvGQRQLLCLARAL 1425
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSLS------G-----GMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1426 LRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNTIMD-YTRVLVLDKGQMAEF 1489
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1274-1499 |
4.56e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.20 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLD--LAIRNINVDISGGEKVGIVGRTGAGKSSltlgLFRII----EPAEGQISIDGVDIAKL---GL 1344
Cdd:COG1135 2 IELENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCInlleRPTSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1345 HELRSRITIIPQDPVLFSG-TLRMNLD-PF--DSYSDEDIW-KALEfshLKTFVsGLPDKLSHECSEggenLSVGQRQll 1419
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSrTVAENVAlPLeiAGVPKAEIRkRVAE---LLELV-GLSDKADAYPSQ----LSGGQKQrv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1420 clarallrktKVLVLDEATAAVDLETD----NLIQStIRSQFeDCTVLTIAHRLN---TIMDytRVLVLDKGQMAE---- 1488
Cdd:COG1135 150 giaralannpKVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDvvrRICD--RVAVLENGRIVEqgpv 225
|
250
....*....|....
gi 1357684105 1489 ---FDSPSSLIAQK 1499
Cdd:COG1135 226 ldvFANPQSELTRR 239
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
983-1245 |
7.30e-15 |
|
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: 76.83 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 983 DPVVNGTQPDRLMRLGVY-GGLGVSQGVAVF-GYSLSVSIGGILASRFlhQSMLFD-VLRSPMSFFERTPSGNLVNRFAK 1059
Cdd:cd18557 24 DTIIKGGDLDVLNELALIlLAIYLLQSVFTFvRYYLFNIAGERIVARL--RRDLFSsLLRQEIAFFDKHKTGELTSRLSS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1060 EMDTIDSLIPMILKMFMGSLFNVLGSCVIILVA----TPMVAFIIPFLGLLYFFVQRFYVASSRQLkrLESVSRSPiyTH 1135
Cdd:cd18557 102 DTSVLQSAVTDNLSQLLRNILQVIGGLIILFILswklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1136 FNETLLGTSVIRAFGEQERfihESDQRVDHNQKAYYPSIVANRWLAIrLEFVGNCIVsFAALFAVL-------ARENLSP 1208
Cdd:cd18557 178 AEESLSNIRTVRSFSAEEK---EIRRYSEALDRSYRLARKKALANAL-FQGITSLLI-YLSLLLVLwyggylvLSGQLTV 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 1357684105 1209 GIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18557 253 GELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
642-884 |
8.96e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDgvFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAY 708
Cdd:PRK09536 4 IDVSD--LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQ-NATLKNNIIFGQKRKESWYQRVVEA--CALQQDLDilpAGDETEIGEKGV-NLSGGQKQRVSLARAVYCDR 784
Cdd:PRK09536 82 VPQDTSLSfEFDVRQVVEMGRTPHRSRFDTWTETdrAAVERAME---RTGVAQFADRPVtSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKD-KTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGsylqlKEEEGAFAE 862
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELV---RRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAG-----PPADVLTAD 230
|
250 260
....*....|....*....|..
gi 1357684105 863 FLRTYASSEQTDGSEPVPNSPS 884
Cdd:PRK09536 231 TLRAAFDARTAVGTDPATGAPT 252
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
662-852 |
8.96e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.84 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-----------VAYVPQQ-AWIQNATLKNNIIFGQK 729
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSyALFPHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 730 R----KESWYQRVVEACALQqDLdilpAGDEteigEKGVN-LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHI 804
Cdd:PRK11432 105 MlgvpKEERKQRVKEALELV-DL----AGFE----DRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 805 FDQVIGPQGLLkDKTRILVTHGLS-YLPQADLVLVMVDGEITEIGS----YLQ 852
Cdd:PRK11432 176 REKIRELQQQF-NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSpqelYRQ 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
659-844 |
1.33e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 74.49 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL--LGEMDkmEGSVAVKGSVAYVPQQAWIQ----------------NATL 720
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 721 KNNIIFGQKrkesWYQRVVEACALQQDLDILP-AGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAH 799
Cdd:cd03262 94 LENITLAPI----KVKGMSKAEAEERALELLEkVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1357684105 800 VGKHIFDqVIgpQGLLKDK-TRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:cd03262 170 LVGEVLD-VM--KDLAEEGmTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1290-1492 |
1.42e-14 |
|
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: 76.63 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEP---AEGQISIDGVDIAKLGLHELRS----RITIIPQDPvlfs 1362
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 gtlrMN-LDP--------------FDSYSDEDIW-KALEfsHLKTfVsGLPDKLS------HEcseggenLSVGQRQllc 1420
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIE--LLER-V-GLPDPERrldrypHE-------LSGGMRQrvm 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1421 larallrktKVLVLDEATAAVD-------LetdNLIQStIRSQFeDCTVLTIAHRLNT---IMDytRVLVLDKGQMAE-- 1488
Cdd:COG0444 161 iaralalepKLLIADEPTTALDvtiqaqiL---NLLKD-LQREL-GLAILFITHDLGVvaeIAD--RVAVMYAGRIVEeg 233
|
....*....
gi 1357684105 1489 -----FDSP 1492
Cdd:COG0444 234 pveelFENP 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1284-1496 |
1.65e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.38 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1284 RSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELR-----------SRIT 1352
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1353 IIPQDPVLFSGTLRMNLDPFDSYS-DEDIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLARALLRKTKV 1431
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEErREKALDALRQVGLENYAHSYPDELSG-----------GMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1432 LVLDEATAAVD--LET---DNLIQSTIRSQFedcTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLI 1496
Cdd:PRK10070 186 LLMDEAFSALDplIRTemqDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
662-849 |
1.95e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 76.69 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------------SVAYVPQQAWI-QNATLKNN 723
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFGQKR-----KESWYQRVVEACALQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDa 798
Cdd:TIGR02142 96 LRYGMKRarpseRRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 799 hvgKHIFDQVIGPQGLLKDKTRI---LVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:TIGR02142 164 ---DPRKYEILPYLERLHAEFGIpilYVSHSLQEVLRlADRVVVLEDGRVAAAGP 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1290-1497 |
2.22e-14 |
|
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: 74.01 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHElRSR--ITIIPQDPVLFSG-TLR 1366
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARagIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNLD-----PFDSYSDEDIWKALE-FSHLKtfvsglpDKLSHEcsegGENLSVGQRQLLCLARALLRKTKVLVLDEATAA 1440
Cdd:cd03224 94 ENLLlgayaRRRAKRKARLERVYElFPRLK-------ERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1441 vdletdnlIQSTIRSQFEDC---------TVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLIA 1497
Cdd:cd03224 163 --------LAPKIVEEIFEAirelrdegvTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
642-848 |
2.43e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV-------------AVKGSVAY 708
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 709 VPQQAWIQ--NATLKNNIIFGQKRKESWYQRVVEACA-LQQDLDILP-AGDETEigekgvNLSGGQKQRVSLARAVYCDR 784
Cdd:PRK13648 88 VFQNPDNQfvGSIVKYDVAFGLENHAVPYDEMHRRVSeALKQVDMLErADYEPN------ALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDQVigpQGLLKDK--TRILVTHGLSYLPQADLVLVMVDGEITEIG 848
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLV---RKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
659-864 |
2.68e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVP----------QQawiQN----ATLKNN 723
Cdd:COG3840 15 PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPpaerpvsmlfQE---NNlfphLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFG----------QKrkeswyQRVVEACA---LQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:COG3840 92 IGLGlrpglkltaeQR------AQVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 791 DPLSAVDA---HVGKHIFDQVIGPQGLlkdkTRILVTHGLS-YLPQADLVLVMVDGEITEIGSY--LQLKEEEGAFAEFL 864
Cdd:COG3840 155 EPFSALDPalrQEMLDLVDELCRERGL----TVLMVTHDPEdAARIADRVLLVADGRIAADGPTaaLLDGEPPPALAAYL 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
641-849 |
3.10e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.89 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 641 SISIEDGVFSWSRSEspTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-----------VAYV 709
Cdd:PRK10851 2 SIEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 710 PQQ-AWIQNATLKNNIIFG------QKRKESWY--QRVVEACALQQdLDIL----PAgdeteigekgvNLSGGQKQRVSL 776
Cdd:PRK10851 80 FQHyALFRHMTVFDNIAFGltvlprRERPNAAAikAKVTQLLEMVQ-LAHLadryPA-----------QLSGGQKQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 777 ARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPQGLLKdKTRILVTHGL-SYLPQADLVLVMVDGEITEIGS 849
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELK-FTSVFVTHDQeEAMEVADRVVVMSQGNIEQAGT 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1274-1488 |
3.25e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.55 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDlAIRNINVDISGGEKVGIVGRTGAGKSSLtLGL-FRIIEPAEGQISIDGVDIAKL---GLHELRS 1349
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTL-LKLlYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1350 RITIIPQDpvlFSgtLRMNLDPFDS---------YSDEDIWKALEFShLKTFvsGLPDKLSHECSEggenLSVGQRQllc 1420
Cdd:COG2884 80 RIGVVFQD---FR--LLPDRTVYENvalplrvtgKSRKEIRRRVREV-LDLV--GLSDKAKALPHE----LSGGEQQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1421 larallrKT----------KVLVLDEATAAVDLETdnliqstirSQ-----FED-----CTVLtIA-HRLNTIMDY-TRV 1478
Cdd:COG2884 145 -------RVaiaralvnrpELLLADEPTGNLDPET---------SWeimelLEEinrrgTTVL-IAtHDLELVDRMpKRV 207
|
250
....*....|
gi 1357684105 1479 LVLDKGQMAE 1488
Cdd:COG2884 208 LELEDGRLVR 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1290-1497 |
3.39e-14 |
|
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: 73.87 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSG-TLRMN 1368
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1369 --LDP-FDSYSDEDI-WKALEFSHLktfvSGLP-----DKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVLDEATA 1439
Cdd:cd03295 96 iaLVPkLLKWPKEKIrERADELLAL----VGLDpaefaDRYPHE-------LSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1440 AVDLET-DNLIQSTIRSQFE-DCTVLTIAHRLN-TIMDYTRVLVLDKGQMAEFDSPSSLIA 1497
Cdd:cd03295 165 ALDPITrDQLQEEFKRLQQElGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
657-885 |
4.23e-14 |
|
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: 78.13 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV------------AVKGSVAYVPQQAWI-QNATLKNN 723
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietnldAVRQSLGMCPQHNILfHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIF-GQKRKESWYQRVVEACALQQDldilpAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGK 802
Cdd:TIGR01257 1024 ILFyAQLKGRSWEEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 803 HIFDQVIGPQgllKDKTRILVTHglsYLPQADL----VLVMVDGEITEIGSYLQLKE--EEGAFAEFLRTYAS-SEQTDG 875
Cdd:TIGR01257 1099 SIWDLLLKYR---SGRTIIMSTH---HMDEADLlgdrIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVRKMKNiQSQRGG 1172
|
250
....*....|
gi 1357684105 876 SEPVPNSPSK 885
Cdd:TIGR01257 1173 CEGTCSCTSK 1182
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1290-1488 |
4.25e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 73.63 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGLHElRSRITIIP--QDPVLFSG 1363
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 -TLRMNL-------------DPFDSYSDEDIW-KALEFshLKTFvsGLPDKLSHECSeggeNLSVGQRQLLCLARALLRK 1428
Cdd:cd03219 90 lTVLENVmvaaqartgsgllLARARREEREAReRAEEL--LERV--GLADLADRPAG----ELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1429 TKVLVLDEATAAVDL-ETDNLIQsTIRS-QFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQM-AE 1488
Cdd:cd03219 162 PKLLLLDEPAAGLNPeETEELAE-LIRElRERGITVLLVEHDMDVVMSLaDRVTVLDQGRViAE 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
663-849 |
4.82e-14 |
|
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: 75.52 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 663 NVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSV-----------------AYVPQQAwiqnaTL----- 720
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEA-----RLfphls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 721 -KNNIIFGQKRKESW-----YQRVVEACALQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:COG4148 94 vRGNLLYGRKRAPRAerrisFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 795 AVDAHVGKHI---FDQvigpqglLKDKTRI---LVTHGL---SYLpqADLVLVMVDGEITEIGS 849
Cdd:COG4148 163 ALDLARKAEIlpyLER-------LRDELDIpilYVSHSLdevARL--ADHVVLLEQGRVVASGP 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
648-798 |
8.71e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 72.97 E-value: 8.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 648 VFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSV--------AYVPQQ----AWi 715
Cdd:COG4525 12 RYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPW- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 716 QNAtlKNNIIFGQKrkeswYQRVVEACALQQDLDILPAGDETEIGEKGV-NLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:COG4525 91 LNV--LDNVAFGLR-----LRGVPKAERRARAEELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
....
gi 1357684105 795 AVDA 798
Cdd:COG4525 164 ALDA 167
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1274-1454 |
9.30e-14 |
|
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: 71.74 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGlHELRS 1349
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDAR-EDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1350 RITIIPQDPVLFSG-TLRMNLDpF------DSYSDEDIWKALEFSHLktfvSGLPDKLSHecseggeNLSVGQRQLLCLA 1422
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGL----AGLADLPVR-------QLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|..
gi 1357684105 1423 RALLRKTKVLVLDEATAAVDLETDNLIQSTIR 1454
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
663-848 |
1.36e-13 |
|
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: 72.68 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 663 NVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------------SVAYVPQQ-AWIQNATLKNNI 724
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSfALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 IFG--------QKRKESwYQRVVEACALQQDLDILPagDEteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAV 796
Cdd:cd03294 124 AFGlevqgvprAEREER-AAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 797 DAHVGKHIFDQVIGPQGLLKdKTRILVTHGLS-YLPQADLVLVMVDGEITEIG 848
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQ-KTIVFITHDLDeALRLGDRIAIMKDGRLVQVG 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1274-1492 |
1.42e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDP------------VLFSgtLRMNLDPFDSYSdEDIWKALEfshlktfVSGLPDKLSHEcsegGENLSVGQRQLLCL 1421
Cdd:PRK13648 88 VFQNPdnqfvgsivkydVAFG--LENHAVPYDEMH-RRVSEALK-------QVDMLERADYE----PNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1422 ARALLRKTKVLVLDEATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSP 1492
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
657-846 |
1.66e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 71.62 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG---------SVAY-------VPQQAW-IQNAT 719
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrrigvVFQDFRlLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIF-----GQKRKEswYQRVVEAcALqqdldilpagDETEIGEKG----VNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:COG2884 96 VYENVALplrvtGKSRKE--IRRRVRE-VL----------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 791 DPLSAVDAHVGKHIFDqvigpqgLLKD-----KTRILVTHGLSYLPQADL-VLVMVDGEITE 846
Cdd:COG2884 163 EPTGNLDPETSWEIME-------LLEEinrrgTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1290-1492 |
1.86e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 73.23 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSslTLG--LFRIIEPAEGQISIDGVDIAKLG---LHELRSRITIIPQDPvlfSGT 1364
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKS--TLGrlLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 L--RMNL-----DPFDSYSDED-------IWKALEfshlktfVSGLP----DKLSHECSegGenlsvGQRQLLCLARALL 1426
Cdd:COG4608 108 LnpRMTVgdiiaEPLRIHGLASkaerrerVAELLE-------LVGLRpehaDRYPHEFS--G-----GQRQRIGIARALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1427 RKTKVLVLDEATAAVDLEtdnlIQSTIRSQFED------CTVLTIAHRLNT---IMDytRVLVLDKGQMAE-------FD 1490
Cdd:COG4608 174 LNPKLIVCDEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAVMYLGKIVEiaprdelYA 247
|
..
gi 1357684105 1491 SP 1492
Cdd:COG4608 248 RP 249
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1274-1469 |
2.04e-13 |
|
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: 71.21 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSR--- 1350
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1351 -ITIIPQDPVLFSGTLRMNLdPFDSYSDEDIWKAL-EFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRK 1428
Cdd:cd03290 80 sVAYAAQKPWLLNATVEENI-TFGSPFNKQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1357684105 1429 TKVLVLDEATAAVDLE-TDNLIQSTIRSQFED--CTVLTIAHRL 1469
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKL 202
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
654-853 |
2.46e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.07 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 654 SESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSvAYVPQQAW---------IQN------- 717
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvFQNpdnqfvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 ATLKNNIIFGQKRK----ESWYQRVVEACAL--QQDL-DILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:PRK13650 97 ATVEDDVAFGLENKgiphEEMKERVNEALELvgMQDFkEREPA-----------RLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 791 DPLSAVDAHvGKHIFDQVIgpQGLLKDK--TRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQL 853
Cdd:PRK13650 166 EATSMLDPE-GRLELIKTI--KGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
659-848 |
3.13e-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: 70.64 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYV--------PQQAWIQNATLkNNIIFGQKR 730
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlglgggfnPELTGRENIYL-NGRLLGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 731 KE--SWYQRVVEACALQQDLDiLPAGdeteigekgvNLSGGQKQRV--SLARAVYCDrsVYLLDDPLSAVDAH----VGK 802
Cdd:cd03220 117 KEidEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLafAIATALEPD--ILLIDEVLAVGDAAfqekCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1357684105 803 HIFDQVigpqglLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:cd03220 184 RLRELL------KQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
659-849 |
4.30e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.59 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAV-----------------KGSVAYVPQQAWIQ--NAT 719
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkklkplRKKVGIVFQFPEHQlfEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIFGQK----RKESWYQRVVEACALqqdldilpAGDETEIGEKG-VNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:PRK13634 103 VEKDICFGPMnfgvSEEDAKQKAREMIEL--------VGLPEELLARSpFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 795 AVDAHVGKHI---FDQVIGPQGLlkdkTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK13634 175 GLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1274-1498 |
4.66e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.30 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLD-LAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRIT 1352
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1353 IIPQDP-VLFSGTLRMNLDPFD------SYSD--EDIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLAR 1423
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGlenkgiPHEEmkERVNEALELVGMQDFKEREPARLSG-----------GQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1424 ALLRKTKVLVLDEATAAVD----LETDNLIQStIRSQFeDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDpegrLELIKTIKG-IRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
659-856 |
4.80e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.67 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVPQQ-----------AWIQNATLKNNIIF 726
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAEnrhvntvfqsyALFPHMTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 727 G---QKR-KESWYQRVVEACALQQdLDILpagdeteIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGK 802
Cdd:PRK09452 110 GlrmQKTpAAEITPRVMEALRMVQ-LEEF-------AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 803 HIfdqvigpQGLLKDKTR------ILVTH----GLSylpQADLVLVMVDGEITEIGSYLQLKEE 856
Cdd:PRK09452 182 QM-------QNELKALQRklgitfVFVTHdqeeALT---MSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1291-1499 |
6.25e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.43 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNL- 1369
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 ----DPFDSY----SDED---IWKALEfshlKTFVSGLPDKLShecseggENLSVGQRQLLCLARALLRKTKVLVLDEAT 1438
Cdd:PRK11231 98 aygrSPWLSLwgrlSAEDnarVNQAME----QTRINHLADRRL-------TDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1439 AAVDL----ETDNLIQstiRSQFEDCTVLTIAHRLNTIMDYTRVL-VLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK11231 167 TYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYCDHLvVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
644-844 |
6.41e-13 |
|
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: 69.44 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 644 IEDGVFSWSRSESPTlkRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------SVAYVPQQAWIQ- 716
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaaPPADRPVSMLFQe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 -----NATLKNNIIFGQK---RKESWYQRVVEACALQQDLdilpAGDETEIGEKgvnLSGGQKQRVSLARAVYCDRSVYL 788
Cdd:cd03298 79 nnlfaHLTVEQNVGLGLSpglKLTAEDRQAIEVALARVGL----AGLEKRLPGE---LSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 789 LDDPLSAVDAHVGKHIFDQVIG---PQGLlkdkTRILVTHGLS-YLPQADLVLVMVDGEI 844
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDlhaETKM----TVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
659-853 |
7.83e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.80 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVP---QQAWIQN------ATLKNNIIFGQK 729
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNysllpwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 730 R-----KESWYQRVVEacalqQDLDI--LPAGDETEIGEkgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGK 802
Cdd:TIGR01184 81 RvlpdlSKSERRAIVE-----EHIALvgLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 803 HIFDQvigpqgLLK-----DKTRILVTHGL-SYLPQADLVLVMVDGEITEIGSYLQL 853
Cdd:TIGR01184 152 NLQEE------LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
650-844 |
8.06e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 68.73 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 650 SWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMD--KMEGSVAVKG----------SVAYVPQqawiqn 717
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGrpldkrsfrkIIGYVPQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 atlkNNIIFGQkrkeswyQRVVEACALQQDLdilpagdeteigeKGvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:cd03213 90 ----DDILHPT-------LTVRETLMFAAKL-------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 798 AHVGKHIFDqvigpqgLLKD-----KTRILVTHGLSYL--PQADLVLVMVDGEI 844
Cdd:cd03213 144 SSSALQVMS-------LLRRladtgRTIICSIHQPSSEifELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1281-1442 |
8.51e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1281 LRYR-SDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIA--KLGLHELRSRITIIPQD 1357
Cdd:PRK13639 7 LKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 P--VLFSGTLR-------MNLdpfdSYSDEDIWKALEFSHLKTFVSGLPDKLSHecseggeNLSVGQRQLLCLARALLRK 1428
Cdd:PRK13639 87 PddQLFAPTVEedvafgpLNL----GLSKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVAIAGILAMK 155
|
170
....*....|....
gi 1357684105 1429 TKVLVLDEATAAVD 1442
Cdd:PRK13639 156 PEIIVLDEPTSGLD 169
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
653-799 |
9.70e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 653 RSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------SVAYV-PQQAWIQNATLK 721
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFGQK---RKESWYQRVVEACALQqDLDILPAGdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDA 798
Cdd:PRK13539 92 ENLEFWAAflgGEELDIAAALEAVGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
.
gi 1357684105 799 H 799
Cdd:PRK13539 161 A 161
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1290-1488 |
9.98e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.37 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSltlgLFRII----EPAEGQISIDGVDIAKL---GLHELRSRITIIPQDPVLFS 1362
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKST----LIRCInlleRPTSGRVLVDGQDLTALsekELRKARRQIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 G-------TLRMNLdpfDSYSDEDIWKALEfsHLKTFVsGLPDKLSHECSeggeNLSVGQRQLLCLARALLRKTKVLVLD 1435
Cdd:PRK11153 96 SrtvfdnvALPLEL---AGTPKAEIKARVT--ELLELV-GLSDKADRYPA----QLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1436 EATAAVDLETDNLIQSTIRSQFED--CTVLTIAHRlntiMDYT-----RVLVLDKGQMAE 1488
Cdd:PRK11153 166 EATSALDPATTRSILELLKDINRElgLTIVLITHE----MDVVkricdRVAVIDAGRLVE 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
659-876 |
1.05e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSaLLGEMDK-MEGSVAVKGsvayvpqqawiQNATLKNNIIFGQKRKESW--- 734
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAG-----------QDVATLDADALAQLRREHFgfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 735 YQR--VVEACALQQDLDIlPA---------------------GDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:PRK10535 92 FQRyhLLSHLTAAQNVEV-PAvyaglerkqrllraqellqrlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 792 PLSAVDAHVGKhifdQVIGPQGLLKDK--TRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFLRTYAS 869
Cdd:PRK10535 171 PTGALDSHSGE----EVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTASG 246
|
....*..
gi 1357684105 870 SEQTDGS 876
Cdd:PRK10535 247 WRQFVSG 253
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
655-849 |
1.08e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.46 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG---------------SVAYVPQQAWIQ--N 717
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPEYQlfE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 ATLKNNIIFGQKR----KESWYQRVVEAcalqqdLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:PRK13637 99 ETIEKDIAFGPINlglsEEEIENRVKRA------MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 794 SAVDAHVGKHIFDQVigpQGLLKDK--TRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK13637 173 AGLDPKGRDEILNKI---KELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
655-844 |
1.09e-12 |
|
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: 69.00 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--------------VAYVPQ-QAWIQNAT 719
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIFG-QKRKESWYQRVVEACalqqdLDILPAGDETEiGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDP---LSA 795
Cdd:cd03224 92 VEENLLLGaYARRRAKRKARLERV-----YELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 796 VdahVGKHIFDQVIGpqglLKDK--TRILVTHGLSY-LPQADLVLVMVDGEI 844
Cdd:cd03224 166 K---IVEEIFEAIRE----LRDEgvTILLVEQNARFaLEIADRAYVLERGRV 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1288-1496 |
1.16e-12 |
|
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: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1288 DLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAklGLHELRSRITIIPQDPVLFSgtlRM 1367
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFP---HM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1368 NldpfdsysdedIWKALEFSHLKTFVSGLPDK-----------LSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDE 1436
Cdd:cd03299 87 T-----------VYKNIAYGLKKRKVDKKEIErkvleiaemlgIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1437 ATAAVDLET-DNLIQ--STIRSQFeDCTVLTIAHRLNTI-MDYTRVLVLDKGQMAEFDSPSSLI 1496
Cdd:cd03299 156 PFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
657-798 |
1.91e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 68.20 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVPQQA----------------WIQNAT 719
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIF-----GQKRKEsWYQRVVEACA---LQQDLDILPAGdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:cd03292 95 VYENVAFalevtGVPPRE-IRKRVPAALElvgLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADE 162
|
....*..
gi 1357684105 792 PLSAVDA 798
Cdd:cd03292 163 PTGNLDP 169
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1291-1493 |
2.10e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.03 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVL-FSGT----L 1365
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveevV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1366 RMNLDPFDSYSDED---IWKALEfshlKTFVSGLPDKLSHECSeGGENlsvgQR--------QllclARALLRKTKVLVL 1434
Cdd:PRK13548 98 AMGRAPHGLSRAEDdalVAAALA----QVDLAHLAGRDYPQLS-GGEQ----QRvqlarvlaQ----LWEPDGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1435 DEATAAVDL----ETDNLIQSTIRSQfeDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPS 1493
Cdd:PRK13548 165 DEPTSALDLahqhHVLRLARQLAHER--GLAVIVVLHDLNLAARYAdRIVLLHQGRLVADGTPA 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1290-1484 |
2.44e-12 |
|
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: 68.51 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGlHELRSRITIIpqdpvlFS--GTLRM 1367
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR-KKFLRRIGVV------FGqkTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1368 NLDPFDSYS-DEDIWKaLEFSHLKTFVSGLPD--KLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLE 1444
Cdd:cd03267 109 DLPVIDSFYlLAAIYD-LPPARFKKRLDELSEllDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1357684105 1445 TDNLIQSTIRSQFED--CTVLTIAHRLNTIMDY-TRVLVLDKG 1484
Cdd:cd03267 188 AQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKG 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
639-842 |
2.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 639 AYSISIEDGVFSWsRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQN- 717
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 --------------ATLKNNIIFGQK----RKESWYQRVVEAcalqqdldiLPAGDETEIGEKG-VNLSGGQKQRVSLAR 778
Cdd:PRK13647 81 vglvfqdpddqvfsSTVWDDVAFGPVnmglDKDEVERRVEEA---------LKAVRMWDFRDKPpYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 779 AVYCDRSVYLLDDPLSAVDAHvGKH----IFDqVIGPQGllkdKTRILVTHGLSYLPQ-ADLVLVMVDG 842
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPR-GQEtlmeILD-RLHNQG----KTVIVATHDVDLAAEwADQVIVLKEG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1274-1486 |
2.70e-12 |
|
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: 67.69 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG--VDIAKlglhelRSRI 1351
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1352 TIIP-----------QDPVLFSGTLRmNLDPFDSYSDEDIWkalefshLKTFvsglpdKLSHECSEGGENLSVGQRQLLC 1420
Cdd:cd03269 73 GYLPeerglypkmkvIDQLVYLAQLK-GLKKEEARRRIDEW-------LERL------ELSEYANKRVEELSKGNQQKVQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1421 LARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFED-CTVLTIAHRLNTIMDY-TRVLVLDKGQM 1486
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
950-1245 |
2.77e-12 |
|
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: 69.38 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 950 AIGVLLSAISLLFflshnllsMFANYWLSLWTDDPVVNGTQPDRLMRLGVyGGLGVSQGVAVFGYsLSVSIGGILASRFL 1029
Cdd:cd18542 2 LLAILALLLATAL--------NLLIPLLIRRIIDSVIGGGLRELLWLLAL-LILGVALLRGVFRY-LQGYLAEKASQKVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1030 HQ--SMLFDVL-RSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILV-----ATPMVAFIIP 1101
Cdd:cd18542 72 YDlrNDLYDHLqRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSinwklTLISLAIIPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1102 FLGLLYFF---VQRFYVASSRQLKRLESVsrspiythFNETLLGTSVIRAFG----EQERFIHESDQRVDHNQKA----- 1169
Cdd:cd18542 152 IALFSYVFfkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFAredyEIEKFDKENEEYRDLNIKLaklla 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1170 -YYPSIvanrwlairlEFVGNC----IVSFAALFAVlaRENLSPGIMGLSISYALQltasLTWLVRMS----SDVETNIV 1240
Cdd:cd18542 224 kYWPLM----------DFLSGLqivlVLWVGGYLVI--NGEITLGELVAFISYLWM----LIWPVRQLgrliNDMSRASA 287
|
....*
gi 1357684105 1241 AVERV 1245
Cdd:cd18542 288 SAERI 292
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
659-848 |
2.83e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSA--LLGEMDKME---GSVAVKGSVAYVPQQAWI-----------QN----- 717
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTirvGDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 -ATLKNNIIFG--QKRKESWYQRVVEACALQQDLDIlpAGDETEIGEKgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:PRK11264 99 hRTVLENIIEGpvIVKGEPKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 795 AVDAHVGKHIFDQVigpQGLLKDK-TRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:PRK11264 174 ALDPELVGEVLNTI---RQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
659-799 |
3.15e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 67.68 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLG--EMDKM-EGSVAVKG----------SVAYVPQQ-AWIQNATLKNNI 724
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvEGGGTtSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 IF-----GQKRKESWYQRVVEACALQQDLDILPAGdeteiGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAH 799
Cdd:cd03234 103 TYtailrLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1291-1483 |
3.25e-12 |
|
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: 68.73 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGvdiaklglhelrsRITIIPQDPVLFSGTLRMNLD 1370
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1371 ---PFDSYSDEDIWKALEfshLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDN 1447
Cdd:cd03291 120 fgvSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1357684105 1448 LIqstirsqFEDCTVLTIAHRlntimdyTRVLVLDK 1483
Cdd:cd03291 197 EI-------FESCVCKLMANK-------TRILVTSK 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
662-847 |
3.62e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRvpEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--------------VAYVP----QQAWIQNATLKNN 723
Cdd:COG1129 273 FSVR--AGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDLSIREN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 II---------FG--QKRKEswyQRVVEAcaLQQDLDILPAGDETEIGekgvNLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:COG1129 351 ITlasldrlsrGGllDRRRE---RALAEE--YIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 793 LSAVDahVG-KH-IFDqvigpqgLLKDKTR-----ILVThglSYLPQ----ADLVLVMVDGEITEI 847
Cdd:COG1129 422 TRGID--VGaKAeIYR-------LIRELAAegkavIVIS---SELPEllglSDRILVMREGRIVGE 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
642-864 |
3.98e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSW-SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALL------------------GEMDKM------ 696
Cdd:PTZ00265 1166 IEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtNDMTNEqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 697 -EGSVAVKGSVAY------------------------------------------VPQQAWIQNATLKNNIIFGqkRKES 733
Cdd:PTZ00265 1246 eEQNVGMKNVNEFsltkeggsgedstvfknsgkilldgvdicdynlkdlrnlfsiVSQEPMLFNMSIYENIKFG--KEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 734 WYQRVVEAC---ALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIG 810
Cdd:PTZ00265 1324 TREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 811 PQGlLKDKTRILVTHGLSYLPQADLVLVMVDGEITeiGSYLQlkeEEGAFAEFL 864
Cdd:PTZ00265 1404 IKD-KADKTIITIAHRIASIKRSDKIVVFNNPDRT--GSFVQ---AHGTHEELL 1451
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1285-1481 |
4.16e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1285 SDLDLAIRNinvdisgGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVL---F 1361
Cdd:PRK09536 20 DGVDLSVRE-------GSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1362 SG--TLRMNLDP----FDSYSDED---IWKALEFSHLKTFVSGLPDKLShecseGGEnlsvgqRQLLCLARALLRKTKVL 1432
Cdd:PRK09536 93 DVrqVVEMGRTPhrsrFDTWTETDraaVERAMERTGVAQFADRPVTSLS-----GGE------RQRVLLARALAQATPVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1433 VLDEATAAVDL----ETDNLIQSTIRsqfEDCTVLTIAHRLNTIMDYTRVLVL 1481
Cdd:PRK09536 162 LLDEPTASLDInhqvRTLELVRRLVD---DGKTAVAAIHDLDLAARYCDELVL 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1293-1499 |
4.40e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.70 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1293 NINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDI----AKLGLHELRSRITIIPQDP--VLFSGTLR 1366
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPeaQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNLD--P--FDSYSDEDIWKALEFshLKTFvsGLPDKLShecSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVD 1442
Cdd:PRK13641 105 KDVEfgPknFGFSEDEAKEKALKW--LKKV--GLSEDLI---SKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1443 LET-DNLIQSTIRSQFEDCTVLTIAHRLNTIMDYTR-VLVLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK13641 178 PEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
659-844 |
4.51e-12 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 67.77 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------------SVAYVPQQ-AWIQNATLK 721
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrRIGMIFQQfNLVPRLSVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFGQKRKESWYQRVV---------EACALQQDLDILP-AGDETEigekgvNLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:COG3638 99 TNVLAGRLGRTSTWRSLLglfppedreRALEALERVGLADkAYQRAD------QLSGGQQQRVAIARALVQEPKLILADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 792 PLSAVDAHVGKHIFDqvigpqgLLKD------KTRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:COG3638 173 PVASLDPKTARQVMD-------LLRRiaredgITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1290-1442 |
4.62e-12 |
|
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: 70.48 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIePAEGQISIDGVDIAKLGLHE---LRSRITIIPQDPvlFsGTL- 1365
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP--F-GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1366 -RMN-----------LDPFDSYSDED--IWKALEFSHLKtfvsglPDKLS---HECSeGgenlsvGQRQLLCLARALLRK 1428
Cdd:COG4172 377 pRMTvgqiiaeglrvHGPGLSAAERRarVAEALEEVGLD------PAARHrypHEFS-G------GQRQRIAIARALILE 443
|
170
....*....|....
gi 1357684105 1429 TKVLVLDEATAAVD 1442
Cdd:COG4172 444 PKLLVLDEPTSALD 457
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1292-1485 |
8.63e-12 |
|
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: 66.01 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDI--AKLGLHELRSRITIIPQDPVLFSgtlrmNL 1369
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP-----HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 DPFDSYSDEDIW---------KALEFSHLKtfVSGLPDKLSHECSEggenLSVGQRQLLCLARALLRKTKVLVLDEATAA 1440
Cdd:cd03262 92 TVLENITLAPIKvkgmskaeaEERALELLE--KVGLADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1441 VDLETDNLIQSTIRSQFED-CTVLTIAHRlntiMDY-----TRVLVLDKGQ 1485
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEgMTMVVVTHE----MGFarevaDRVIFMDDGR 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1289-1511 |
8.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.42 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1289 LAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG-LHELRSRITIIPQDP--------- 1358
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1359 ---VLFsGTLRMNLDPfdsysdEDIWKALEFSHLKTFVSGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVLD 1435
Cdd:PRK13633 104 eedVAF-GPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHL-------LSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1436 EATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQkgafYRMAKDAGL 1511
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE----VEMMKKIGL 243
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1031-1245 |
9.81e-12 |
|
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: 67.45 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1031 QSMLFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCV-----------IILVATPMVAF 1098
Cdd:cd18552 75 RNDLFDkLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGvlfyldwkltlIALVVLPLAAL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1099 IIpflgllYFFVQRFYVASSRQLKRLESVSrspiyTHFNETLLGTSVIRAFG----EQERFIHESDQRVDHNQKayypsI 1174
Cdd:cd18552 155 PI------RRIGKRLRKISRRSQESMGDLT-----SVLQETLSGIRVVKAFGaedyEIKRFRKANERLRRLSMK-----I 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1175 VANRWLAIRL-EFVGNCIVSFAALFA---VLArENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18552 219 ARARALSSPLmELLGAIAIALVLWYGgyqVIS-GELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1293-1498 |
1.28e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.93 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1293 NINVDISGGEKVGIVGRTGAGKSSLtLGL---FriIEPAEGQISIDGVDIAKLGLHElrsR-ITIIPQDPVLFSG-TLRM 1367
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTL-LNLiagF--LPPDSGRILWNGQDLTALPPAE---RpVSMLFQENNLFPHlTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1368 N----LDPFDSYSDED---IWKALEfshlKTfvsGLPDKLSHECSEggenLSVGQRQLLCLARALLRKTKVLVLDEATAA 1440
Cdd:COG3840 91 NiglgLRPGLKLTAEQraqVEQALE----RV---GLAGLLDRLPGQ----LSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1441 VD----LETDNLIQSTIRSQfeDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:COG3840 160 LDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIAdRVLLVADGRIAADGPTAALLDG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
658-849 |
1.29e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.72 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 658 TLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALlGEMDKMEGSVAVKGSVAY---------------------VPQQAWIQ 716
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 NATLKNNIIFGQKRKESWYQRVVEAcALQQDLDILPAGDETE--IGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 795 AVDAHVGKHIFDQVIGpqglLKDK-TRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK14239 178 ALDPISAGKIEETLLG----LKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1290-1511 |
1.34e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.13 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSS---LTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDP-VLFSGtl 1365
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPdNQFVG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1366 rmnldpfdSYSDEDIWKALE-----FSHLKTFVS------GLPDKLSHECSeggeNLSVGQRQLLCLARALLRKTKVLVL 1434
Cdd:PRK13640 100 --------ATVGDDVAFGLEnravpRPEMIKIVRdvladvGMLDYIDSEPA----NLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1435 DEATAAVDLETDNLIQSTIRSQFED--CTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIAQKgafyRMAKDAGL 1511
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV----EMLKEIGL 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
659-848 |
1.45e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.47 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL-----LGEMDKMEGSVAVKGS----------------VAYVPQQawIQN 717
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQdifkmdvielrrrvqmVFQIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 ATLKNNIIFGQK------RKESWYQRVVEACALQQDLDILpagdETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:PRK14247 97 LSIFENVALGLKlnrlvkSKKELQERVRWALEKAQLWDEV----KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 792 PLSAVDAHVGKHIFDQVIgpqGLLKDKTRILVTHglsYLPQA----DLVLVMVDGEITEIG 848
Cdd:PRK14247 173 PTANLDPENTAKIESLFL---ELKKDMTIVLVTH---FPQQAarisDYVAFLYKGQIVEWG 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1291-1506 |
1.69e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.22 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGV------DIAKLGLHELRSRITIIPQDPVLFSG- 1363
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 TLRMNLD-PFDSYSDED---IWKALEFSHLKTfvsGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATA 1439
Cdd:PRK14246 106 SIYDNIAyPLKSHGIKEkreIKKIVEECLRKV---GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1440 AVDLETDNLIQSTIRSQFEDCTVLTIAH---RLNTIMDYtrVLVLDKGQMAE-------FDSPSSLIAQKGAFYRMA 1506
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEwgssneiFTSPKNELTEKYVIGRIS 257
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
642-846 |
1.78e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.66 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSR-SESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSvAYVPQQAW------ 714
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 ---IQN-------ATLKNNIIFGQKR----KESWYQRVVEACALQQDLDILPagdeteigEKGVNLSGGQKQRVSLARAV 780
Cdd:PRK13642 84 gmvFQNpdnqfvgATVEDDVAFGMENqgipREEMIKRVDEALLAVNMLDFKT--------REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 781 YCDRSVYLLDDPLSAVDAhVGKHIFDQVIGPqglLKDK---TRILVTHGLSYLPQADLVLVMVDGEITE 846
Cdd:PRK13642 156 ALRPEIIILDESTSMLDP-TGRQEIMRVIHE---IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
659-862 |
1.87e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 66.42 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLgEMDKMEGSVAVKG-------------SVAYVPQQAWIQNATLKNNI- 724
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 IFGQ-KRKESWyqRVVEACALQQDLDILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAhvgkh 803
Cdd:cd03289 99 PYGKwSDEEIW--KVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP----- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 804 IFDQVIgpQGLLK----DKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAE 862
Cdd:cd03289 172 ITYQVI--RKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1290-1499 |
1.94e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.73 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDI-AKLG---LHELRSRITIIPQDP--VLFSG 1363
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQFPesQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 TL-----------RMNLDPFDSYSdEDIWKALEFShlKTFVSGLPDKLSHecseggenlsvGQRQLLCLARALLRKTKVL 1432
Cdd:PRK13646 102 TVereiifgpknfKMNLDEVKNYA-HRLLMDLGFS--RDVMSQSPFQMSG-----------GQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1433 VLDEATAAVDLETDNLIQSTIRS-QFEDC-TVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYAdEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-849 |
2.22e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.84 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 643 SIEDgVFSWSR-----SESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQN 717
Cdd:PRK14246 6 SAED-VFNISRlylyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 A--------------------TLKNNIIFGQK----RKESWYQRVVEACalqqdldILPAGDETEIGEK----GVNLSGG 769
Cdd:PRK14246 85 AiklrkevgmvfqqpnpfphlSIYDNIAYPLKshgiKEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 770 QKQRVSLARAVYCDRSVYLLDDPLSAVDAhVGKHIFDQVIGPqgLLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITE--LKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWG 234
|
.
gi 1357684105 849 S 849
Cdd:PRK14246 235 S 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1290-1488 |
2.22e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 65.45 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSL--TLGLfrIIEPAEGQISIDGVDIAKLGLHEL----RSRITIIPQD------ 1357
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFfnllpe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 ---------PVLFSGTLRmnldpfdsysDEDIWKALEFshLKTFvsGLPDKLSHECSEggenLSVGQRQLLCLARALLRK 1428
Cdd:COG1136 101 ltalenvalPLLLAGVSR----------KERRERAREL--LERV--GLGDRLDHRPSQ----LSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1429 TKVLVLDEATAAVDLETD----NLIQSTIRSQfeDCTVLTIAH--RLNTIMDytRVLVLDKGQMAE 1488
Cdd:COG1136 163 PKLILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHdpELAARAD--RVIRLRDGRIVS 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
661-805 |
2.29e-11 |
|
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: 68.62 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 661 RLNVRVPEGSLVAVVGHVGSGKSSLLSaLLGEMDKMEG---SVAVKGSVAYVPQQAWIQNATLKNNIIFgQKRKESWYQR 737
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY-PDSSEDMKRR 547
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 738 VVEACALQQDLDILPAGD--ETEIGEKGVN-----LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIF 805
Cdd:TIGR00954 548 GLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1290-1488 |
2.41e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 65.83 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGLHEL------RS--RITIIPQD 1357
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDITGLPPHRIarlgiaRTfqNPRLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 PVL----------FSGTLRMNLDPFDSYSDEDIW---KALEfsHLKTFvsGLPDKLSHECSeggeNLSVGQRQLLCLARA 1424
Cdd:COG0411 95 TVLenvlvaaharLGRGLLAALLRLPRARREEREareRAEE--LLERV--GLADRADEPAG----NLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1425 LLRKTKVLVLDEATAAVDL-ETDNLIQsTIRS--QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQM-AE 1488
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLAdRIVVLDFGRViAE 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1291-1483 |
2.99e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.33 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIdgvdiaklglHElRSRITIIPQDPVLFSGTLR 1366
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGM----------PE-GEDLLFLPQRPYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNLdpfdSYSdediWkalefshlktfvsglpdklshecsegGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETD 1446
Cdd:cd03223 82 EQL----IYP----W--------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*....
gi 1357684105 1447 NLIQSTIRSQFedCTVLTIAHR--LNTImdYTRVLVLDK 1483
Cdd:cd03223 128 DRLYQLLKELG--ITVISVGHRpsLWKF--HDRVLDLDG 162
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
649-827 |
3.03e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.44 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 649 FSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALlGEMDKMEGSVAVKGSVAYVPQQAWIQNATLK------- 721
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLNrlrrqvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 --------------NNIIFGQKRKeSWYQRV-----VEACALQQDLdilpaGDETE--IGEKGVNLSGGQKQRVSLARAV 780
Cdd:PRK14258 92 mvhpkpnlfpmsvyDNVAYGVKIV-GWRPKLeiddiVESALKDADL-----WDEIKhkIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1357684105 781 YCDRSVYLLDDPLSAVDAHVGKHIfDQVIGPQGLLKDKTRILVTHGL 827
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNL 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
661-844 |
3.11e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 661 RLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--VAYVPQQAWIQ----------NATLKNNIIFG- 727
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVSmlfqennlfsHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 728 ---------QKRKeswYQRVVEACALQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDA 798
Cdd:PRK10771 97 npglklnaaQREK---LHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 799 HVGKHIF---DQVIGPQGLlkdkTRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:PRK10771 163 ALRQEMLtlvSQVCQERQL----TLLMVSHSLEDAARiAPRSLVVADGRI 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
659-846 |
3.30e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.84 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSaLLGEMDK-MEGSVAVKGSVayVPQQAWIQNATLKNN-------------- 723
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNGQP--MSKLSSAAKAELRNQklgfiyqfhhllpd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 -----------IIFGQKRKEswyqrvveacALQQDLDILPA-GDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:PRK11629 102 ftalenvamplLIGKKKPAE----------INSRALEMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 792 PLSAVDAHVGKHIFdQVIGPQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITE 846
Cdd:PRK11629 172 PTGNLDARNADSIF-QLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
659-853 |
3.91e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 66.25 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLS--ALLGEMDkmEGSVAVKG----------------SVAYVPQQ-AWIQNAT 719
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRciNLLERPT--SGSVLVDGvdltalserelraarrKIGMIFQHfNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIF-----GQKRKESWyQRVVEacaLqqdLDIlpagdeTEIGEKG----VNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:COG1135 99 VAENVALpleiaGVPKAEIR-KRVAE---L---LEL------VGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 791 DPLSAVDAHVGKHIFDqvigpqgLLKD------KTRILVTHglsylpQ-------ADLVLVMVDGEITEIGSYLQL 853
Cdd:COG1135 166 EATSALDPETTRSILD-------LLKDinrelgLTIVLITH------EmdvvrriCDRVAVLENGRIVEQGPVLDV 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1274-1497 |
3.93e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDL-AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRIT 1352
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1353 IIPQDP-VLFSGTLRMNLDPF----DSYSDEDIWKALEFSHLKTfvsglpDKLSHECSEGGEnLSVGQRQLLCLARALLR 1427
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAV------NMLDFKTREPAR-LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1428 KTKVLVLDEATAAVDLETDNLIQSTIRsQFED---CTVLTIAHRLNTIMDYTRVLVLDKGQMAEFDSPSSLIA 1497
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
660-853 |
4.65e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 660 KRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAV-----------KGSVAYVPQQ-AWIQNATLKNNIIFG 727
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrmndvppaERGVGMVFQSyALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 728 QK----RKESWYQRVveacalQQDLDILPAGDETEIGEKGvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKH 803
Cdd:PRK11000 100 LKlagaKKEEINQRV------NQVAEVLQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 804 IFDQVIGPQGLLKdKTRILVTHG-LSYLPQADLVLVMVDGEITEIGSYLQL 853
Cdd:PRK11000 172 MRIEISRLHKRLG-RTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
666-846 |
4.77e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.42 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 666 VPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------------------------SVAYVPQQAWIQNATLK 721
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakhvgfvfqSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NnIIFGQKRKESWYQRV--VEACALQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAvYCDRSVYLL-DDPLSAVDA 798
Cdd:PRK10584 113 A-LLRGESSRQSRNGAKalLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARA-FNGRPDVLFaDEPTGNLDR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 799 HVGKHIFDQVIgpqGLLKD--KTRILVTHGLSYLPQADLVLVMVDGEITE 846
Cdd:PRK10584 180 QTGDKIADLLF---SLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
652-826 |
5.46e-11 |
|
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: 63.53 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 652 SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------------SVAYVPQQAWIQNA- 718
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIFGQkRKESWYQRVVEAcALQQ----DLDILPAGdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:TIGR01189 89 SALENLHFWA-AIHGGAQRTIED-ALAAvgltGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1357684105 795 AVDAH-VGK--HIFDQVIGPQGLLkdktrILVTHG 826
Cdd:TIGR01189 157 ALDKAgVALlaGLLRAHLARGGIV-----LLTTHQ 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
650-849 |
5.50e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.79 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 650 SWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWIQ 716
Cdd:PRK13548 9 SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 NATLKNNII------FGQKRKESwyQRVVEAcALQQ-DLDILPAGDETEigekgvnLSGGQKQRVSLARA---VYCD--- 783
Cdd:PRK13548 89 FPFTVEEVVamgrapHGLSRAED--DALVAA-ALAQvDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqLWEPdgp 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 784 RSVYLLDDPLSAVD-AHvGKHIFDqvigpqgLLKDKTR------ILVTHGLS----YlpqADLVLVMVDGEITEIGS 849
Cdd:PRK13548 159 PRWLLLDEPTSALDlAH-QHHVLR-------LARQLAHerglavIVVLHDLNlaarY---ADRIVLLHQGRLVADGT 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
659-848 |
7.10e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.48 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL-----LGEMDKMEGSVAVKGSVAYVPQQAWIQ----------------N 717
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 ATLKNNIIFGQK------RKESWYQRV---VEACALQQDLdilpagdETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYL 788
Cdd:PRK14267 100 LTIYDNVAIGVKlnglvkSKKELDERVewaLKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 789 LDDPLSAVDAhVGKHIFDQVIGPqgLLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:PRK14267 173 MDEPTANIDP-VGTAKIEELLFE--LKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
662-849 |
7.28e-11 |
|
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: 65.46 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLG---EMDKMEGSVAVKGS-----------------VAYVPQQAwiQNA--- 718
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDP--MTSlnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 --TLKNNI-----IFGQKRKESWYQRVVEAcalqqdLDI--LPAGDETeigekgVN-----LSGGQKQRVSLARAVYCDR 784
Cdd:COG0444 102 vmTVGDQIaeplrIHGGLSKAEARERAIEL------LERvgLPDPERR------LDrypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGLS---YLpqADLVLVMVDGEITEIGS 849
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQILN-------LLKDLQRelglaiLFITHDLGvvaEI--ADRVAVMYAGRIVEEGP 234
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
950-1245 |
9.74e-11 |
|
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: 64.73 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 950 AIGVLLSAISllfflshNLLSMFANYWLSLWTD---DPVVNGTQPD--RLMR-LGVYGGLGVSQGVAVFGYS-LSVSIGg 1022
Cdd:cd18547 2 ILVIILAIIS-------TLLSVLGPYLLGKAIDliiEGLGGGGGVDfsGLLRiLLLLLGLYLLSALFSYLQNrLMARVS- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1023 ilasrflhQSMLFDvLRS---------PMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVAT 1093
Cdd:cd18547 74 --------QRTVYD-LRKdlfeklqrlPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYIS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1094 P----MVAFIIPFLGLLYFFV----QRFYVASSRQLKRLESvsrspiytHFNETLLGTSVIRAFGEQERFIHESDQrvdH 1165
Cdd:cd18547 145 PlltlIVLVTVPLSLLVTKFIakrsQKYFRKQQKALGELNG--------YIEEMISGQKVVKAFNREEEAIEEFDE---I 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1166 NQKAYYPSIVANRWLAIR---LEFVGN----CIVSFAALFAVlaRENLSPGIMGLSISYALQLTASLTWLVRMSSDVETN 1238
Cdd:cd18547 214 NEELYKASFKAQFYSGLLmpiMNFINNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSA 291
|
....*..
gi 1357684105 1239 IVAVERV 1245
Cdd:cd18547 292 LAGAERV 298
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1290-1498 |
1.24e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.56 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSL--TLGlfRIIEPAEGQISIDGvDIAKL-----GLH-ELRSRitiipqDPVLF 1361
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlkLIA--GILEPTSGRVEVNG-RVSALlelgaGFHpELTGR------ENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1362 SGT-LRMNLDPFDSYSDEdIwkaLEFSHL--------KTFVSGL-------------PDklshecseggenlsvgqrqll 1419
Cdd:COG1134 112 NGRlLGLSRKEIDEKFDE-I---VEFAELgdfidqpvKTYSSGMrarlafavatavdPD--------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1420 clarallrktkVLVLDEATAAVDLE----TDNLIQSTIRsqfEDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSS 1494
Cdd:COG1134 167 -----------ILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
....
gi 1357684105 1495 LIAQ 1498
Cdd:COG1134 233 VIAA 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
659-849 |
1.31e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------SVAYVPQQAWI--QNA-------TLK 721
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIvfQNPddqlfapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFGQKR----KESWYQRVVEACAlqqdldilpagdetEIGEKGV------NLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:PRK13639 98 EDVAFGPLNlglsKEEVEKRVKEALK--------------AVGMEGFenkpphHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 792 PLSAVDahvgkhifdqvigPQG------LLKD-----KTRILVTHGLSYLP-QADLVLVMVDGEITEIGS 849
Cdd:PRK13639 164 PTSGLD-------------PMGasqimkLLYDlnkegITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1274-1467 |
1.40e-10 |
|
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: 62.87 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLD--LAIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAklglhEL 1347
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIagleRPTSGEVLVDGEPVT-----GP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1348 RSRITIIPQDPVLFS----------GtLRMNLDPfDSYSDEDIWKALEFSHLKTFVSGLPdklsHEcseggenLSVGQRQ 1417
Cdd:cd03293 72 GPDRGYVFQQDALLPwltvldnvalG-LELQGVP-KAEARERAEELLELVGLSGFENAYP----HQ-------LSGGMRQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1418 LLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDC--TVLTIAH 1467
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1283-1498 |
1.41e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1283 YRSDLDlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDP--VL 1360
Cdd:PRK13652 13 YSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1361 FSGTLRMNL--DPFDSYSDEDIWKALEFSHLKTF-VSGLPDKLSHecseggeNLSVGQRQLLCLARALLRKTKVLVLDEA 1437
Cdd:PRK13652 92 FSPTVEQDIafGPINLGLDEETVAHRVSSALHMLgLEELRDRVPH-------HLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1438 TAAVDLETDNLIQSTIRSQFED--CTVLTIAHRLNTI---MDYtrVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpemADY--IYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
659-845 |
1.50e-10 |
|
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: 61.29 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYV--PQQAWiqnatlKNNIifgqkrkeswyq 736
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFasPRDAR------RAGI------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 737 rvveACALQqdldilpagdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVigpqGLLK 816
Cdd:cd03216 78 ----AMVYQ--------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLR 129
|
170 180 190
....*....|....*....|....*....|..
gi 1357684105 817 D--KTRILVTHGLSYLPQ-ADLVLVMVDGEIT 845
Cdd:cd03216 130 AqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
659-849 |
1.56e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.09 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL--LGEMDkmEGSVAVKG---------------SVAYVPQQ--------A 713
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGedltdskkdinklrrKVGMVFQQfnlfphltV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 714 wIQNATLKNNIIFGQKRKEswyqrvveacALQQDLDILpagDETEIGEKG----VNLSGGQKQRVSLARAVYCDRSVYLL 789
Cdd:COG1126 95 -LENVTLAPIKVKKMSKAE----------AEERAMELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 790 DDPLSAVD----AHVGkhifdQVIgpQGLLKDK-TRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:COG1126 161 DEPTSALDpelvGEVL-----DVM--RDLAKEGmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
956-1416 |
2.40e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.82 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 956 SAISLLFFLSHNLLSMFANYWLsLWTDDPVVNGTQPDRLMRLGVYGGLgvsqgVAVFGYSLSVSigGILASRFLHQSM-- 1033
Cdd:COG4615 11 SRWLLLLALLLGLLSGLANAGL-IALINQALNATGAALARLLLLFAGL-----LVLLLLSRLAS--QLLLTRLGQHAVar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 ----LFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIdSLIPMILKMFMGSLFNVLGSCV-IILVATPMVAFIIPFLGLLy 1107
Cdd:COG4615 83 lrlrLSRrILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAyLAWLSPPLFLLTLVLLGLG- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1108 FFVQRFYVASSRQLKRLESVSRSPIYTHFnetllgTSVIRAFGEQ-------ERF----IHESDQRV-DHNQKAYYPSIV 1175
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHF------RALLEGFKELklnrrrrRAFfdedLQPTAERYrDLRIRADTIFAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1176 ANRWlairlefvGNCIVsFAA----LFAVLARENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERVKEYS-- 1249
Cdd:COG4615 235 ANNW--------GNLLF-FALigliLFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELEla 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1250 -DTEKEAEWRHEPPTVPPDWpteGCIHITNFGLRYRSDLD---LAIRNINVDISGGEKVGIVGRTGAGKSSLT---LGLF 1322
Cdd:COG4615 306 lAAAEPAAADAAAPPAPADF---QTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLAkllTGLY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1323 RiiePAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSgtlrmNLDPFDSYSDEDiwKALEfsHLKTFvsglpdKLSH 1402
Cdd:COG4615 383 R---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-----RLLGLDGEADPA--RARE--LLERL------ELDH 444
|
490
....*....|....*....
gi 1357684105 1403 ECS-EGGE----NLSVGQR 1416
Cdd:COG4615 445 KVSvEDGRfsttDLSQGQR 463
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
659-844 |
2.94e-10 |
|
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: 62.20 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV----------------AVKGSVAYVPQQ-AWIQNATLK 721
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrQLRRQIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFGQKRKESWYQ---------RVVEACALQQDLDILpagdetEIGEKGV-NLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:cd03256 97 ENVLSGRLGRRSTWRslfglfpkeEKQRALAALERVGLL------DKAYQRAdQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 792 PLSAVD---AHvgkhifdQVIgpqGLLKDKTR------ILVTHGLSY-LPQADLVLVMVDGEI 844
Cdd:cd03256 171 PVASLDpasSR-------QVM---DLLKRINReegitvIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
659-792 |
2.96e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--SVAYVPQQAWI-QNATLKNNIIFG-------Q 728
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLdDDLTVLDTVLDGdaelralE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 729 KRKESWYQRVVEACA-------LQQDLDILPAGD-ETEIGE--KGV------------NLSGGQKQRVSLARAVYCDRSV 786
Cdd:COG0488 94 AELEELEAKLAEPDEdlerlaeLQEEFEALGGWEaEARAEEilSGLgfpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
....*.
gi 1357684105 787 YLLDDP 792
Cdd:COG0488 174 LLLDEP 179
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1274-1498 |
3.26e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLDLA-------IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKL---G 1343
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1344 LHELRSRITIIPQDPV-----------LFSGTLR--MNLDPfdsysDEDIWKALEFSHLKTFVSGLPDKLSHEcseggen 1410
Cdd:PRK10419 84 RKAFRRDIQMVFQDSIsavnprktvreIIREPLRhlLSLDK-----AERLARASEMLRAVDLDDSVLDKRPPQ------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1411 LSVGQRQLLCLARALLRKTKVLVLDEATAAVDLetdnLIQSTIRSQFED------CTVLTIAHRLNTIMDY-TRVLVLDK 1483
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDL----VLQAGVIRLLKKlqqqfgTACLFITHDLRLVERFcQRVMVMDN 227
|
250 260
....*....|....*....|....
gi 1357684105 1484 GQMAE---------FDSPSSLIAQ 1498
Cdd:PRK10419 228 GQIVEtqpvgdkltFSSPAGRVLQ 251
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1274-1442 |
3.29e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRsDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITI 1353
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDP--VLFSGT---------LRMNLDPfdSYSDEDIWKALEFSHLKTFvsglPDKLSHecseggeNLSVGQRQLLCLA 1422
Cdd:PRK13647 84 VFQDPddQVFSSTvwddvafgpVNMGLDK--DEVERRVEEALKAVRMWDF----RDKPPY-------HLSYGQKKRVAIA 150
|
170 180
....*....|....*....|
gi 1357684105 1423 RALLRKTKVLVLDEATAAVD 1442
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLD 170
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
655-844 |
3.44e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.92 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-----------------SVAYV---PQQAW 714
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVfqfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 IQNATLKnNIIFG--------QKRKES---WYQRVveacALQQDLdilpagdeteIGEKGVNLSGGQKQRVSLARAVYCD 783
Cdd:PRK13641 99 FENTVLK-DVEFGpknfgfseDEAKEKalkWLKKV----GLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 784 RSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKD-----KTRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQ-------LFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
641-865 |
3.83e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 641 SISIEDGVFSWSrsESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL-LGEMDKmEGSVAVKGS-------------- 705
Cdd:COG4161 2 SIQLKNINCFYG--SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHqfdfsqkpsekair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 706 -----VAYVPQQ--AWIQNATLKNNI-----IFGQKRKESWY--QRVVEACALQQDLDILPAgdeteigekgvNLSGGQK 771
Cdd:COG4161 79 llrqkVGMVFQQynLWPHLTVMENLIeapckVLGLSKEQAREkaMKLLARLRLTDKADRFPL-----------HLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 772 QRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFD--QVIGPQGLlkdkTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEiiRELSQTGI----TQVIVTHEVEFARKvASQVVYMEKGRIIEQG 223
|
250 260
....*....|....*....|
gi 1357684105 849 ---SYLQLKEEEgaFAEFLR 865
Cdd:COG4161 224 dasHFTQPQTEA--FAHYLS 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
648-849 |
4.11e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.28 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 648 VFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSA--LLGEMDkmEGSVAVKG----------------SVAYV 709
Cdd:PRK11153 10 VFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT--SGRVLVDGqdltalsekelrkarrQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 710 PQQAWIQNA-TLKNNIIF-----GQKRKESwYQRVVEACA---LQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAV 780
Cdd:PRK11153 88 FQHFNLLSSrTVFDNVALplelaGTPKAEI-KARVTELLElvgLSDKADRYPA-----------QLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 781 YCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILE-------LLKDINRelgltiVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
659-848 |
4.80e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.98 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL--LGEMD---KMEGSVAVKG---------------SVAYVPQQAwiqN- 717
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIpgaRVEGEILLDGediydpdvdvvelrrRVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 --ATLKNNIIFGQK----RKESWYQRVVEAcALQQdldilpAG--DETE--IGEKGVNLSGGQKQRVSLARAVYCDRSVY 787
Cdd:COG1117 104 fpKSIYDNVAYGLRlhgiKSKSELDEIVEE-SLRK------AAlwDEVKdrLKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 788 LLDDPLSAVD----AHVGKHIFDqvigpqglLKDK-TRILVTHGLSylpQA----DLVLVMVDGEITEIG 848
Cdd:COG1117 177 LMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTHNMQ---QAarvsDYTAFFYLGELVEFG 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
662-849 |
5.17e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.94 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGeMDKMEGSVAVKG-SVAYVPQQAW------IQnatlknnIIF-------- 726
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ-------VVFqdpfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 727 ------------------GQKRKESWyQRVVEAcaLQQ-DLDilPAGDETEIGEkgvnLSGGQKQRVSLARAVYCDRSVY 787
Cdd:COG4172 377 prmtvgqiiaeglrvhgpGLSAAERR-ARVAEA--LEEvGLD--PAARHRYPHE----FSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 788 LLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTRilvTHGLSYL----------PQADLVLVMVDGEITEIGS 849
Cdd:COG4172 448 VLDEPTSALDVSVQAQILD-------LLRDLQR---EHGLAYLfishdlavvrALAHRVMVMKDGKVVEQGP 509
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
655-849 |
5.46e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL--LGEMDKME---GSVAVKGSVA----------YVPQQAWI-QNA 718
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDlivDGLKVNDPKVderlirqeagMVFQQFYLfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIFG--QKRKESwyqrvvEACALQQDLDIL-PAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSA 795
Cdd:PRK09493 93 TALENVMFGplRVRGAS------KEEAEKQARELLaKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 796 VDAHVgKHIFDQVIgpQGLLKD-KTRILVTHGLSYLPQADLVLVMVD-GEITEIGS 849
Cdd:PRK09493 167 LDPEL-RHEVLKVM--QDLAEEgMTMVIVTHEIGFAEKVASRLIFIDkGRIAEDGD 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
656-844 |
5.98e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 656 SPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQawIQNATLKNNIIFgQKRKESWY 735
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKLVGIVF-QNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 736 QRVVEacalqQDLDILPAG---DETEI--------GEKGV---------NLSGGQKQRVSLARAVYCDRSVYLLDDPLSA 795
Cdd:PRK13644 92 GRTVE-----EDLAFGPENlclPPIEIrkrvdralAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1357684105 796 VDAHVGKHIFDQVigPQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEI 844
Cdd:PRK13644 167 LDPDSGIAVLERI--KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
647-845 |
8.53e-10 |
|
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: 60.81 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 647 GVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGsvaYVPqqaWIQNATLKNNI-- 724
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVP---WKRRKKFLRRIgv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 IFGQKRKESWYQRVVEACALQQDLDILPAG-------------DETEIGEKGV-NLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:cd03267 99 VFGQKTQLWWDLPVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 791 DPLSAVDAHVGKHIFDQVigpQGLLKDK--TRILVTHGLSYLPQ-ADLVLVMVDGEIT 845
Cdd:cd03267 179 EPTIGLDVVAQENIRNFL---KEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
659-844 |
9.46e-10 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 60.77 E-value: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------------SVAYVPQQ-AWIQNATLK 721
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrRIGMIFQHyNLIERLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFG----QKRKESWYQRVVEAcALQQDLDILpagDETEIGEKGV----NLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:TIGR02315 98 ENVLHGrlgyKPTWRSLLGRFSEE-DKERALSAL---ERVGLADKAYqradQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 794 SAVDAHVGKHIFDqvigpqgLLKD------KTRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:TIGR02315 174 ASLDPKTSKQVMD-------YLKRinkedgITVIINLHQVDLAKKyADRIVGLKAGEI 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1290-1492 |
9.63e-10 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 60.82 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGLHElrSRITIIPQDPVLFSG-T 1364
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIagleRPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 LRMNL------DPFDSYSDEDIWKA-----LEFSHLktfvSGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKVLV 1433
Cdd:cd03296 91 VFDNVafglrvKPRSERPPEAEIRAkvhelLKLVQL----DWLADRYPAQ-------LSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1434 LDEATAAVDLETDNLIQSTIRSQFEDCTVLTI--AHRLNTIMDYT-RVLVLDKGQMAEFDSP 1492
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVAdRVVVMNKGRIEQVGTP 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
659-854 |
1.00e-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: 60.46 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKS---SLLSALL----GE-----MDKMEGSVAVKGSVAYVPQQAWIQNA-TLKNNI- 724
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTttiKMLTTLLkptsGRatvagHDVVREPREVRRRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 ----IFGQKRKEsWYQRVVEACALqqdLDILPAGDETEigekgVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHV 800
Cdd:cd03265 96 iharLYGVPGAE-RRERIDELLDF---VGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 801 GKHIFDQVigpQGLLK--DKTRILVTHglsYLPQADL----VLVMVDGEITEIGSYLQLK 854
Cdd:cd03265 167 RAHVWEYI---EKLKEefGMTILLTTH---YMEEAEQlcdrVAIIDHGRIIAEGTPEELK 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
656-867 |
1.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 656 SPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVPQQAWIQNATLKNNIIFGQKRKESW 734
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 735 YQRVVEACAL--------QQDLDILPA------GDETEIGEKG-VNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD-- 797
Cdd:PRK13643 99 EETVLKDVAFgpqnfgipKEKAEKIAAeklemvGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpk 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 798 AHVGKHIFDQVIGPQGllkdKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGSYLQLKEEegafAEFLRTY 867
Cdd:PRK13643 179 ARIEMMQLFESIHQSG----QTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE----VDFLKAH 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
657-798 |
1.12e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGS-----VAVKGSVA---YVPQQ----AWiQNAtlKNNI 724
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgKPVEGPGAergVVFQNegllPW-RNV--QDNV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 725 IFG-QKRKESWYQRVVEACALQQDLDILPAGdETEIGEkgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDA 798
Cdd:PRK11248 92 AFGlQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1289-1486 |
1.15e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1289 LAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG--VDIA------KLGlhelrsrITIIPQDPVL 1360
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprdaiALG-------IGMVHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1361 F-------------SGTLRMNLDpfdsysdediWKAL-----EFShlKTFvsGL---PDKLSHEcseggenLSVGQRQll 1419
Cdd:COG3845 92 VpnltvaenivlglEPTKGGRLD----------RKAArarirELS--ERY--GLdvdPDAKVED-------LSVGEQQ-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1420 clarallrK----------TKVLVLDEATaAV--DLETDNLIQsTIRsQF--EDCTVLTIAHRLNTIMDYT-RVLVLDKG 1484
Cdd:COG3845 149 --------RveilkalyrgARILILDEPT-AVltPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIAdRVTVLRRG 217
|
..
gi 1357684105 1485 QM 1486
Cdd:COG3845 218 KV 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1292-1496 |
1.17e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.77 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDP 1371
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1372 FDSYSDEDI---WKALEFSHLKTFVSGlpDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDL--ETD 1446
Cdd:PRK10253 104 RGRYPHQPLftrWRKEDEEAVTKAMQA--TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQID 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1447 NLIQSTIRSQFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLI 1496
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1274-1489 |
1.17e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYrsDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIE-----PAEGQISIDGVDI--AKLGLHE 1346
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1347 LRSRITIIPQDPVLFSGTLRMNLdpfdSYSDEDI-WK-ALEF-----SHLKTfvSGLPDKLSHECSEGGENLSVGQRQLL 1419
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEIddiveSALKD--ADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1420 CLARALLRKTKVLVLDEATAAVD----LETDNLIQS-TIRSQFEDCTVLTIAHRLNTIMDYTRVLVLDK---GQMAEF 1489
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEnriGQLVEF 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1291-1454 |
1.17e-09 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 60.25 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSL---TLGLfriIEPAEGQISIDGVDIAKLGLHElRSRITII--PQDPVLFSG-T 1364
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGL---VKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 LRMNLD---PFDSYSDEDIWKALEfSHLKTFvsglpdKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAV 1441
Cdd:cd03218 92 VEENILavlEIRGLSKKEREEKLE-ELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170
....*....|...
gi 1357684105 1442 DLETDNLIQSTIR 1454
Cdd:cd03218 165 DPIAVQDIQKIIK 177
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1284-1350 |
1.25e-09 |
|
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: 60.74 E-value: 1.25e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1284 RSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG---LHELRSR 1350
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRK 102
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1274-1487 |
1.25e-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: 60.07 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYR--SDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLhELRSRI 1351
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1352 TIIPQDPVLFSG-TLRMNLDPF-DSYsdediwkALEFSHLKTFVSGLPDKL--SHECSEGGENLSVGQRQLLCLARALLR 1427
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFaGLY-------GLKGDELTARLEELADRLgmEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1428 KTKVLVLDEATAAVDLETDNLIQSTIRSQFED-CTVLTIAHRLNTIMDYT-RVLVLDKGQMA 1487
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCdRVVVLHRGRVV 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
642-853 |
1.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPTLKRLN---VRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVK--------------- 703
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipanlkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 704 ------GSVAYVPQQAWIQNaTLKNNIIFGQ----KRKESWYQRVVEACALQQdldiLPagdETEIGEKGVNLSGGQKQR 773
Cdd:PRK13645 87 rlrkeiGLVFQFPEYQLFQE-TIEKDIAFGPvnlgENKQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 774 VSLARAVYCDRSVYLLDDPLSAVDAHvGKHIFDQVIGPQGLLKDKTRILVTHGL-SYLPQADLVLVMVDGEITEIGSYLQ 852
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFE 237
|
.
gi 1357684105 853 L 853
Cdd:PRK13645 238 I 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1296-1487 |
1.61e-09 |
|
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: 59.43 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1296 VDISGGEKVGIVGRTGAGKSSLtLGLFRIIE-PAEGQISIDGVDIAKLglhELRSR-ITIIPQDPVLFSG-TLRMNLD-- 1370
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTL-LNLIAGFEtPQSGRVLINGVDVTAA---PPADRpVSMLFQENNLFAHlTVEQNVGlg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1371 --PFDSYSDED---IWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLARALLRKTKVLVLDEATAAVD--L 1443
Cdd:cd03298 95 lsPGLKLTAEDrqaIEVALARVGLAGLEKRLPGELSG-----------GERQRVALARVLVRDKPVLLLDEPFAALDpaL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1357684105 1444 ETDNL-IQSTIRSQfEDCTVLTIAHRLNTIMD-YTRVLVLDKGQMA 1487
Cdd:cd03298 164 RAEMLdLVLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1283-1442 |
1.63e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1283 YRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFS 1362
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 GTLRMNLD-PFDSYSDEDIWKALEfSHLKTFvsGLPDklsHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAV 1441
Cdd:PRK10247 95 DTVYDNLIfPWQIRNQQPDPAIFL-DDLERF--ALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
.
gi 1357684105 1442 D 1442
Cdd:PRK10247 169 D 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
652-798 |
1.66e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.43 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 652 SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------------SVAYVPQQAWIQNA- 718
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiarGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIifgqkrkeSWYQRVveaCALQQDLDILPAGDETEIGEKGVN-LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:cd03231 89 SVLENL--------RFWHAD---HSDEQVEEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
.
gi 1357684105 798 A 798
Cdd:cd03231 158 K 158
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
650-849 |
1.70e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.13 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 650 SWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQ---- 712
Cdd:COG4559 8 SVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHssla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 713 --------------AWIQNATLKNNIIfgqkrkeswyQRVVEACalqqDLDILPAGDETEigekgvnLSGGQKQRVSLAR 778
Cdd:COG4559 88 fpftveevvalgraPHGSSAAQDRQIV----------REALALV----GLAHLAGRSYQT-------LSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 779 A---VYCDRSVY----LLDDPLSAVD-AHVgKHIFDqvigpqgLLKDKTR-----ILVTHGLS----YlpqADLVLVMVD 841
Cdd:COG4559 147 VlaqLWEPVDGGprwlFLDEPTSALDlAHQ-HAVLR-------LARQLARrgggvVAVLHDLNlaaqY---ADRILLLHQ 215
|
....*...
gi 1357684105 842 GEITEIGS 849
Cdd:COG4559 216 GRLVAQGT 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
642-792 |
1.78e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.84 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDgvFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAV--KGSVAYVPQqawiqnat 719
Cdd:cd03221 1 IELEN--LSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 720 lknniifgqkrkeswyqrvveacalqqdldilpagdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1290-1481 |
2.01e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSslTLG--LFRIIEPAEGQISIDGVDIAKLGLHE-LRSRITIIPQDPVL------ 1360
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS--TLMkiLSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLvpnlsv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1361 ----FSGTLRMNLDPFDsysdediWKALE------FSHLktfvsGL---PDKLshecsegGENLSVGQRQLLCLARALLR 1427
Cdd:COG1129 97 aeniFLGREPRRGGLID-------WRAMRrrarelLARL-----GLdidPDTP-------VGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1428 KTKVLVLDEATAAvdL---ETDNLIQ--STIRSQfeDCTVLTIAHRLNTIMDYT-RVLVL 1481
Cdd:COG1129 158 DARVLILDEPTAS--LterEVERLFRiiRRLKAQ--GVAIIYISHRLDEVFEIAdRVTVL 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1280-1455 |
2.30e-09 |
|
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: 58.91 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1280 GLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPV 1359
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1360 LFSGTLRMNLD---PFDSYSDEDIWKALEFSHLktfvSGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVLDE 1436
Cdd:TIGR01189 85 KPELSALENLHfwaAIHGGAQRTIEDALAAVGL----TGFEDLPAAQ-------LSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*....
gi 1357684105 1437 ATAAVDLETDNLIQSTIRS 1455
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRA 172
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
998-1209 |
3.07e-09 |
|
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: 59.81 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 998 GVYGGLGVSQGVAVFGYSLSVsigGILASRFLHQ--SMLFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKM 1074
Cdd:cd18546 43 AAYLAVVLAGWVAQRAQTRLT---GRTGERLLYDlrLRVFAhLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1075 FMGSLFNVLGSCVIILV-----ATPMVAFIIPFLGLLYFFvQRfyvASSRQLKRL-ESVSRspIYTHFNETLLGTSVIRA 1148
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVldprlALVALAALPPLALATRWF-RR---RSSRAYRRArERIAA--VNADLQETLAGIRVVQA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1149 FGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNciVSFAALFAV----LARENLSPG 1209
Cdd:cd18546 194 FRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGN--LATAAVLLVgawrVAAGTLTVG 256
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1291-1488 |
3.18e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.54 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIE-----PAEGQISIDGVDIAKLGLHELRSRITIIPQDP------V 1359
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1360 LFSGT---LRMN-LDPFDSYSDEDIWKALEFSHLKtfvsglpDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLD 1435
Cdd:PRK14247 99 IFENValgLKLNrLVKSKKELQERVRWALEKAQLW-------DEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1436 EATAAVDLETDNLIQSTIRSQFEDCTVLTIAH---RLNTIMDYtrVLVLDKGQMAE 1488
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVE 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1290-1488 |
3.49e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG---LHELRSRITIIPQDPvLFSGTLR 1366
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNL-----DPFDSY----SDEDIWKALEFSHLKtfVSGLP---DKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVL 1434
Cdd:PRK15079 115 MTIgeiiaEPLRTYhpklSRQEVKDRVKAMMLK--VGLLPnliNRYPHE-------FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1435 DEATAAVDLETD----NLIQSTIRSQfeDCTVLTIAHRLNT---IMDytRVLVLDKGQMAE 1488
Cdd:PRK15079 186 DEPVSALDVSIQaqvvNLLQQLQREM--GLSLIFIAHDLAVvkhISD--RVLVMYLGHAVE 242
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1291-1499 |
3.52e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHElRSR--ITIIPQDPVLFS------ 1362
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARrgIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 ---GTLRMNLDPFDSYSDEDIWKALEFSHlktfVSGLPDKLshecsegGENLSVGQRQLLCLARALLRKTKVLVLDEATA 1439
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFH----IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1440 AVD----LETDNLIQSTIRSQFedcTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK10895 167 GVDpisvIDIKRIIEHLRDSGL---GVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
659-855 |
4.24e-09 |
|
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: 58.84 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVPQQAWI----------QNA------TLK 721
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlfQGGalfdslTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFGQKR----KESWYQRVVEAC----ALQQDLDILPAgdeteigEkgvnLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:COG1127 101 ENVAFPLREhtdlSEAEIRELVLEKlelvGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 794 SAVDAhVGKHIFDQVIgpqgL-LKDK---TRILVTHGLSYLPQ-ADLVLVMVDGEITEIGSYLQLKE 855
Cdd:COG1127 170 AGLDP-ITSAVIDELI----ReLRDElglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
659-844 |
4.47e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.44 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--------------VAYVP----QQAWIQNATL 720
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 721 KNNIIFGQKrkeswyqrvveacalqqdldilpagdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDahV 800
Cdd:cd03215 96 AENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--V 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 801 G--KHIFDQVIgpqgLLKD--KTRILVThglSYLPQ----ADLVLVMVDGEI 844
Cdd:cd03215 138 GakAEIYRLIR----ELADagKAVLLIS---SELDEllglCDRILVMYEGRI 182
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
950-1245 |
4.94e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 59.45 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 950 AIGVLLSAISllfflshNLLSMFANYwLSLWTDDPVVNGTQPDRLMRLGVY--GGLGvsqGVAVFGYSLSVSIGGILAsr 1027
Cdd:cd18563 2 ILGFLLMLLG-------TALGLVPPY-LTKILIDDVLIQLGPGGNTSLLLLlvLGLA---GAYVLSALLGILRGRLLA-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1028 FLHQSMLFDvLRS---------PMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAF 1098
Cdd:cd18563 69 RLGERITAD-LRRdlyehlqrlSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1099 II----PFLGLL-YFFVQRFYVASSRQLKRlesvsRSPIYTHFNETLLGTSVIRAFG----EQERFihesDQRvdhNQKA 1169
Cdd:cd18563 148 LVlipvPLVVWGsYFFWKKIRRLFHRQWRR-----WSRLNSVLNDTLPGIRVVKAFGqekrEIKRF----DEA---NQEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1170 YYPSIVANRWLAIRLEFVGNCIVSFAALFAVLARENLSPGIMGLS-----ISYALQLTASLTWLVRMSSDVETNIVAVER 1244
Cdd:cd18563 216 LDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGtlvafLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
.
gi 1357684105 1245 V 1245
Cdd:cd18563 296 I 296
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1291-1488 |
5.16e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSltlgLFRII------EPAEGQISIDGVDIAKLGLHElRSR--ITIIPQDPVLFS 1362
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKST----LAKTImghpkyEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 GTlrmnldpfdsysdediwkalefsHLKTFVSGLPDKLShecseGGEnlsvgqRQLLCLARALLRKTKVLVLDEATAAVD 1442
Cdd:cd03217 91 GV-----------------------KNADFLRYVNEGFS-----GGE------KKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1443 LETDNLIQSTIRS-QFEDCTVLTIAHRLNtIMDY---TRVLVLDKGQMAE 1488
Cdd:cd03217 137 IDALRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVK 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
659-883 |
6.29e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.49 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-------------SVAYVPQQAWI-QNATLKNNI 724
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTpEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 IFGQKRKESWYQRVVeacalQQDLDILP-AGDETEI---GEKGV-NLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDah 799
Cdd:PRK11231 98 AYGRSPWLSLWGRLS-----AEDNARVNqAMEQTRInhlADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 800 vgkhIFDQV--IGPQGLLKD--KTRILVTHGLSylpQA----DLVLVMVDGEITEIGSylqlkEEEGAFAEFLRTYASSE 871
Cdd:PRK11231 171 ----INHQVelMRLMRELNTqgKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGT-----PEEVMTPGLLRTVFDVE 238
|
250
....*....|..
gi 1357684105 872 QTDGSEPVPNSP 883
Cdd:PRK11231 239 AEIHPEPVSGTP 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1292-1363 |
6.81e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 6.81e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSltlgLFRII----EPAEGQISID-GVDIAKLglhelrsritiiPQDPVLFSG 1363
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRIGYL------------PQEPPLDDD 75
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
662-849 |
6.86e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.85 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVP-----------QQAWIQNATLKNNIIFGQK 729
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 730 R----KESWYQRVVEACALQQDLDIlpagdeteIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIF 805
Cdd:PRK11607 118 QdklpKAEIASRVNEMLGLVHMQEF--------AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1357684105 806 DQVIgpqGLLK--DKTRILVTHGL-SYLPQADLVLVMVDGEITEIGS 849
Cdd:PRK11607 190 LEVV---DILErvGVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
652-799 |
6.86e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 652 SRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------------SVAYVPQQAWIQNA- 718
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIFgqkrkeswyqrvveACALQQDLDilpagDET------EIGEKGV------NLSGGQKQRVSLARAVYCDRSV 786
Cdd:PRK13538 90 TALENLRF--------------YQRLHGPGD-----DEAlwealaQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPL 150
|
170
....*....|...
gi 1357684105 787 YLLDDPLSAVDAH 799
Cdd:PRK13538 151 WILDEPFTAIDKQ 163
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
657-842 |
6.93e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAV--KGSVAYVPQQAWIQNATLKNNIIFGQKRkESW 734
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYPATA-EAF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 735 ----YQRVVEACALQQDLDILpagDETEIGEKGvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVig 810
Cdd:COG4178 456 sdaeLREALEAVGLGHLAERL---DEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL-- 528
|
170 180 190
....*....|....*....|....*....|..
gi 1357684105 811 pQGLLKDKTRILVTHGLSYLPQADLVLVMVDG 842
Cdd:COG4178 529 -REELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
637-825 |
7.79e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 637 CSAYSISIEDGVFSWsrsesptLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKgsvayVPQQAWIQ 716
Cdd:COG2401 31 LEAFGVELRVVERYV-------LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 NATLKNNIIfgqkRKESWYQ--RVVEACALqqdldilpaGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLS 794
Cdd:COG2401 99 EASLIDAIG----RKGDFKDavELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1357684105 795 AVD---AHVGKHIFdqvigpQGLLKD--KTRILVTH 825
Cdd:COG2401 166 HLDrqtAKRVARNL------QKLARRagITLVVATH 195
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
659-848 |
7.90e-09 |
|
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: 57.59 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGsLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS------------VAYVPQQ-AWIQN-------- 717
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNftvrefld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 --ATLKNniIFGQKRKEswyqrvvEACALQQDLDILPAGDEtEIGEkgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSA 795
Cdd:cd03264 95 yiAWLKG--IPSKEVKA-------RVDEVLELVNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 796 VDAhVGKHIFDQVIGPQGllKDKTRILVTH---GLSYLpqADLVLVMVDGEITEIG 848
Cdd:cd03264 161 LDP-EERIRFRNLLSELG--EDRIVILSTHiveDVESL--CNQVAVLNKGKLVFEG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
659-849 |
8.79e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQNATLKNNIIFGQKRKESWYQRV 738
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 739 VEACALQQDLDILPAGDETE-----IGEKGVN---------LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHI 804
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREkaldaLRQVGLEnyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1357684105 805 FDQVIGPQGlLKDKTRILVTHGL-SYLPQADLVLVMVDGEITEIGS 849
Cdd:PRK10070 204 QDELVKLQA-KHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
674-839 |
1.14e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 674 VVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-------------VAYVPQQAWIQNATLKNNIIFG-QKRKESwyqrvV 739
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLIFPwQIRNQQ-----P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 740 EACALQQDLDI--LPagdeTEIGEKGVN-LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHvGKHIFDQVIgpQGLLK 816
Cdd:PRK10247 113 DPAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHNVNEII--HRYVR 185
|
170 180
....*....|....*....|....*
gi 1357684105 817 DK--TRILVTHGLSYLPQADLVLVM 839
Cdd:PRK10247 186 EQniAVLWVTHDKDEINHADKVITL 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
659-792 |
1.17e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV--AVKGSVAYVPQqawiQNATLKNNiifgqkrkeswyQ 736
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklGETVKIGYFDQ----HQEELDPD------------K 394
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 737 RVVEacALQqdlDILPAGDETEI----------GEK-----GVnLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:COG0488 395 TVLD--ELR---DGAPGGTEQEVrgylgrflfsGDDafkpvGV-LSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
567-847 |
1.25e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 567 VYVLSNDQNVLDAQKA-FVSLALFnILRFPL----NMLPMVISsmvqASVSLKRLRVFlsheELQEDSVEH--PAAGCSA 639
Cdd:PRK10522 250 VFYMANSLGWADTNVAaTYSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLNKL----ALAPYKAEFprPQAFPDW 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 640 YSISIEDGVFSWSrSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-VAYVPQQAWIQ-- 716
Cdd:PRK10522 321 QTLELRNVTFAYQ-DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRKlf 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 NATLKNNIIFGQKRKESWYQrvVEACALQQDLDILPAGDETEIGEKGV---NLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEGKP--ANPALVEKWLERLKMAHKLELEDGRIsnlKLSKGQKKRLALLLALAEERDILLLDEWA 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 794 SAVDAHVgKHIFDQVIGPQGLLKDKTRILVTHGLSYLPQADLVLVMVDGEITEI 847
Cdd:PRK10522 478 ADQDPHF-RREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSEL 530
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
659-841 |
1.29e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 55.62 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV--AVKGSVAYVPQQAWIQNATLKNNIIFgqkrkeSWYQ 736
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmPEGEDLLFLPQRPYLPLGTLREQLIY------PWDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 737 RvveacalqqdldilpagdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLK 816
Cdd:cd03223 91 V----------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ-------LLK 135
|
170 180
....*....|....*....|....*..
gi 1357684105 817 DK--TRILVTHGLSYLPQADLVLVMVD 841
Cdd:cd03223 136 ELgiTVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
655-848 |
1.79e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAY----------VPQQAWIQNATLKNNI 724
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 IFgqKRKESWYQRVVEACALQQDLDILPAG-----------------DETEIGEKGVNLSGGQKQRVSLARAVYCDRSVY 787
Cdd:PRK10619 97 VF--QHFNLWSHMTVLENVMEAPIQVLGLSkqeareravkylakvgiDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 788 LLDDPLSAVDAHVGKHIFD--QVIGPQGllkdKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRimQQLAEEG----KTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
643-853 |
2.26e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.79 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 643 SIEDGVfSWSRSESPTLKR---LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAvkgsvayvpqqaWI-QNA 718
Cdd:PRK15079 19 DIKDGK-QWFWQPPKTLKAvdgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA------------WLgKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIFGQKRKE----------SWYQRVVEACALQQDLDIL-PAGDETEIGEK--------GV--NL--------SGG 769
Cdd:PRK15079 86 LGMKDDEWRAVRSDiqmifqdplaSLNPRMTIGEIIAEPLRTYhPKLSRQEVKDRvkammlkvGLlpNLinryphefSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 770 QKQRVSLARAVYCDRSVYLLDDPLSAVDAhvgkHIFDQVIgpqGLLKDKTR------ILVTHGLSYLPQ-ADLVLVMVDG 842
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDV----SIQAQVV---NLLQQLQRemglslIFIAHDLAVVKHiSDRVLVMYLG 238
|
250
....*....|.
gi 1357684105 843 EITEIGSYLQL 853
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1290-1498 |
2.33e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISI----DGVDIAKLGLhELRSRIT-----------II 1354
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigilhqeydLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1355 PQDPVLFSGTLRMNLD-PFDSYSDEDIW--KALEFSHLKTfVSGLpDKLSHEcseggenLSVGQRQLLCLARALLRKTKV 1431
Cdd:TIGR03269 378 PHRTVLDNLTEAIGLElPDELARMKAVItlKMVGFDEEKA-EEIL-DKYPDE-------LSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1432 LVLDEATAAVDLETDNLIQSTI---RSQFEDcTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVCdRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
950-1245 |
2.48e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 57.10 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 950 AIGVLLSAISLLFflshNLLSMFAnywlslwTDDPVVNGTQPDRLMRLGVYGGLGVSQGVAVFGYSLSVSIGGILASRFL 1029
Cdd:cd18540 9 ILMLLVALLDAVF----PLLTKYA-------IDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1030 HQSMlFDVLRS-PMSFFERTPSGNLVNRFAKEMDTIDSLIP-MILKMFMGsLFNVLGSCVIILVATP----MVAFIIPFL 1103
Cdd:cd18540 78 RKKA-FEHLQTlSFSYFDKTPVGWIMARVTSDTQRLGEIISwGLVDLVWG-ITYMIGILIVMLILNWklalIVLAVVPVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1104 GLLYFFVQRFYVASSRQLKRLESVsrspIYTHFNETLLGTSVIRAFGEQERFIHESDQrvdHNQKAYYPSIVANRWLAIR 1183
Cdd:cd18540 156 AVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKTLVREEKNLREFKE---LTEEMRRASVRAARLSALF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1184 LEFVgNCIVSFAALFA-----VLAREN-LSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18540 229 LPIV-LFLGSIATALVlwyggILVLAGaITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
642-844 |
2.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGVFSWSRSESPT----LKRLNVRVPEGSLVAVVGHVGSGKSSL---LSALLgemDKMEGSVAVKGSVAYVPQQAW 714
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL---IPSEGKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 -IQNatlKNNIIFGQKRKESWYQRVVEACAL-QQDLDILPAGDETEIGE--KGVN-----------LSGGQKQRVSLARA 779
Cdd:PRK13633 82 dIRN---KAGMVFQNPDNQIVATIVEEDVAFgPENLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 780 VYCDRSVYLLDDPLSAVDAhVGKHifdQVIGPQGLLKDK---TRILVTHGLSYLPQADLVLVMVDGEI 844
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDP-SGRR---EVVNTIKELNKKygiTIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
659-806 |
2.93e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.56 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLS----------------ALLGEMDKMEGSVA-----VKGSVAYVPQQAWIQN 717
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsglitgdksagshiELLGRTVQREGRLArdirkSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 A-TLKNNIIFGQ-------KRKESWYQRVVEACALQQdldILPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLL 789
Cdd:PRK09984 100 RlSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQA---LTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170
....*....|....*..
gi 1357684105 790 DDPLSAVDAHVGKHIFD 806
Cdd:PRK09984 177 DEPIASLDPESARIVMD 193
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
662-864 |
3.08e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.18 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSAL-LGEMDKmEGSVAVKGS-------------------VAYVPQQ--AWiQNAT 719
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLW-PHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIFGQKRkeswYQRVVEACALQQDLDILPAGDETEIGEK-GVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDA 798
Cdd:PRK11124 99 VQQNLIEAPCR----VLGLSKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 799 HVGKHIFDQVIGPQGllKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG---SYLQLKEEegAFAEFL 864
Cdd:PRK11124 175 EITAQIVSIIRELAE--TGITQVIVTHEVEVARKtASRVVYMENGHIVEQGdasCFTQPQTE--AFKNYL 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1298-1499 |
3.50e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.15 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1298 ISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDI---AKLGlhelRSRITIIPQ-DPVLFSGTLRMNLDPFD 1373
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparARLA----RARIGVVPQfDNLDLEFTVRENLLVFG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1374 SY-------SDEDIWKALEFSHLKTfvsglpdKLSHECSEggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETD 1446
Cdd:PRK13536 140 RYfgmstreIEAVIPSLLEFARLES-------KADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1447 NLIQSTIRSQF-EDCTVLTIAHrlntIMDYT-----RVLVLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK13536 209 HLIWERLRSLLaRGKTILLTTH----FMEEAerlcdRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
659-849 |
3.80e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVA--------YVPQqawiqnATLKNNIIF---- 726
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPE------LTGRENIYLngrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 727 -GQKRKEswYQRVVEACAlqqdldilpagDETEIGE------KgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAH 799
Cdd:COG1134 116 lGLSRKE--IDEKFDEIV-----------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 800 ----VGKHIFDqvigpqglLKDKTR--ILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:COG1134 181 fqkkCLARIRE--------LRESGRtvIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1280-1456 |
3.80e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.34 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1280 GLRYRSDLDlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAkLGLHELRS-RITIIPQDP 1358
Cdd:PRK15112 19 GWFRRQTVE-AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1359 V-----------LFSGTLRMNLDPFDSYSDEDIWKALEFshlktfVSGLPDKLSHEcsegGENLSVGQRQLLCLARALLR 1427
Cdd:PRK15112 97 StslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQ------VGLLPDHASYY----PHMLAPGQKQRLGLARALIL 166
|
170 180
....*....|....*....|....*....
gi 1357684105 1428 KTKVLVLDEATAAVDLetdnliqsTIRSQ 1456
Cdd:PRK15112 167 RPKVIIADEALASLDM--------SMRSQ 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
659-797 |
4.01e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 55.63 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------------SVAYVPQQAWI-QNATLKNN 723
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 724 II-FGQKRKESWYQRVVEACALQQDLDILPAGDEteigeKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:cd03218 96 ILaVLEIRGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1293-1496 |
4.19e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1293 NINVDISGGEKVGIVGRTGAGKSSLtlglFRIIEPAE----GQISIDGVDI--AKLGLHELR-------SRITIIPQ--- 1356
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTL----LRCINKLEeitsGDLIVDGLKVndPKVDERLIRqeagmvfQQFYLFPHlta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1357 -DPVLFsGTLRMNldpfdSYSDEDIWK-ALEfshLKTFVsGLPDKLSHECSEggenLSVGQRQLLCLARALLRKTKVLVL 1434
Cdd:PRK09493 95 lENVMF-GPLRVR-----GASKEEAEKqARE---LLAKV-GLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1435 DEATAAVDLETDNLIQSTIRSQFED-CTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLI 1496
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
766-849 |
4.75e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 56.00 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 766 LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPQ---GLlkdkTRILVTHGLSYLPQ-ADLVLVMVD 841
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQeklGI----SYIYVSQHLGIVKHiSDKVLVMHQ 225
|
....*...
gi 1357684105 842 GEITEIGS 849
Cdd:COG4167 226 GEVVEYGK 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
653-849 |
4.93e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 653 RSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS-------------VAYVPQQA--WIQN 717
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 ATLKNNIIFGQKR----KESWYQRVVEA---CALQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:PRK13652 94 PTVEQDIAFGPINlgldEETVAHRVSSAlhmLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 791 DPLSAVDAHVGKHIFDQVigpQGLLKD--KTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFL---NDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1290-1497 |
4.97e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.50 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtLGLFRII---EPAEGQI---------------------------------S 1333
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRIiyhvalcekcgyverpskvgepcpvcggtlepeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1334 IDGVDIAKLGLHELRSRITIIPQDPVLFSGTLR-----MNLDPFDSYS-DEDIWKALEFSHLKtfvsglpdKLSHECSEG 1407
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIEMV--------QLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1408 GENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS--QFEDCTVLTIAHRLNTIMDYT-RVLVLDKG 1484
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSdKAIWLENG 245
|
250
....*....|...
gi 1357684105 1485 QMAEFDSPSSLIA 1497
Cdd:TIGR03269 246 EIKEEGTPDEVVA 258
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
641-825 |
5.12e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 641 SISIEDGVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGsvAYVPQQAWIQNA-- 718
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARAri 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 -------------TLKNN-IIFGQKRKESwyQRVVEAcALQQDLDIlpAGDETEIGEKGVNLSGGQKQRVSLARAVYCDR 784
Cdd:PRK13536 117 gvvpqfdnldlefTVRENlLVFGRYFGMS--TREIEA-VIPSLLEF--ARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDQVigpQGLL-KDKTRILVTH 825
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERL---RSLLaRGKTILLTTH 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
657-849 |
6.47e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSV-----------AYVpqqawIQN------AT 719
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadrdiAMV-----FQNyalyphMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIFGQK-R---KESWYQRVVEACalqqdlDILpagdetEIGE----KGVNLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:PRK11650 93 VRENMAYGLKiRgmpKAEIEERVAEAA------RIL------ELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 792 PLSAVDAHVGKHIFDQVIGPQGLLKdKTRILVTHGlsylpQ------ADLVLVMVDGEITEIGS 849
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLK-TTSLYVTHD-----QveamtlADRVVVMNGGVAEQIGT 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1301-1496 |
7.61e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.56 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1301 GEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQD-PVLFSGTLRM-----------N 1368
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRElvaigrypwhgA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1369 LDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLShecseGGEnlsvgqRQLLCLARALLRKTKVLVLDEATAAVDL----E 1444
Cdd:PRK10575 117 LGRFGAADREKVEEAISLVGLKPLAHRLVDSLS-----GGE------RQRAWIAMLVAQDSRCLLLDEPTSALDIahqvD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1445 TDNLIQSTirSQFEDCTVLTIAHRLNTIMDYTRVLV-LDKGQMAEFDSPSSLI 1496
Cdd:PRK10575 186 VLALVHRL--SQERGLTVIAVLHDINMAARYCDYLVaLRGGEMIAQGTPAELM 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
653-845 |
8.10e-08 |
|
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: 54.19 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 653 RSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL---LGEMDKMEGSVAVKG------------SVAYVPQQAW-IQ 716
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEIIYVSEEDVhFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 NATLKNNIIFgqkrkeswyqrvveACALQqdldilpaGDETEIGekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAV 796
Cdd:cd03233 97 TLTVRETLDF--------------ALRCK--------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 797 DAHVGKHIFDQvigpqglLKDKTRILVTHGLSYLPQA--------DLVLVMVDGEIT 845
Cdd:cd03233 150 DSSTALEILKC-------IRTMADVLKTTTFVSLYQAsdeiydlfDKVLVLYEGRQI 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
659-846 |
8.10e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------------SVAYVPQQA--------- 713
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVFQDSisavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 714 --WIQNATLKNNIIFGQKRKESWYQRVVEACALQ-QDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:PRK10419 108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 791 DPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGLSYLPQ-ADLVLVMVDGEITE 846
Cdd:PRK10419 177 EAVSNLDLVLQAGVIR-------LLKKLQQqfgtacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
662-849 |
8.17e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAY--------VPQQAWI----QNATL------KNN 723
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiclPPEKRRIgyvfQDARLfphykvRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFGQKRK-ESWYQRVVEACALQQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAhvgk 802
Cdd:PRK11144 97 LRYGMAKSmVAQFDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL---- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 803 hifdqvigP---------QGLLKD-KTRIL-VTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK11144 162 --------PrkrellpylERLAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
957-1245 |
8.71e-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: 55.55 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 957 AISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPDRLMRLGVYGGLGVSQGVAVFGYSLSVSIGGilasrflhQSMLFD 1036
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVG--------QRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 --------VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATP---MVAFI-IPFLG 1104
Cdd:cd18545 75 lrqdlfshLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVrlaLVTLAvLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1105 LLYFFVQRFyvasSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVANRWLAIRL 1184
Cdd:cd18545 155 LVVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLV 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1185 EF---VGNCIVSFAALFAVLArENLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18545 231 ELisaLGTALVYWYGGKLVLG-GAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
642-848 |
8.86e-08 |
|
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: 55.09 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 642 ISIEDGvfSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVA--------------VKGSVA 707
Cdd:COG1119 4 LELRNV--TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerrggedvweLRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 708 YV-P--QQAWIQNATLKNNII------FGQKRKESWYQRvVEACALQQDLDILPAGDETeIGEkgvnLSGGQKQRVSLAR 778
Cdd:COG1119 82 LVsPalQLRFPRDETVLDVVLsgffdsIGLYREPTDEQR-ERARELLELLGLAHLADRP-FGT----LSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 779 AVYCDRSVYLLDDPLSAVDAHvGKHIFDQVIGPQGLLKDKTRILVTHGLSYLPQA-DLVLVMVDGEITEIG 848
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1277-1497 |
1.01e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1277 TNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG--VDIAKLGLHELRSRITII 1354
Cdd:PRK13638 5 SDLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1355 PQDP------------VLFSgtLRmNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLA 1422
Cdd:PRK13638 83 FQDPeqqifytdidsdIAFS--LR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1423 RALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDCTVLTI-AHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIA 1497
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEISdAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1288-1495 |
1.10e-07 |
|
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: 54.55 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1288 DLAIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGLHelRSRITIIPQDPVLFSg 1363
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIagfeTPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 tlrmNLDPFDSYS-------------DEDIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLARALLRKTK 1430
Cdd:cd03300 86 ----HLTVFENIAfglrlkklpkaeiKERVAEALDLVQLEGYANRKPSQLSG-----------GQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1431 VLVLDEATAAVD--------LETDNLIQSTirsqfeDCTVLTIAHRLN---TIMDytRVLVLDKGQMAEFDSPSSL 1495
Cdd:cd03300 151 VLLLDEPLGALDlklrkdmqLELKRLQKEL------GITFVFVTHDQEealTMSD--RIAVMNKGKIQQIGTPEEI 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1291-1487 |
1.11e-07 |
|
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: 53.71 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSL--TLGLFRIIEPAEGQISIDGVdiaKLGLHELRSRITIIPQDPVLFsGTLrmn 1368
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILH-PTL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1369 ldpfdsysdeDIWKALEFS-HLKtfvsglpdklshecseggeNLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDN 1447
Cdd:cd03213 98 ----------TVRETLMFAaKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1357684105 1448 LIQSTIRS-QFEDCTVLTIAHRLNTIMDYT--RVLVLDKGQMA 1487
Cdd:cd03213 149 QVMSLLRRlADTGRTIICSIHQPSSEIFELfdKLLLLSQGRVI 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
659-844 |
1.19e-07 |
|
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: 53.82 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS---------VAYVPQQAWI-QNATLKNNIIF-- 726
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLyPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 727 ---GQKRKEswyqrvveacALQQDLDILPAGDETEIGEKGVN-LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAhVGK 802
Cdd:cd03269 96 qlkGLKKEE----------ARRRIDEWLERLELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1357684105 803 HIFDQVIGPQgLLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEI 844
Cdd:cd03269 165 ELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
659-857 |
1.22e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSL---LSALL--------------------GEMDKMEGSVAVKGS---------- 705
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtgtiewifkdeknkkktKEKEKVLEKLVIQKTrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 706 ----VAYVPQQAWIQ--NATLKNNIIFGQK----RKESWYQRVVEACALQqDLDilpagdETEIGEKGVNLSGGQKQRVS 775
Cdd:PRK13651 103 irrrVGVVFQFAEYQlfEQTIEKDIIFGPVsmgvSKEEAKKRAAKYIELV-GLD------ESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 776 LARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvIGPQGLLKDKTRILVTHGL-SYLPQADLVLVMVDGEITEIG-SYLQL 853
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYDIL 253
|
....
gi 1357684105 854 KEEE 857
Cdd:PRK13651 254 SDNK 257
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
982-1245 |
1.37e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 54.80 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 982 DDPVVNGTQPDRLMRLGVYGGLGVSQGVAVFGYSLsvsIGGILASRFLHQ--SMLFD-VLRSPMSFFERTPSGNLVNRfa 1058
Cdd:cd18543 27 DGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRY---LAGRLSLGVEHDlrTDLFAhLQRLDGAFHDRWQSGQLLSR-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1059 kemdtIDSLIPMIlKMFMGSLFNVLGSCVIILVATPMVAFIIPFLGL--------LYFFVQRF---YVASSRQLK-RLES 1126
Cdd:cd18543 102 -----ATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALvalaslppLVLVARRFrrrYFPASRRAQdQAGD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1127 VSrspiyTHFNETLLGTSVIRAFGeQERfiHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGNciVSFAALFAVLA---- 1202
Cdd:cd18543 176 LA-----TVVEESVTGIRVVKAFG-RER--RELDRFEAAARRLRATRLRAARLRARFWPLLEA--LPELGLAAVLAlggw 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1357684105 1203 ---RENLSPGIMGLSISYALQLTA---SLTWLVRMSSDVETnivAVERV 1245
Cdd:cd18543 246 lvaNGSLTLGTLVAFSAYLTMLVWpvrMLGWLLAMAQRARA---AAERV 291
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
655-849 |
1.52e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.75 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVK--------------------GSVAYVPQQAW 714
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstsknkdikqirkkvGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 IQNATLKnNIIFGQKR----KESWYQRVVEACALqqdldilpAGDETEIGEKG-VNLSGGQKQRVSLARAVYCDRSVYLL 789
Cdd:PRK13649 99 FEETVLK-DVAFGPQNfgvsQEEAEALAREKLAL--------VGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 790 DDPLSAVDAHVGKHIFDqvIGPQGLLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK13649 170 DEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1290-1481 |
1.53e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 53.39 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVdiAKLGLheLRSRITIIPQDPVLFSGTLRMNL 1369
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 ----DPFDSYSDED---IWKALEFSHLktfvSGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVD 1442
Cdd:NF040873 83 warrGLWRRLTRDDraaVDDALERVGL----ADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1357684105 1443 LETDNLIQSTIRSQFED-CTVLTIAHRLNTIMDYTRVLVL 1481
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
659-827 |
1.54e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.40 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSAL-----LGEMDKMEGSVAVKGSVAYVP---------------QQAWIQNA 718
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 TLKNNIIFGQKRkeSWYQ----RVVEACALQQDLdilpaGDETE--IGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:PRK14243 106 SIYDNIAYGARI--NGYKgdmdELVERSLRQAAL-----WDEVKdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1357684105 793 LSAVDAHVGKHIfDQVIgpQGLLKDKTRILVTHGL 827
Cdd:PRK14243 179 CSALDPISTLRI-EELM--HELKEQYTIIIVTHNM 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
647-849 |
1.62e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.82 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 647 GVFSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDK---MEGSVAVKGSV----------AYVPQQ- 712
Cdd:TIGR00955 29 GCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDd 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 713 AWIQNATLKNNIIFGQ----KRKESWYQRVVEACALQQDLDILPAGDeTEIGEKGV--NLSGGQKQRVSLARAVYCDRSV 786
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAhlrmPRRVTKKEKRERVDEVLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 787 YLLDDPLSAVDAHVGKHIFdQVIgpQGL-LKDKTRILVTHGLSY--LPQADLVLVMVDGEITEIGS 849
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVV-QVL--KGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1290-1484 |
1.62e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGlHELRSR--ITIIPQD-PVLFSGTLR 1366
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNL----DPFDSYSDEDIwkaLEFSHLKTFVSGLPDK--LSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAA 1440
Cdd:PRK09700 99 ENLyigrHLTKKVCGVNI---IDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1357684105 1441 V-DLETDNL--IQSTIRSqfEDCTVLTIAHRLNTIMDY-TRVLVLDKG 1484
Cdd:PRK09700 176 LtNKEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-844 |
1.73e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 669 GSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAvkgsvayvpqqawiqnatlknnIIFGQKRKESWYQRVveacalqqdl 748
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------YIDGEDILEEVLDQL---------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 749 dilpagDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIGPQGLLKDK---TRILVTH 825
Cdd:smart00382 50 ------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSeknLTVILTT 123
|
170
....*....|....*....
gi 1357684105 826 GLSYLPQADLVLVMVDGEI 844
Cdd:smart00382 124 NDEKDLGPALLRRRFDRRI 142
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1002-1245 |
1.76e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 54.83 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1002 GLGVSQGVAVFGYS-LSVSIGgilaSRFLHQ--SMLFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLipmilkmFMG 1077
Cdd:cd18564 62 GIALLRGLASYAGTyLTALVG----QRVVLDlrRDLFAhLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDL-------LVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1078 SLFNVLGSCVIILVATPMVAFIIPFLGLLYFFVQRFYVASSRQL-KRLESVSR------SPIYTHFNETLLGTSVIRAFG 1150
Cdd:cd18564 131 GVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFsRRIKEASReqrrreGALASVAQESLSAIRVVQAFG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1151 ----EQERFIHESDQRVDHNQKAYYPSIVANRWLAIrLEFVGNCIVSFAALFAVLAREnLSPGIMGLSISYALQLTASLT 1226
Cdd:cd18564 211 reehEERRFARENRKSLRAGLRAARLQALLSPVVDV-LVAVGTALVLWFGAWLVLAGR-LTPGDLLVFLAYLKNLYKPVR 288
|
250
....*....|....*....
gi 1357684105 1227 WLVRMSSDVETNIVAVERV 1245
Cdd:cd18564 289 DLAKLTGRIAKASASAERV 307
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
659-856 |
1.81e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 53.30 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDK--MEGSVAVKG-SVAYVPQQ---------AW-----IQNATLK 721
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGeDITDLPPEerarlgiflAFqyppeIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NniifgqkrkeswYQRVVeacalqqdldilpagdeteigekGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVG 801
Cdd:cd03217 96 D------------FLRYV-----------------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 802 KHIFDQVigpQGLL-KDKTRILVTHG---LSYLpQADLVLVMVDGEITEIGS---YLQLKEE 856
Cdd:cd03217 141 RLVAEVI---NKLReEGKSVLIITHYqrlLDYI-KPDRVHVLYDGRIVKSGDkelALEIEKK 198
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1008-1231 |
2.15e-07 |
|
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: 54.33 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1008 GVAVFGYSLSVsIGGILASRFlhqSMLF------DVLRSPMSF----FERTPSGNLVNRFAKEMDTIDSLIPMILKMFMG 1077
Cdd:cd18548 47 LLALLGLIAGI-LAGYFAAKA---SQGFgrdlrkDLFEKIQSFsfaeIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1078 SLFNVLGSCVIILVATPMVAFI----IPFLGLLYFFVQRF-YVASSRQLKRLESVSRSpiythFNETLLGTSVIRAFG-- 1150
Cdd:cd18548 123 APIMLIGAIIMAFRINPKLALIllvaIPILALVVFLIMKKaIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFNre 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1151 --EQERFIHESDQRVDHNQKayypsivANRWLAIrLEFVGNCIVSFAALFAVL------ARENLSPG-IMGLsISYALQL 1221
Cdd:cd18548 198 dyEEERFDKANDDLTDTSLK-------AGRLMAL-LNPLMMLIMNLAIVAILWfgghliNAGSLQVGdLVAF-INYLMQI 268
|
250
....*....|
gi 1357684105 1222 TASLTWLVRM 1231
Cdd:cd18548 269 LMSLMMLSMV 278
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
659-808 |
2.19e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------------SVAYVPQQAWI-QNATLKNN 723
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFGQ--KRKESWYQRVVEAcalqqdLDILPAGDETEIGEKGvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVG 801
Cdd:PRK11614 101 LAMGGffAERDQFQERIKWV------YELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
....*..
gi 1357684105 802 KHIFDQV 808
Cdd:PRK11614 174 QQIFDTI 180
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
957-1175 |
2.28e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 54.08 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 957 AISLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPDRLMRLGvygglgvsqGVAVFGYSLSvSIGGILASRFLH---QSM 1033
Cdd:cd18778 2 ILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLA---------LLLLGAYLLR-ALLNFLRIYLNHvaeQKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFDvLRS---------PMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFI----I 1100
Cdd:cd18778 72 VAD-LRSdlydklqrlSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLtlipI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1101 PFLGLLyffvQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFG----EQERFIHESDQRVDHNQKA------Y 1170
Cdd:cd18778 151 PFLALG----AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGreeeEAKRFEALSRRYRKAQLRAmklwaiF 226
|
....*
gi 1357684105 1171 YPSIV 1175
Cdd:cd18778 227 HPLME 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
660-847 |
3.12e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 660 KRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV--------------AVKGSVAYVPQQ----AWIQNATLK 721
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkdisprspldAVKKGMAYITESrrdnGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFGQKRKESWY------------QRVVEAcaLQQDLDILPAGDETEIGEkgvnLSGGQKQRVSLARAVYCDRSVYLL 789
Cdd:PRK09700 360 QNMAISRSLKDGGYkgamglfhevdeQRTAEN--QRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 790 DDPLSAVDAHVGKHIFD--QVIGPQGllkdKTRILVThglSYLPQ----ADLVLVMVDGEITEI 847
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKvmRQLADDG----KVILMVS---SELPEiitvCDRIAVFCEGRLTQI 490
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
649-853 |
3.18e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 649 FSWSRSESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------SVAYVPQQAWIQNATL 720
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 721 KN--------------NIIF--GQKRKES--WYQRVVEACALQQDLDILpagDETEIGEKGV-------NLSGGQKQRVS 775
Cdd:PRK10261 102 RGadmamifqepmtslNPVFtvGEQIAESirLHQGASREEAMVEAKRML---DQVRIPEAQTilsryphQLSGGMRQRVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 776 LARAVYCDRSVYLLDDPLSAVDAHVGKHIFdQVIgpQGLLKDKTR--ILVTHGLSYLPQ-ADLVLVMVDGEITEIGSYLQ 852
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQIL-QLI--KVLQKEMSMgvIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQ 255
|
.
gi 1357684105 853 L 853
Cdd:PRK10261 256 I 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1281-1488 |
3.44e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1281 LRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIePAEGQISIDGVDIAKLGLHEL---RSRITIIPQD 1357
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 PvlfSGTL--RMNLdpfdsysDEDIWKALEFsHLKTFVS--------------GL-PDKLSHECSEggenLSVGQRQLLC 1420
Cdd:PRK15134 371 P---NSSLnpRLNV-------LQIIEEGLRV-HQPTLSAaqreqqviavmeevGLdPETRHRYPAE----FSGGQRQRIA 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1421 LARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS--QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAE 1488
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLHVVRALChQVIVLRQGEVVE 506
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
655-849 |
3.92e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 53.63 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVK--------------------GSVAYVPQQAW 714
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdkyirpvrkriGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 715 IQNaTLKNNIIFGQKrkeSWYQRVVEACALQQDLdILPAGDETEIGEKG-VNLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:PRK13646 99 FED-TVEREIIFGPK---NFKMNLDEVKNYAHRL-LMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 794 SAVDAHvGKHIFDQVIGPQGLLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK13646 174 AGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTS 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1497 |
4.20e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.49 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1289 LAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIdGVDIAKLG-----LHELRSRITIIPQDP--VLF 1361
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkLKPLRKKVGIVFQFPehQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1362 SGTLR-------MNldpFDSYSDEDIWKALEFSHLktfvSGLPDKLSHECSeggENLSVGQRQLLCLARALLRKTKVLVL 1434
Cdd:PRK13634 100 EETVEkdicfgpMN---FGVSEEDAKQKAREMIEL----VGLPEELLARSP---FELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1435 DEATAAVD----LETDNLIQSTIRSQfeDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIA 1497
Cdd:PRK13634 170 DEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYAdQIVVMHKGTVFLQGTPREIFA 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1290-1342 |
4.20e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.92 E-value: 4.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtlgLfRII----EPAEGQISIDGVDIAKL 1342
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTL---L-RMIagleDPTSGEILIGGRDVTDL 70
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1290-1498 |
4.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG----LHELRSRITIIPQDP--VLFSG 1363
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 TLRMNL----DPFDSYSDEdiwkALEFSHLKTFVSGlpdkLSHECSEGGE-NLSVGQRQLLCLARALLRKTKVLVLDEAT 1438
Cdd:PRK13643 101 TVLKDVafgpQNFGIPKEK----AEKIAAEKLEMVG----LADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1439 AAVD----LETDNLIQSTIRSqfeDCTVLTIAHRLNTIMDYTR-VLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:PRK13643 173 AGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
950-1171 |
4.69e-07 |
|
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: 53.25 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 950 AIGVLLSAIS-----LLFFLSHNLLSMFANYWLSLWTDDPVVngtqpDRLMRLGVY-GGLGVSQGVAVFGYSLSVSIGGI 1023
Cdd:cd18577 2 IIGLLAAIAAgaalpLMTIVFGDLFDAFTDFGSGESSPDEFL-----DDVNKYALYfVYLGIGSFVLSYIQTACWTITGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1024 LASRFLHQSMLFDVLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATPMVAFI---- 1099
Cdd:cd18577 77 RQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVllat 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1100 IPFLGLLYFFVQRFYV-ASSRQLKRLESVSrspiyTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYY 1171
Cdd:cd18577 157 LPLIAIVGGIMGKLLSkYTKKEQEAYAKAG-----SIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGI 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1286-1492 |
4.75e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1286 DLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHelRSRITIIPQDPVLFSG-T 1364
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 LRMNLD--------PFDSYSDEdIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLARALLRKTKVLVLDE 1436
Cdd:PRK11607 108 VEQNIAfglkqdklPKAEIASR-VNEMLGLVHMQEFAKRKPHQLSG-----------GQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1437 ATAAVDLETDNLIQSTIRSQFE--DCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSP 1492
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEP 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1290-1486 |
5.11e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.18 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHE---LRSRITIIPQDPVLFsgtlr 1366
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLL----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNLDPFDSYSDEDIWKALEFSHLKTFVSGLPDK--LSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDle 1444
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKvgLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1357684105 1445 tDNLIQSTIRsQFED-----CTVLTIAHRLNTIMDYT-RVLVLDKGQM 1486
Cdd:PRK10908 170 -DALSEGILR-LFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
950-1168 |
5.83e-07 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 52.80 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 950 AIGVLLSAISllfflshNLLSMFANYWLSLWTDDPVVNGTQPDRLMRLGVYGgLGVSQGVAVFGYSLSVSIGGilASRFL 1029
Cdd:cd18541 2 LLGILFLILV-------DLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLI-LLLALLIGIFRFLWRYLIFG--ASRRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1030 HQSM---LFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIdslipmilKMFMG----SLFNVLGSCVIILVA--------T 1093
Cdd:cd18541 72 EYDLrndLFAhLLTLSPSFYQKNRTGDLMARATNDLNAV--------RMALGpgilYLVDALFLGVLVLVMmftispklT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1094 PMVAFIIPFLGLL-YFFVQRFYVassRQLKRLESVSRspIYTHFNETLLGTSVIRAFG----EQERFIHESDQRVDHNQK 1168
Cdd:cd18541 144 LIALLPLPLLALLvYRLGKKIHK---RFRKVQEAFSD--LSDRVQESFSGIRVIKAFVqeeaEIERFDKLNEEYVEKNLR 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1290-1488 |
6.24e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG---LHELRSRITIIPQDPVlfsgtlr 1366
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNLDPFDSYSDEdIWKAL-------------EFSHLKTFVSGLPD---KLSHEcseggenLSVGQRQLLCLARALLRKTK 1430
Cdd:PRK10261 412 ASLDPRQTVGDS-IMEPLrvhgllpgkaaaaRVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1431 VLVLDEATAAVDLETDNLIQSTIRSQFEDCTV--LTIAHRLNTIMDYT-RVLVLDKGQMAE 1488
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVE 544
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
657-799 |
7.28e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 52.05 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGemdkmeGSVAVKGSVAYVPQQAWIQNATLKNNIIFGQKRKE---- 732
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG------NYLPDSGSILVRHDGGWVDLAQASPREILALRRRTigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 733 SWYQRVV-------------------EACALQQDLDILpagDETEIGEKGVNL-----SGGQKQRVSLARAVYCDRSVYL 788
Cdd:COG4778 99 SQFLRVIprvsaldvvaepllergvdREEARARARELL---ARLNLPERLWDLppatfSGGEQQRVNIARGFIADPPLLL 175
|
170
....*....|.
gi 1357684105 789 LDDPLSAVDAH 799
Cdd:COG4778 176 LDEPTASLDAA 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1274-1340 |
7.63e-07 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 50.14 E-value: 7.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1274 IHITNFGLRYrSDLDLaIRNINVDISGGEKVGIVGRTGAGKSSltlgLFRII----EPAEGQI-SIDGVDIA 1340
Cdd:cd03221 1 IELENLSKTY-GGKLL-LKDISLTINPGDRIGLVGRNGAGKST----LLKLIagelEPDEGIVtWGSTVKIG 66
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
959-1245 |
7.68e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 52.55 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 959 SLLFFLSHNLLSMFANYWLSLWTDDPVVNGTQPDRLMRLGVYGGLGVSQGVAVF--GYSLSVsIGGILASRFlhQSMLFD 1036
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGlrGGCFSY-AGTRLVRRL--RRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 -VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATP---MVAFII-PFLGLLYFFVQ 1111
Cdd:cd18572 78 sLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltLLAFITvPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1112 RFYvassRQLKRLESVSRSPIYTHFNETLLGTSVIRAFG----EQERFIHESDQRVDHNQK---AYypsiVANRWLAIRL 1184
Cdd:cd18572 158 RYY----RKLSKEIQDALAEANQVAEEALSNIRTVRSFAteerEARRYERALDKALKLSVRqalAY----AGYVAVNTLL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1185 EFVGNCIVSFAALFAVLAREnLSPGIMglsISYAL---QLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18572 230 QNGTQVLVLFYGGHLVLSGR-MSAGQL---VTFMLyqqQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1292-1487 |
9.98e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHE-LRSRITIIPQD---PVLF-SGTLR 1366
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqsSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1367 MNLDPFdSYSDEDIW--KALEFSHLKTFVSGLPDKLSHECSEGGeNLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLE 1444
Cdd:PRK15439 360 WNVCAL-THNRRGFWikPARENAVLERYRRALNIKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1357684105 1445 TDNLIQSTIRSQFEDCT-VLTIAHRLNTIMDYT-RVLVLDKGQMA 1487
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEIS 482
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1292-1482 |
1.17e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSLtlglFRII----EPAEGQISIDGVDIAKLGlHELRsritiipQDpVLFSG---- 1363
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSL----LRILaglaRPDAGEVLWQGEPIRRQR-DEYH-------QD-LLYLGhqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 ---------TLRMNLDPFDSYSDEDIWKALEfshlKTFVSGLPDKLSHecseggeNLSVGQRQLLCLARALLRKTKVLVL 1434
Cdd:PRK13538 85 ikteltaleNLRFYQRLHGPGDDEALWEALA----QVGLAGFEDVPVR-------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1435 DEATAAVDLETDNLIQSTIRSQFED--CTVLTIAHRLNTIMDYTRVLVLD 1482
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1290-1484 |
1.42e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELrsrITIIPQD-------PVLFS 1362
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 GTLRMNldpfdSYSDEDiWKALEFSHLKTFVSGL---PDKLSHECSEGGEnLSVGQRQLLCLARALLRKTKVLVLDEATA 1439
Cdd:PRK15056 99 DVVMMG-----RYGHMG-WLRRAKKRDRQIVTAAlarVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1357684105 1440 AVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDYTRVLVLDKG 1484
Cdd:PRK15056 172 GVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1037-1245 |
1.60e-06 |
|
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: 51.67 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATP----MVAFIIPFLGLLYFFV-Q 1111
Cdd:cd18551 79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWvltlVTLAVVPLAFLIILPLgR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1112 RFYVASSRQLKRLESVSrspiyTHFNETLLGTSVIRAFGEQERfihESDQRVDHNQKAYYPSIVANRWLAIRLEFVGncI 1191
Cdd:cd18551 159 RIRKASKRAQDALGELS-----AALERALSAIRTVKASNAEER---ETKRGGEAAERLYRAGLKAAKIEALIGPLMG--L 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1192 VSFAALFAVL----ARenLSPGIMGLS-----ISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18551 229 AVQLALLVVLgvggAR--VASGALTVGtlvafLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
661-872 |
1.73e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 661 RLNVRVP---EGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG-SVAYVPQQawiqnatlknniifgqkrkeswyq 736
Cdd:cd03222 14 FLLVELGvvkEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY------------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 737 rvveacalqqdldilpagdeteigekgVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIfDQVIGPQGLLK 816
Cdd:cd03222 70 ---------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEEG 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 817 DKTRILVTHGLSYLPQADLVLVMVDGEITEIGSYLQLKEEEGAFAEFLRTYASSEQ 872
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1288-1454 |
1.81e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.26 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1288 DLAIRNINVDISGGEKVGIVGRTGAGKSSL--TL-GLFRiiePAEGQISIDGVDIaklGLHELRSRITII-PQD---PVL 1360
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrLIaGLLP---PAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1361 fsgTLRMNLD---PFDSYSDEDIWKALEFSHLKTfVSGLPdklshecsegGENLSVGQRQLLCLARALLRKTKVLVLDEA 1437
Cdd:PRK13539 89 ---TVAENLEfwaAFLGGEELDIAAALEAVGLAP-LAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|....*..
gi 1357684105 1438 TAAVDLETDNLIQSTIR 1454
Cdd:PRK13539 155 TAALDAAAVALFAELIR 171
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
659-864 |
1.81e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 52.50 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGeMDKMEG-SVAVKGSVAYVPQQAWIQ--------------------- 716
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG-MDQYEPtSGRIIYHVALCEKCGYVErpskvgepcpvcggtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 -----------NATLKNNIIFgqKRKESWY--QRVVEAC-------------ALQQDLDILpagDETEIGEK----GVNL 766
Cdd:TIGR03269 95 dfwnlsdklrrRIRKRIAIML--QRTFALYgdDTVLDNVlealeeigyegkeAVGRAVDLI---EMVQLSHRithiARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 767 SGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIgpQGLLKDKTRILVThglSYLPQ-----ADLVLVMVD 841
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLT---SHWPEviedlSDKAIWLEN 244
|
250 260 270
....*....|....*....|....*....|
gi 1357684105 842 GEITEIGS-------YLQLKEEEGAFAEFL 864
Cdd:TIGR03269 245 GEIKEEGTpdevvavFMEGVSEVEKECEVE 274
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1287-1486 |
1.94e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 49.74 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1287 LDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHE-LRSRITIIPQDP----VLF 1361
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRkregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1362 SGTLRMNLdpfdsysdediwkalefshlktfvsGLPDKLShecseGGeN---LSVGQrqllclarALLRKTKVLVLDEAT 1438
Cdd:cd03215 92 DLSVAENI-------------------------ALSSLLS-----GG-NqqkVVLAR--------WLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1439 AAVDLETDNLIQSTIRSQFED-CTVLTIAHRLNTIM---DytRVLVLDKGQM 1486
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLglcD--RILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
662-797 |
1.96e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.66 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAV--------------KGSVAYVPQQAWI-QNATLKNNII- 725
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDNLMa 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 726 FGQKRKE-SWYQRVVEACALQQDLDILPAGDETeigekGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:PRK10895 102 VLQIRDDlSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1290-1439 |
2.00e-06 |
|
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: 50.75 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHEL-RSRITIIPQDPVLFSG-TLRM 1367
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1368 NLD------PFDSYSDEDIWKALE-FSHLKTFVSglpdklshecSEGGeNLSVGQRQLLCLARALLRKTKVLVLDEATA 1439
Cdd:COG0410 98 NLLlgayarRDRAEVRADLERVYElFPRLKERRR----------QRAG-TLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1290-1442 |
2.41e-06 |
|
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: 49.95 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHElRSrITIIPQDPVLF-------- 1361
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAMVFQNYALYphmtvydn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1362 -SGTLRMNLDPFDSYSD--EDIWKALEFSHLktfvsglpdkLSHECSEggenLSVGQRQLLCLARALLRKTKVLVLDEAT 1438
Cdd:cd03301 93 iAFGLKLRKVPKDEIDErvREVAELLQIEHL----------LDRKPKQ----LSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
....
gi 1357684105 1439 AAVD 1442
Cdd:cd03301 159 SNLD 162
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1291-1485 |
2.51e-06 |
|
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: 50.47 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLtLGL-FRIIEPAEGQ-ISIDGVDIAKLGLHELRSRI---------TIIPQDPV 1359
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTL-LSLiTGDLPPTYGNdVRLFGERRGGEDVWELRKRIglvspalqlRFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1360 L------FSGTLrmnlDPFDSYSDEDIWKALEfsHLKTF-VSGLPDKLSHECSEGgenlsvgQRQLLCLARALLRKTKVL 1432
Cdd:COG1119 98 LdvvlsgFFDSI----GLYREPTDEQRERARE--LLELLgLAHLADRPFGTLSQG-------EQRRVLIARALVKDPELL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1433 VLDEATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHRLNTIMD-YTRVLVLDKGQ 1485
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDklAAEGAPTLVLVTHHVEEIPPgITHVLLLKDGR 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1290-1495 |
2.54e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 51.25 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtlgLfRII----EPAEGQISIDGVDIAKLGLHElRsRITIIPQDPVLFS--- 1362
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL---L-RMIagfeTPDSGRILLDGRDVTGLPPEK-R-NVGMVFQDYALFPhlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 -------GtLRMnldpfDSYSDEDIWK----ALEFSHLktfvSGLPDKLSHEcseggenLSVGQRQ---------Llcla 1422
Cdd:COG3842 94 vaenvafG-LRM-----RGVPKAEIRArvaeLLELVGL----EGLADRYPHQ-------LSGGQQQrvalaralaP---- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1423 rallrKTKVLVLDEATAAVDLETDNLIQSTIRSQFEDC--TVLTIAHRLN---TIMDytRVLVLDKGQMAEFDSPSSL 1495
Cdd:COG3842 153 -----EPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealALAD--RIAVMNDGRIEQVGTPEEI 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
661-848 |
2.61e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 661 RLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDkMEGSVA----------------------VKGSVAYVPQQAWIQ-- 716
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaeklefngqdlqrisekerrnlVGAEVAMIFQDPMTSln 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 717 -NATLKNNIIFGQK-----RKESWYQRVVEACAL------QQDLDILPAgdeteigekgvNLSGGQKQRVSLARAVYCDR 784
Cdd:PRK11022 104 pCYTVGFQIMEAIKvhqggNKKTRRQRAIDLLNQvgipdpASRLDVYPH-----------QLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 785 SVYLLDDPLSAVDAHVGKHIFDQVIGPQGlLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIG 848
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQ-KENMALVLITHDLALVAEaAHKIIVMYAGQVVETG 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
657-778 |
2.85e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--------------VAYVPQ----QAWIQNA 718
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDM 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 719 TLKNNIIFGQKRKESW-------YQRVVEACA-LQQDLDILPAGDETEIGekgvNLSGGQKQRVSLAR 778
Cdd:COG3845 352 SVAENLILGRYRRPPFsrggfldRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGNQQKVILAR 415
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1034-1245 |
3.03e-06 |
|
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: 50.88 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFDVLRS-PMSFFERTPSGNLVNRFAKEMD-TIDSLIP--MILKMFMGSLFNVLGscvIILVATPMVAFIIPFLGLLYFF 1109
Cdd:cd18554 85 LFDHLQKlSLRYYANNRSGEIISRVINDVEqTKDFITTglMNIWLDMITIIIAIC---IMLVLNPKLTFVSLVIFPFYIL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1110 VQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQErfiHESDQRVDHNQKAYYPSIVANRWLAIRLEFVGN 1189
Cdd:cd18554 162 AVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEK---HEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNT 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1190 C-------IVSFAALFAVLAreNLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18554 239 ItdlapllVIGFAAYLVIEG--NLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
662-845 |
3.12e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRvpEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG--------------SVAYVP----QQAWIQNATLKNN 723
Cdd:PRK11288 274 FSVR--AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidirsprdairaGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFGQKRKESWYQRVVE-------ACALQQDLDILPAGDETEIGekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAV 796
Cdd:PRK11288 352 INISARRHHLRAGCLINnrweaenADRFIRSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 797 DahVG-KHIFDQVIgpQGLLKDKTRILVTHglSYLPQ----ADLVLVMVDGEIT 845
Cdd:PRK11288 428 D--VGaKHEIYNVI--YELAAQGVAVLFVS--SDLPEvlgvADRIVVMREGRIA 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
656-844 |
3.25e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 656 SPTLKRLN---VRVPEGSLVAVVGHVGSGKSSLLSALLGEMD-KMEGSV--------------AVKGSVAYVPQ----QA 713
Cdd:TIGR02633 270 NPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVfingkpvdirnpaqAIRAGIAMVPEdrkrHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 714 WIQNATLKNNIIFGQKRKESWYQRVVEACALQ------QDLDILPAGDETEIGekgvNLSGGQKQRVSLARAVYCDRSVY 787
Cdd:TIGR02633 350 IVPILGVGKNITLSVLKSFCFKMRIDAAAELQiigsaiQRLKVKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 788 LLDDPLSAVDAHVGKHIFdQVIGpqGLLKDKTRILVTHglSYLPQ----ADLVLVMVDGEI 844
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIY-KLIN--QLAQEGVAIIVVS--SELAEvlglSDRVLVIGEGKL 481
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
655-849 |
3.68e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.61 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKS-SLLSA--LLGEmdkmeGSVAVKGSVAYVPQQawIQNATLK-------NNI 724
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrLLPD-----PAAHPSGSILFDGQD--LLGLSERelrrirgNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 725 --IF-------------GQKRKES--WYQRVVEACALQQDLDILpagDETEI--GEKGVN-----LSGGQKQRVSLARAV 780
Cdd:COG4172 95 amIFqepmtslnplhtiGKQIAEVlrLHRGLSGAAARARALELL---ERVGIpdPERRLDayphqLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 781 YCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1292-1350 |
3.93e-06 |
|
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: 49.74 E-value: 3.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1292 RNINVDISGGEKVGIVGRTGAGKSSLtLGLFRIIE-PAEGQISIDGVDIAKL---GLHELRSR 1350
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDrPTSGTVRLAGQDLFALdedARARLRAR 90
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1280-1497 |
3.93e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.57 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1280 GLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGlHELRSRITIIPQ--- 1356
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGVVPQfdn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1357 -DPVLfsgTLRMNLDPFDSY-------SDEDIWKALEFSHLKTfvsglpdKLSHECSEggenLSVGQRQLLCLARALLRK 1428
Cdd:PRK13537 91 lDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1429 TKVLVLDEATAAVDLETDNLIQSTIRSQF-EDCTVLTIAH------RLntimdYTRVLVLDKGQMAEFDSPSSLIA 1497
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1273-1486 |
4.03e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1273 CIHITNfglRYRSDLDlairNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPA-EGQISIDG--VDIaKLGLHELRS 1349
Cdd:TIGR02633 265 CWDVIN---PHRKRVD----DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDI-RNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1350 RITIIPQD-------PVLFSG---TLRMnLDPF------DSYSDED-IWKALEFSHLKTFVSGLPDKlshecseggeNLS 1412
Cdd:TIGR02633 337 GIAMVPEDrkrhgivPILGVGkniTLSV-LKSFcfkmriDAAAELQiIGSAIQRLKVKTASPFLPIG----------RLS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1413 VGQRQLLCLARALLRKTKVLVLDEATAAVDL----ETDNLIQSTIRsqfEDCTVLTIAHRLNTIMDYT-RVLVLDKGQM 1486
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVgakyEIYKLINQLAQ---EGVAIIVVSSELAEVLGLSdRVLVIGEGKL 481
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1276-1358 |
4.33e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.22 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1276 ITNFGLRYRSDLDL--AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEP----AEGQISIDGVDIAKLGLHELR- 1348
Cdd:COG4172 9 VEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRr 88
|
90
....*....|...
gi 1357684105 1349 ---SRITIIPQDP 1358
Cdd:COG4172 89 irgNRIAMIFQEP 101
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1290-1488 |
4.67e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG----------VDIAKLGLHELR----SRITIIP 1355
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1356 QDPVlfsgtlrMNLDPFDSYSD---EDIWKALEFSHLKTFVSG--------LPDklSHEC-SEGGENLSVGQRQLLCLAR 1423
Cdd:PRK10261 111 QEPM-------TSLNPVFTVGEqiaESIRLHQGASREEAMVEAkrmldqvrIPE--AQTIlSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1424 ALLRKTKVLVLDEATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAE 1488
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIAdRVLVMYQGEAVE 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1262-1442 |
5.21e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1262 PTVPPDWPTegcIHITNFGLRYrSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTL---GLFRiiePAEGQISIDGVD 1338
Cdd:PRK10522 314 PQAFPDWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMlltGLYQ---PQSGEILLDGKP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1339 IAKLGLHELRSRITIIPQDPVLFSGTLRMNLDPFDsysDEDIWKALEfsHLKtfvsgLPDKLSHecsEGGE----NLSVG 1414
Cdd:PRK10522 387 VTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPAN---PALVEKWLE--RLK-----MAHKLEL---EDGRisnlKLSKG 453
|
170 180
....*....|....*....|....*...
gi 1357684105 1415 QRQLLCLARALLRKTKVLVLDEATAAVD 1442
Cdd:PRK10522 454 QKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
645-867 |
5.37e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 645 EDGVFSWSrsesptLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVP-------QQAWIQN 717
Cdd:PRK13545 32 KDGEYHYA------LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAissglngQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 718 ATLKnNIIFGQKRKEswyqrvveacaLQQdldILPAGDE-TEIGeKGVN-----LSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:PRK13545 106 IELK-GLMMGLTKEK-----------IKE---IIPEIIEfADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 792 PLSAVDAHVGKHIFDQV--IGPQGllkdKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGSylqLKEEEGAFAEFLRTY 867
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMneFKEQG----KTIFFISHSLSQVKSfCTKALWLHYGQVKEYGD---IKEVVDHYDEFLKKY 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1290-1492 |
5.71e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.09 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSS----LTlGlfrIIEPAEGQISIDGVDIAKLgLHELRSRITiipqdpVLFsG-- 1363
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTtikmLT-G---ILVPTSGEVRVLGYVPFKR-RKEFARRIG------VVF-Gqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 -TLRMNLDPFDSYS--------DEDIWKAlefsHLKTFVSGLpdklshecsEGGE-------NLSVGQRqllclarallR 1427
Cdd:COG4586 105 sQLWWDLPAIDSFRllkaiyriPDAEYKK----RLDELVELL---------DLGElldtpvrQLSLGQR----------M 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1428 KT----------KVLVLDEATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAeFDSP 1492
Cdd:COG4586 162 RCelaaallhrpKILFLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEALcDRVIVIDHGRII-YDGS 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1293-1482 |
6.26e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1293 NINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQIsidgvdiaklgLHELRSRITIIPQ----DPVLFSGTLR-M 1367
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTLPLTVNRfL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1368 NLDPfdSYSDEDIWKALEFSHLKTFVSGLPDKLShecseGGENlsvgqrQLLCLARALLRKTKVLVLDEATAAVD----L 1443
Cdd:PRK09544 91 RLRP--GTKKEDILPALKRVQAGHLIDAPMQKLS-----GGET------QRVLLARALLNRPQLLVLDEPTQGVDvngqV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1357684105 1444 ETDNLIQStIRSQFeDCTVLTIAHRLNTIMDYT-RVLVLD 1482
Cdd:PRK09544 158 ALYDLIDQ-LRREL-DCAVLMVSHDLHLVMAKTdEVLCLN 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
657-857 |
6.71e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--------------VAYVPQQAWI-QNATLK 721
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 722 NNIIFGQKRKESWYQRVVEACAL---QQDLDIlPAGdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDA 798
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAAlgcQLDLDS-SAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 799 HVGKHIFDQVigpQGLLKDKTRIL-VTHGLSYLPQ-ADLVLVMVDGEITEIGSYLQLKEEE 857
Cdd:PRK15439 174 AETERLFSRI---RELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1288-1468 |
7.08e-06 |
|
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: 50.52 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1288 DLAIRNINVDISGGEKVGIVGRTGAGKSSLtlglFRIIepAE------GQISIDGvdiaklglhelRSRITIIPQDPVLF 1361
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRIL--GElwpvygGRLTKPA-----------KGKLFYVPQRPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1362 SGTLR------MNLDPF--DSYSDEDIWKALEFSHLKTFVSglpdklshecSEGG--------ENLSVGQRQLLCLARAL 1425
Cdd:TIGR00954 528 LGTLRdqiiypDSSEDMkrRGLSDKDLEQILDNVQLTHILE----------REGGwsavqdwmDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1357684105 1426 LRKTKVLVLDEATAAVDLETDNLIqstirsqFEDC-----TVLTIAHR 1468
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1290-1347 |
9.51e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 48.58 E-value: 9.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISID----GVDIAKLGLHEL 1347
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREI 87
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
674-849 |
1.15e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.08 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 674 VVGHVGSGKSSLLSALLGEMDKMEGSVAVK----------GSVAYVPQQAWIQNA---------------------TLKN 722
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNFkelrrrvsmvfqfpeyqlfkdTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 723 NIIFG-----QKRKESwYQRV---VEACALQQD-LDILPAGdeteigekgvnLSGGQKQRVSLARAVYCDRSVYLLDDPL 793
Cdd:PRK13631 137 DIMFGpvalgVKKSEA-KKLAkfyLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPT 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 794 SAVDAHvGKHIFDQVIgPQGLLKDKTRILVTHGLSY-LPQADLVLVMVDGEITEIGS 849
Cdd:PRK13631 205 AGLDPK-GEHEMMQLI-LDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1002-1169 |
1.24e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 48.99 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1002 GLGVSQGVAVF--GYSLSVSiGGILASRFlhQSMLFD-VLRSPMSFFERTP--SGNLVNRFAKEMDTIDSLIPMILKMFM 1076
Cdd:cd18578 60 VLAIVAGIAYFlqGYLFGIA-GERLTRRL--RKLAFRaILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLIL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1077 GSLFNVLGSCVIILVATPMVAFI----IPFLGLLYFFVQRFYVASSRQLKR-LESVSRspiytHFNETLLGTSVIRAFGE 1151
Cdd:cd18578 137 QAIVTLVAGLIIAFVYGWKLALVglatVPLLLLAGYLRMRLLSGFEEKNKKaYEESSK-----IASEAVSNIRTVASLTL 211
|
170
....*....|....*...
gi 1357684105 1152 QERFIHESDQRVDHNQKA 1169
Cdd:cd18578 212 EDYFLEKYEEALEEPLKK 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1280-1358 |
1.33e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1280 GLRYRSDLDL-AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSR-ITIIPQD 1357
Cdd:COG3845 262 NLSVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPED 341
|
.
gi 1357684105 1358 P 1358
Cdd:COG3845 342 R 342
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1265-1490 |
1.48e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.49 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1265 PPDWPTEGCIHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIE--P---AEGQISIDGVDI 1339
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1340 --AKLGLHELRSRITIIPQDPVLFSGT--------LRMNLDPFDSYSDEDIWKALEFSHL----KtfvsglpDKLShecs 1405
Cdd:COG1117 81 ydPDVDVVELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALwdevK-------DRLK---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1406 EGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVD-LETDNlIQSTIRSQFEDCTVLTIAHRLNT---IMDYTrvLVL 1481
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHNMQQaarVSDYT--AFF 226
|
....*....
gi 1357684105 1482 DKGQMAEFD 1490
Cdd:COG1117 227 YLGELVEFG 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1290-1469 |
1.57e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.23 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRI--IEP---AEGQISIDGVDI--AKLGLHELRSRITIIPQDPVLFS 1362
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1363 GT--------LRMNLDPFDSYSDEDIWKALEFSHLKTFVSglpDKLsHECSEGgenLSVGQRQLLCLARALLRKTKVLVL 1434
Cdd:PRK14239 100 MSiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVK---DRL-HDSALG---LSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1357684105 1435 DEATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRL 1469
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1273-1489 |
1.70e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1273 CIHITNFGLRYRSDLDLAIRNinvdisgGEKVGIVGRTGAGKSSLTLGLFRIIEPA-EGQISIDG--VDIA------KLG 1343
Cdd:PRK13549 267 AWDPVNPHIKRVDDVSFSLRR-------GEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGkpVKIRnpqqaiAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1344 ---LHELRSRITIIPQDPVLFSGTLrMNLDPFDSYSDEDiwKALEFSHLKTFVSGLPDKLSH-ECSEGgeNLSVGQRQLL 1419
Cdd:PRK13549 340 iamVPEDRKRDGIVPVMGVGKNITL-AALDRFTGGSRID--DAAELKTILESIQRLKVKTASpELAIA--RLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1420 CLARALLRKTKVLVLDEATAAVDL----ETDNLIQSTIRsqfEDCTVLTIAHRLNTIMDYT-RVLVLDKGQM-AEF 1489
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQLVQ---QGVAIIVISSELPEVLGLSdRVLVMHEGKLkGDL 487
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1293-1487 |
1.85e-05 |
|
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: 47.29 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1293 NINVDISGgEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDI----AKLGLHELRSRITIIPQDPVLFSG-TLRM 1367
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1368 NLdpfdsysdEDIWKALEFSHLKTFVSGLPD--KLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLET 1445
Cdd:cd03297 95 NL--------AFGLKRKRNREDRISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1357684105 1446 DNLIQSTIRSQFED--CTVLTIAHRLNTIMDYT-RVLVLDKGQMA 1487
Cdd:cd03297 167 RLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLAdRIVVMEDGRLQ 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1291-1498 |
1.97e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.56 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSS---LTLGLFRiiePAEGQISIDGVDIAKlglHELRSR-ITIIPQDPVLFSGT-- 1364
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTvlrLVAGLEK---PTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHMsl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 -------LRMNLDPFDSYSdEDIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLARALLRKTKVLVLDEA 1437
Cdd:PRK11432 96 genvgygLKMLGVPKEERK-QRVKEALELVDLAGFEDRYVDQISG-----------GQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1438 TAAVDLETDNLIQSTIR---SQFeDCTVLTIAHrlntimDYTR-------VLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:PRK11432 164 LSNLDANLRRSMREKIRelqQQF-NITSLYVTH------DQSEafavsdtVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
659-849 |
1.98e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.86 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVK------GSVAYVPQQAwiqnatlknNIIFgQKRKE 732
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRI---------RMIF-QDPST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 733 SW--YQRVveacalQQDLDI---LPAGDETEIGEKGVN-------------------LSGGQKQRVSLARAVYCDRSVYL 788
Cdd:PRK15112 99 SLnpRQRI------SQILDFplrLNTDLEPEQREKQIIetlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 789 LDDPLSAVDAhvgkHIFDQVIGPQGLLKDK---TRILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK15112 173 ADEALASLDM----SMRSQLINLMLELQEKqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1291-1483 |
2.00e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.91 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIE-----PAEGQISIDGVDI--AKLGLHELRSRITIIPQDPVLFSg 1363
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1364 tlrmNLDPFDSY-----------SDEDIWKALEFSHLKtfvSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVL 1432
Cdd:PRK14267 99 ----HLTIYDNVaigvklnglvkSKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1433 VLDEATAAVDLETDNLIQSTIRSQFEDCTVLTIAH---RLNTIMDYTRVLVLDK 1483
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYLGK 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1289-1490 |
2.04e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.85 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1289 LAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFR---IIEP--AEGQISIDGVDIAKLGLH--ELRSRITIIPQDPVLF 1361
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1362 SGTLRMNL------DPFDSYSDEDIWKALEFSHLKTFVSglpDKLShecsEGGENLSVGQRQLLCLARALLRKTKVLVLD 1435
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1436 EATAAVDLETDNLIQSTIRSQFEDCTVLTIAHRLNT---IMDYT---RVLVLDK----GQMAEFD 1490
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMTaffNVELTEGggryGYLVEFD 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
767-849 |
2.10e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.42 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 767 SGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKhifdQVIgpqGLLKDKTR------ILVTHGLSYLPQ-ADLVLVM 839
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQA----QVL---NLMMDLQQelglsyVFISHDLSVVEHiADEVMVM 228
|
90
....*....|
gi 1357684105 840 VDGEITEIGS 849
Cdd:PRK11308 229 YLGRCVEKGT 238
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1290-1488 |
2.21e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSL--TLGLFRIiePAEGQISIDG--VDI-----AKLGLhELRSRITIIPQD--- 1357
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEM--PRSGTLNIAGnhFDFsktpsDKAIR-ELRRNVGMVFQQynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 -PVLfsgTLRMNL--DPF------DSYSDEDIWKALEFSHLKTFVSGLPdklshecseggENLSVGQRQLLCLARALLRK 1428
Cdd:PRK11124 94 wPHL---TVQQNLieAPCrvlglsKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1429 TKVLVLDEATAAVDLETDNLIQSTIRS-QFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAE 1488
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKTaSRVVYMENGHIVE 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
668-872 |
2.26e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 668 EGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--VAYVPQQAwiqnatLKNNI------------IFGQKRKE- 732
Cdd:PRK10762 277 KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDG------LANGIvyisedrkrdglVLGMSVKEn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 733 ----SWYQRVVEACALQQDLDILPAGD------------ETEIGekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAV 796
Cdd:PRK10762 351 msltALRYFSRAGGSLKHADEQQAVSDfirlfniktpsmEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 797 DAHVGKHIFdQVIG---PQGLlkdkTRILVThglSYLPQ----ADLVLVMVDGEITeigsylqlkeeegafAEFLRTYAS 869
Cdd:PRK10762 427 DVGAKKEIY-QLINqfkAEGL----SIILVS---SEMPEvlgmSDRILVMHEGRIS---------------GEFTREQAT 483
|
...
gi 1357684105 870 SEQ 872
Cdd:PRK10762 484 QEK 486
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1034-1245 |
2.49e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 47.86 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATP----MVAFIIPFLGLLYF 1108
Cdd:cd18576 75 LYRhLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltlLMLATVPVVVLVAV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1109 FVQRFYVASSRQlkRLESVSRSpiYTHFNETLLGTSVIRAFG----EQERFihesDQRVDHNQKAyypSIVANRWLAIRL 1184
Cdd:cd18576 155 LFGRRIRKLSKK--VQDELAEA--NTIVEETLQGIRVVKAFTredyEIERY----RKALERVVKL---ALKRARIRALFS 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1185 EFVGNCIvsFAALFAVL---ARE----NLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18576 224 SFIIFLL--FGAIVAVLwygGRLvlagELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
659-805 |
2.63e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV--------------AVKGSVAYVPQQA-WIQNATLKNN 723
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkeidfksskeALENGISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 724 IIFGQKRKESWY------QRVVEACALQQDLDILPAgdeteigEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:PRK10982 94 MWLGRYPTKGMFvdqdkmYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
....*...
gi 1357684105 798 AHVGKHIF 805
Cdd:PRK10982 167 EKEVNHLF 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
659-853 |
3.28e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.40 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEG-------------------SVAVKGSVAYVPQQAWIQNAT 719
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 720 LKNNIIFGQKRKESWYQRVVEACALQQDLDI-LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDA 798
Cdd:PRK14271 117 IMDNVLAGVRAHKLVPRKEFRGVAQARLTEVgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 799 HVGKHIFDQVigpQGLLKDKTRILVTHGLSYLPQ-ADLVLVMVDGEITEIGSYLQL 853
Cdd:PRK14271 197 TTTEKIEEFI---RSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1301-1481 |
3.37e-05 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 46.33 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1301 GEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHELRSRITIIPQDPVLFSGTLRMNLDPF-DSYSDED 1379
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWhADHSDEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1380 IWKALEFSHLktfvSGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQFED 1459
Cdd:cd03231 106 VEEALARVGL----NGFEDRPVAQ-------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCAR 174
|
170 180
....*....|....*....|....
gi 1357684105 1460 --CTVLTIAHRLNTIMDYTRVLVL 1481
Cdd:cd03231 175 ggMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1034-1245 |
3.92e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 47.48 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1034 LFD-VLRSPMSFFERTPSGNLVNRFAKEMDTIDSLIPMILKMFMGSLFNVLGSCVIILVATP----MVAFIIPF-LGLLY 1107
Cdd:cd18575 75 VFAhLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltlLVLLVIPLvVLPII 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1108 FFVQRFYVASSRQLKRLESVSrspiyTHFNETLLGTSVIRAFGEQERFIHESDQRVDhnqKAYypsIVANRWLAIRLEFV 1187
Cdd:cd18575 155 LFGRRVRRLSRASQDRLADLS-----AFAEETLSAIKTVQAFTREDAERQRFATAVE---AAF---AAALRRIRARALLT 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1188 GNCIV-SFAALFAVL---ARE----NLSPGIMGLSISYALQLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18575 224 ALVIFlVFGAIVFVLwlgAHDvlagRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
656-849 |
4.01e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.00 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 656 SPTLKRlnvrvpeGSLVAVVGHVGSGKSSLLSALLGEM----DKMEGSVAVKGsVAYVPQQ------AWI-QNA------ 718
Cdd:PRK10418 23 SLTLQR-------GRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDG-KPVAPCAlrgrkiATImQNPrsafnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 719 --TLKNNII-----FGQKRKESWYQRVVEACALQQDLDILPAgdeteigeKGVNLSGGQKQRVSLARAVYCDRSVYLLDD 791
Cdd:PRK10418 95 lhTMHTHARetclaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 792 PLSAVDAHVGKHIFD------QVIGPqGLLkdktriLVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK10418 167 PTTDLDVVAQARILDllesivQKRAL-GML------LVTHDMGVVARlADDVAVMSHGRIVEQGD 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1291-1510 |
4.60e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLtLGLF--RIIEPAE-------GQISIDGVDIAKLGLHELRSRITIIPQ--DPV 1359
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTL-LKALagDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1360 L-FSGTLRMNLDPF--------DSYSDEDI-WKALEFSHLKTFVSGLPDKLShecseGGENLSVGQRQLLCL---ARALL 1426
Cdd:PRK13547 96 FaFSAREIVLLGRYpharragaLTHRDGEIaWQALALAGATALVGRDVTTLS-----GGELARVQFARVLAQlwpPHDAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1427 RKTKVLVLDEATAAVDLETDNLIQSTIRSQFED--CTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPS-----SLIAQ 1498
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHAdRIAMLADGAIVAHGAPAdvltpAHIAR 250
|
250
....*....|..
gi 1357684105 1499 KGAFYRMAKDAG 1510
Cdd:PRK13547 251 CYGFAVRLVDAG 262
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1291-1472 |
4.62e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG---LHELRsrITIIPQDPVLFSgtlrm 1367
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG--IYLVPQEPLLFP----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1368 NLDpfdsySDEDIW-----KALEFSHLKTFVSGLPDKLSHECSEGgeNLSVGQRQLLCLARALLRKTKVLVLDEATAAVD 1442
Cdd:PRK15439 100 NLS-----VKENILfglpkRQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190
....*....|....*....|....*....|..
gi 1357684105 1443 -LETDNLIQStIRS-QFEDCTVLTIAHRLNTI 1472
Cdd:PRK15439 173 pAETERLFSR-IRElLAQGVGIVFISHKLPEI 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
655-797 |
4.95e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.10 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 655 ESPTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS------VAYVPQQAWI-------QNATLK 721
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghrsginPYLTLR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 722 NNIIFgQKRKESWYQRVVEAC---ALQQDLDiLPAGdeteigekgvNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:PRK13540 93 ENCLY-DIHFSPGAVGITELCrlfSLEHLID-YPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1290-1488 |
5.18e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIE-----PAEgQISIDGVDIAKLGLHELR----SRITIIPQDPVl 1360
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvMAE-KLEFNGQDLQRISEKERRnlvgAEVAMIFQDPM- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1361 fsgtlrMNLDPfdSYS-DEDIWKALEFSH-------------LKTFVsGLPDKLS------HEcseggenLSVGQRQLLC 1420
Cdd:PRK11022 100 ------TSLNP--CYTvGFQIMEAIKVHQggnkktrrqraidLLNQV-GIPDPASrldvypHQ-------LSGGMSQRVM 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1421 LARALLRKTKVLVLDEATAAVDLEtdnlIQSTI------RSQFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAE 1488
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVT----IQAQIiellleLQQKENMALVLITHDLALVAEAAhKIIVMYAGQVVE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1492 |
5.69e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.15 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDI-AKLGLH---------------ELRSRITI 1353
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgDKKNNHelitnpyskkiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1354 IPQDP--VLFSGTLR-------MNLDPFDSYSDEDIWKALEFSHLK-TFVSGLPDKLSHecseggenlsvGQRQLLCLAR 1423
Cdd:PRK13631 121 VFQFPeyQLFKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSG-----------GQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1424 ALLRKTKVLVLDEATAAVDLETDN-LIQSTIRSQFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSP 1492
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILKTGTP 260
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
766-849 |
6.65e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 46.65 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 766 LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKhifdQVIgpqGLLKD------KTRILVTHGLS---YLpqADLV 836
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQA----QVL---NLLEDlqdelgLTYLFISHDLSvvrHI--SDRV 228
|
90
....*....|...
gi 1357684105 837 LVMVDGEITEIGS 849
Cdd:COG4608 229 AVMYLGKIVEIAP 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1301-1358 |
6.69e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.88 E-value: 6.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 1301 GEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIA---KLGLHELRSRITIIPQDP 1358
Cdd:PRK11308 41 GKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP 101
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
659-797 |
7.63e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--VAYVPQQAWIqNATLKNNIifgqkrkeswyQ 736
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL-DTTLPLTV-----------N 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 737 RVVEACALQQDLDILPAGDETEIG-------EKgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:PRK09544 88 RFLRLRPGTKKEDILPALKRVQAGhlidapmQK---LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1037-1245 |
8.43e-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: 46.28 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 VLRSPMSFFERTPSGNLVNRFakeMDTI-------DSLIPMILKMFMgslfnVLGSCVIILVATPMVAFIIPFLGLLYFF 1109
Cdd:cd18570 85 LLKLPLSFFETRKTGEIISRF---NDANkireaisSTTISLFLDLLM-----VIISGIILFFYNWKLFLITLLIIPLYIL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1110 VQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVanrwLAIRLEFVGN 1189
Cdd:cd18570 157 IILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGK----LSNLQSSIKG 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1190 CIVSFAALFA-------VLaRENLSPGIMgLSIsYALQ--LTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18570 233 LISLIGSLLIlwigsylVI-KGQLSLGQL-IAF-NALLgyFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1294-1497 |
1.13e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 45.51 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1294 INVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDI-------AKLGL-HELRSRITIIPQD-------- 1357
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsQQKGLiRQLRQHVGFVFQNfnlfphrt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 --------PVLFSGTLRmnldpfdsysDEDIWKALEFShLKTFVSGLPDKLShecseggENLSVGQRQLLCLARALLRKT 1429
Cdd:PRK11264 102 vleniiegPVIVKGEPK----------EEATARARELL-AKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1430 KVLVLDEATAAVDLETDNLIQSTIRSQFEDC-TVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIA 1497
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALFA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1291-1340 |
1.14e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.60 E-value: 1.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSltlgLFRII----EPAEGQISI-DGVDIA 1340
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKST----LLKLLagelEPDSGTVKLgETVKIG 381
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1295-1499 |
1.22e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.34 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1295 NVDISGGEKVGIVGRTGAGKSSLtLGLFR-IIEPAEGQISIDGVDiaklglHelrsRITIIPQDPV--------LFSG-T 1364
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL-LNLIAgFLTPASGSLTLNGQD------H----TTTPPSRRPVsmlfqennLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1365 LRMN----LDP---FDSYSDEDIWKALEFSHLKTFVSGLPDKLSHecseggenlsvGQRQLLCLARALLRKTKVLVLDEA 1437
Cdd:PRK10771 88 VAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQLSG-----------GQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1438 TAAVD----LETDNLIQSTIRSQfeDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLIAQK 1499
Cdd:PRK10771 157 FSALDpalrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1291-1498 |
1.26e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.35 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIA-------------KLGLHELRSRITIIPQD 1357
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 PVLFSGTLRMnldpfdsysdEDIWKA------LEFSHLKTFVSGLPDKLSHECSEGGE---NLSVGQRQLLCLARALLRK 1428
Cdd:PRK10619 101 FNLWSHMTVL----------ENVMEApiqvlgLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1429 TKVLVLDEATAAVDLEtdnLIQSTIR--SQF--EDCTVLTIAHRlntiMDYTR-----VLVLDKGQMAEFDSPSSLIAQ 1498
Cdd:PRK10619 171 PEVLLFDEPTSALDPE---LVGEVLRimQQLaeEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1290-1442 |
1.40e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.09 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSltlgLFRII----EPAEGQISIDGVDIAKLGlHELRSRITIIPQ--------- 1356
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVP-AENRHVNTVFQSyalfphmtv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1357 -DPVLFSgtLRMNLDPFDSYsDEDIWKALEFSHLKTFVSGLPdklshecseggENLSVGQRQLLCLARALLRKTKVLVLD 1435
Cdd:PRK09452 104 fENVAFG--LRMQKTPAAEI-TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
....*..
gi 1357684105 1436 EATAAVD 1442
Cdd:PRK09452 170 ESLSALD 176
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1024-1148 |
1.47e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 45.66 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1024 LASRFLHQsmlfdVLRSPMSFFERTPSGNLVNRFAkEMDTI-DSLIPMILKMFMGSLFnVLGSCVIILVATPMVAFII-- 1100
Cdd:cd18782 77 LGGTIIDH-----LLRLPLGFFDKRPVGELSTRIS-ELDTIrGFLTGTALTTLLDVLF-SVIYIAVLFSYSPLLTLVVla 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1101 --PFLGLLYFFVQRFYvasSRQLKRLESvSRSPIYTHFNETLLGTSVIRA 1148
Cdd:cd18782 150 tvPLQLLLTFLFGPIL---RRQIRRRAE-ASAKTQSYLVESLTGIQTVKA 195
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1290-1497 |
1.48e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 45.26 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHE-LRSRITIIPQDPVLFSG-TLRM 1367
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1368 NLDPFDSYSDEDiwkalEFSHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDN 1447
Cdd:PRK11614 100 NLAMGGFFAERD-----QFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1357684105 1448 LIQSTIRS-QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSPSSLIA 1497
Cdd:PRK11614 175 QIFDTIEQlREQGMTIFLVEQNANQALKLAdRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1297-1497 |
1.66e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.09 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1297 DISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIA-KLGLHELRSRITIipqDPVLFSGTLRMNLDPfdsY 1375
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTV---RDLLSSITKDFYTHP---Y 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1376 SDEDIWKALEfshlktfVSGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRS 1455
Cdd:cd03237 95 FKTEIAKPLQ-------IEQILDREVPE-------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1456 QFE--DCTVLTIAHrlNTIM-DYT--RVLVLDkGQMAEF---DSPSSLIA 1497
Cdd:cd03237 161 FAEnnEKTAFVVEH--DIIMiDYLadRLIVFE-GEPSVNgvaNPPQSLRS 207
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
662-849 |
2.30e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.10 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDK---MEGSVAVKG-SVAYVPQQAWIQNATLKNNIIFgQKRKESW--Y 735
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGrEILNLPEKELNKLRAEQISMIF-QDPMTSLnpY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 736 QRV----VEACALQQDLDILPAGDET-------EIGE--KGVNL-----SGGQKQRVSLARAVYCDRSVYLLDDPLSAVD 797
Cdd:PRK09473 114 MRVgeqlMEVLMLHKGMSKAEAFEESvrmldavKMPEarKRMKMyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 798 AHVGKHIFDqvigpqgLLKDKTR------ILVTHGLSYLPQ-ADLVLVMVDGEITEIGS 849
Cdd:PRK09473 194 VTVQAQIMT-------LLNELKRefntaiIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1037-1245 |
2.40e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 44.86 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 VLRSPMSFFERTPSGNLVNRFaKEMDTIDSLI-PMILKMFMGSLFNVLgsCVIILVA-----TPMVAFIIPFLGLLyffv 1110
Cdd:cd18568 85 LLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFI--YLGLMFYynlqlTLIVLAFIPLYVLL---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1111 qrfYVASSRQLKRLES---VSRSPIYTHFNETLLGTSVIRAFGEQERFIHESDQRVDHNQKAYYPSIVanrwLAIRLEFV 1187
Cdd:cd18568 158 ---TLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK----LSIVLQLI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357684105 1188 GNcIVSFAALFAVL-------ARENLSPG-IMGLSISYALqLTASLTWLVRMSSDVETNIVAVERV 1245
Cdd:cd18568 231 SS-LINHLGTIAVLwygaylvISGQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRISVERL 294
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
662-825 |
2.46e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 44.80 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 662 LNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS------------VAYVPQQAWIQ-NATLKNNI-IFG 727
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDpDFTVRENLlVFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 728 Q------KRKESWYQRVVEACALQQDLDilpagdeTEIGEkgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVG 801
Cdd:PRK13537 106 RyfglsaAAARALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180
....*....|....*....|....*
gi 1357684105 802 KHIFDQVigpQGLL-KDKTRILVTH 825
Cdd:PRK13537 175 HLMWERL---RSLLaRGKTILLTTH 196
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1289-1484 |
2.69e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.60 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1289 LAIRNINVDISGGEKVGIVGRTGAGKSS----LTlGLFRiiePAEGQISIDGVDIAKLGLHE--------------LRSR 1350
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTvfncLT-GFYK---PTGGTILLRGQHIEGLPGHQiarmgvvrtfqhvrLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1351 ITIIPQDPV---------LFSGTLRMnldPFDSYSDEDiwkALEFSHLKTFVSGLpdkLSHECSEGGeNLSVGQRQLLCL 1421
Cdd:PRK11300 95 MTVIENLLVaqhqqlktgLFSGLLKT---PAFRRAESE---ALDRAATWLERVGL---LEHANRQAG-NLAYGQQRRLEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1422 ARALLRKTKVLVLDEATAAVD-LETDNLIQ--STIRSQFeDCTVLTIAHRLNTIMDYT-RVLVLDKG 1484
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGISdRIYVVNQG 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1274-1356 |
2.88e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1274 IHITNFGLRYRSDLdlAIRNINVDISGGEKVGIVGRTGAGKSSLtLGLF---RIIEpaEGQISIDGVDIAKLGlH--ELR 1348
Cdd:NF033858 2 ARLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSL-LSLIagaRKIQ--QGRVEVLGGDMADAR-HrrAVC 75
|
....*...
gi 1357684105 1349 SRITIIPQ 1356
Cdd:NF033858 76 PRIAYMPQ 83
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1301-1474 |
2.95e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1301 GEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQIsidgvdiaklglhelrsritiipqdpvlfsgtLRMNLDPFDSYSDEDI 1380
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1381 WKALEFshlktfvsglpdklshecsEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQF--- 1457
Cdd:smart00382 50 LLIIVG-------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170 180
....*....|....*....|.
gi 1357684105 1458 ----EDCTVLTIAHRLNTIMD 1474
Cdd:smart00382 111 lkseKNLTVILTTNDEKDLGP 131
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
1037-1155 |
3.02e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 44.42 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1037 VLRSPMSFFERTPSGNLVNRfAKEMDTI-DSLIPMILKMFMGSLFnVLGSCVIILVATPMVAFIIPFLGLLYFFvqrFYV 1115
Cdd:cd18555 85 LLKLPYSFFENRSSGDLLFR-ANSNVYIrQILSNQVISLIIDLLL-LVIYLIYMLYYSPLLTLIVLLLGLLIVL---LLL 159
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1357684105 1116 ASSRQLKRL---ESVSRSPIYTHFNETLLGTSVIRAFGEQERF 1155
Cdd:cd18555 160 LTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSLGSEKNI 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1278-1445 |
3.12e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.79 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1278 NFGLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIaklglhelrsritIIPQD 1357
Cdd:COG2401 33 AFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-------------QFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1358 PVLfsgtlrmnLDPFdsYSDEDIWKALEFSHlktfVSGLPD------KLSHecseggenLSVGQRQLLCLARALLRKTKV 1431
Cdd:COG2401 100 ASL--------IDAI--GRKGDFKDAVELLN----AVGLSDavlwlrRFKE--------LSTGQKFRFRLALLLAERPKL 157
|
170
....*....|....
gi 1357684105 1432 LVLDEATAAVDLET 1445
Cdd:COG2401 158 LVIDEFCSHLDRQT 171
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
950-1200 |
3.50e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 44.48 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 950 AIGVLLSAISLLFflshNLLSMFanywLSLWTDDPVVNGTQP------------DRLMRLGVYGGL--GVSQGVAVFGYS 1015
Cdd:cd18565 2 VLGLLASILNRLF----DLAPPL----LIGVAIDAVFNGEASflplvpaslgpaDPRGQLWLLGGLtvAAFLLESLFQYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1016 LSVSIGGiLASRFLH--QSMLFD-VLRSPMSFFERTPSGNL-------VN---RFAkeMDTIDSLIPMilkmfmgsLFNV 1082
Cdd:cd18565 74 SGVLWRR-FAQRVQHdlRTDTYDhVQRLDMAFFEDRQTGDLmsvlnndVNqleRFL--DDGANSIIRV--------VVTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1083 LGSCVIILVATPMVAFI----IPFLGLL-YFFVQRfyvASSRQLKRLESVSRspIYTHFNETLLGTSVIRAFG----EQE 1153
Cdd:cd18565 143 LGIGAILFYLNWQLALVallpVPLIIAGtYWFQRR---IEPRYRAVREAVGD--LNARLENNLSGIAVIKAFTaedfERE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 1154 RFIHESDQRVDHNQKA------YYPSIvanrWLAIRlefvgnciVSFAALFAV 1200
Cdd:cd18565 218 RVADASEEYRDANWRAirlraaFFPVI----RLVAG--------AGFVATFVV 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1306-1469 |
3.74e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1306 IVGRTGAGKSSLTLGLFRIIEPAEG-----QISIDGVDIAKL-GLHELRSRITIIPQDPVLFSGTLRMNLdpFDSYSDED 1379
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNV--LAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1380 IWKALEF---SHLKTFVSGLPDKLSHECSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDNLIQSTIRSQ 1456
Cdd:PRK14271 130 LVPRKEFrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170
....*....|...
gi 1357684105 1457 FEDCTVLTIAHRL 1469
Cdd:PRK14271 210 ADRLTVIIVTHNL 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
767-849 |
4.21e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 767 SGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFdqvigpqGLLKdktRILVTHGLSYL-PQADL---------V 836
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL-------ALLK---SLQQKHQLAYLfISHDLhvvralchqV 496
|
90
....*....|...
gi 1357684105 837 LVMVDGEITEIGS 849
Cdd:PRK15134 497 IVLRQGEVVEQGD 509
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1290-1486 |
4.27e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRII---EPAEGQISIDG----------VDIAKLGLH--------ELR 1348
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtvqregrlaRDIRKSRANtgyifqqfNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1349 SRITIIpqDPVLFsGTL------RMNLDPFDSYSDEDIWKALefshlkTFVSglpdkLSHECSEGGENLSVGQRQLLCLA 1422
Cdd:PRK09984 99 NRLSVL--ENVLI-GALgstpfwRTCFSWFTREQKQRALQAL------TRVG-----MVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1423 RALLRKTKVLVLDEATAAVDLETDNLIQSTIR--SQFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQM 1486
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1009-1154 |
4.41e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.99 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1009 VAVFGYSLSVSiggiLASRFLHQsmlfdVLRSPMSFFERTPSGNLVNRFakemDTIDSLIPMILKMFMGSLFN---VLGS 1085
Cdd:cd18567 66 VLYLSTSLNLQ----WTSNLFRH-----LLRLPLSYFEKRHLGDIVSRF----GSLDEIQQTLTTGFVEALLDglmAILT 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1086 CVIILVATPMVAFIIPFLGLLYFFVQRFYVASSRQLKRLESVSRSPIYTHFNETLLGTSVIRAFG-EQER 1154
Cdd:cd18567 133 LVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGrEAER 202
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1486 |
4.83e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.92 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISI---DGVDIAKLGLHE-------------------- 1346
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEkvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1347 -LRSRITIIPQ--DPVLFSGTLRMNLdPFDSYS-----DEDIWKALEFSHLktfvSGLPDKLsheCSEGGENLSVGQRQL 1418
Cdd:PRK13651 102 eIRRRVGVVFQfaEYQLFEQTIEKDI-IFGPVSmgvskEEAKKRAAKYIEL----VGLDESY---LQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1419 LCLARALLRKTKVLVLDEATAAVD-------LET-DNLIQstirsqfEDCTVLTIAHRLNTIMDYT-RVLVLDKGQM 1486
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDpqgvkeiLEIfDNLNK-------QGKTIILVTHDLDNVLEWTkRTIFFKDGKI 243
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
661-844 |
6.43e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 661 RLNVrVPeGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAV-KG-SVAYVPQQawiQNATLKNNiifgqkrkESWYQ-- 736
Cdd:PRK10636 332 KLNL-VP-GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGiKLGYFAQH---QLEFLRAD--------ESPLQhl 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 737 -RVVEACALQQDLDILPA----GDE-TEIGEKgvnLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDQVIG 810
Cdd:PRK10636 399 aRLAPQELEQKLRDYLGGfgfqGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
170 180 190
....*....|....*....|....*....|....*.
gi 1357684105 811 PQGLLkdktrILVTHGLSYLPQA--DLVLVMvDGEI 844
Cdd:PRK10636 476 FEGAL-----VVVSHDRHLLRSTtdDLYLVH-DGKV 505
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
660-845 |
7.40e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 660 KRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG------SVA--------YVP---QQ---------A 713
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalSTAqrlarglvYLPedrQSsglyldaplA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 714 WIQNATLKNNIIFgqkrkesWYQRVVEACALQQ---DLDILPAGDETEIGekgvNLSGGQKQRVSLARAVYCDRSVYLLD 790
Cdd:PRK15439 360 WNVCALTHNRRGF-------WIKPARENAVLERyrrALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 791 DPLSAVDAHVGKHIFdQVIgpQGLLKDKTRIL-VTHGLSYLPQ-ADLVLVMVDGEIT 845
Cdd:PRK15439 429 EPTRGVDVSARNDIY-QLI--RSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1290-1504 |
8.40e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG----VDIAKlGLHELRSRITIIPqdpvlFSGtL 1365
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsaalIAISS-GLNGQLTGIENIE-----LKG-L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1366 RMNLDpfDSYSDEDIWKALEFSHL--------KTFVSGLPDKLshecsegGENLSVGqrqllclarallRKTKVLVLDEA 1437
Cdd:PRK13545 112 MMGLT--KEKIKEIIPEIIEFADIgkfiyqpvKTYSSGMKSRL-------GFAISVH------------INPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1438 TAAVDLE-TDNLIQSTIRSQFEDCTVLTIAHRLNTIMDY-TRVLVLDKGQMAEFDSPSSLIAQKGAFYR 1504
Cdd:PRK13545 171 LSVGDQTfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFcTKALWLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1290-1485 |
9.23e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLG-LHELRSRITIIPQDpvlfsgtlrMN 1368
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpKSSQEAGIGIIHQE---------LN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1369 LDPFDSYSdEDIWKALEFSHL-------KTFVSGlpDKL---------SHE-CSEggenLSVGQRQLLCLARALLRKTKV 1431
Cdd:PRK10762 90 LIPQLTIA-ENIFLGREFVNRfgridwkKMYAEA--DKLlarlnlrfsSDKlVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1432 LVLDEATAAV-DLETDNLIqSTIRS-QFEDCTVLTIAHRLNTIMDYT-RVLVLDKGQ 1485
Cdd:PRK10762 163 IIMDEPTDALtDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEICdDVTVFRDGQ 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
706-797 |
1.16e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 42.32 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 706 VAYVPQQAWI-QNATLKNNI-IFGQKRKESWYQRVVEACALQQDLDIlpagdeTEIGE-KGVNLSGGQKQRVSLARAVYC 782
Cdd:COG1137 80 IGYLPQEASIfRKLTVEDNIlAVLELRKLSKKEREERLEELLEEFGI------THLRKsKAYSLSGGERRRVEIARALAT 153
|
90
....*....|....*
gi 1357684105 783 DRSVYLLDDPLSAVD 797
Cdd:COG1137 154 NPKFILLDEPFAGVD 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
659-842 |
1.19e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKG----------------SVAYvPQQAWIQNATLKN 722
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlgiGIIY-QELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 723 NIIFGQ-KRKESWYQRVVEACALQQDLDI--LPAGDETEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDPLSAV-DA 798
Cdd:PRK09700 100 NLYIGRhLTKKVCGVNIIDWREMRVRAAMmlLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1357684105 799 HVGK--HIFDQvigpqgLLKDKTRIL-VTHGLSYLPQ-ADLVLVMVDG 842
Cdd:PRK09700 180 EVDYlfLIMNQ------LRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
766-846 |
1.42e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 766 LSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTRIL------VTHGLSYLPQ-ADLVLV 838
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQ-------LLRELQQELnmgllfITHNLSIVRKlADRVAV 229
|
....*...
gi 1357684105 839 MVDGEITE 846
Cdd:PRK15134 230 MQNGRCVE 237
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1290-1492 |
2.16e-03 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 42.06 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLtlgLfRII----EPAEGQISIDGVDiAKLGLHELRSRITIIPQDPVLFsgtl 1365
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL---L-RIIagleTPDSGRIVLNGRD-LFTNLPPRERRVGFVFQHYALF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1366 RmNLDPFD---------SYSDEDIwKA-----LEFSHLktfvSGLPDKLSHEcseggenLSVGQRQLLCLARALLRKTKV 1431
Cdd:COG1118 88 P-HMTVAEniafglrvrPPSKAEI-RArveelLELVQL----EGLADRYPSQ-------LSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1357684105 1432 LVLDEATAAVD------LEtDNLIQstIRSQFEdCTVLTIAHRLNTIMDYT-RVLVLDKGQMAEFDSP 1492
Cdd:COG1118 155 LLLDEPFGALDakvrkeLR-RWLRR--LHDELG-GTTVFVTHDQEEALELAdRVVVMNQGRIEQVGTP 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1290-1358 |
2.21e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.02 E-value: 2.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIePAEGQIS----IDGVDIAKLGLHEL-RSR---ITIIPQDP 1358
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatFNGREILNLPEKELnKLRaeqISMIFQDP 106
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
657-792 |
2.23e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 657 PTLKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSV--AVKGSVAYVPQ---QAWIQNATLKNNIifGQKRK 731
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQdhaYDFENDLTLFDWM--SQWRQ 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357684105 732 ESWYQRVVEAcALQQdldILPAGDetEIGEKGVNLSGGQKQRVSLARAVYCDRSVYLLDDP 792
Cdd:PRK15064 411 EGDDEQAVRG-TLGR---LLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1290-1357 |
2.70e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.93 E-value: 2.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357684105 1290 AIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDGVDIAKLGLHE-LRSRITIIPQD 1357
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPED 335
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
672-692 |
2.99e-03 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 40.29 E-value: 2.99e-03
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1280-1348 |
3.10e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.06 E-value: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357684105 1280 GLRYRSDLDLAIRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDG-----VDIAKLGLHELR 1348
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERR 84
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1291-1485 |
3.15e-03 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.20 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1291 IRNINVDISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQIsidgvdIAKLG-LHELRSRITIIPQDPVLFsgtlrmnl 1369
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTApLAEAREDTRLMFQDARLL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1370 dPFDSYSD------EDIWKALEFSHLKTFvsGLPDKlsheCSEGGENLSVGQRQLLCLARALLRKTKVLVLDEATAAVD- 1442
Cdd:PRK11247 94 -PWKKVIDnvglglKGQWRDAALQALAAV--GLADR----ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1443 ---LETDNLIQSTIRSQ-FedcTVLTIAHRLN---TIMDytRVLVLDKGQ 1485
Cdd:PRK11247 167 ltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGK 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
667-825 |
3.15e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 667 PEGSLVAVVGHVGSGKSSLLSAL---LGemdkMEGSVAVKGSVAYVPQQAWIQNATLknNIIFGQkrkeswyqrvveaca 743
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIglaLG----GAQSATRRRSGVKAGCIVAAVSAEL--IFTRLQ--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 744 lqqdldilpagdeteigekgvnLSGGQKQRVSLARAV----YCDRSVYLLDDPLSAVDAHVGKHIFDqVIGPQgLLKDKT 819
Cdd:cd03227 78 ----------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE-AILEH-LVKGAQ 133
|
....*.
gi 1357684105 820 RILVTH 825
Cdd:cd03227 134 VIVITH 139
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
659-797 |
3.66e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGS--------------VAYVPQqawiqnaTL-KN- 722
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ-------GLgKNl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 723 --------NI-----IFGQKRKESwYQRVVE---ACALQQDLDiLPAGdeteigekgvNLSGGQKQRVSLARAVYCDRSV 786
Cdd:NF033858 90 yptlsvfeNLdffgrLFGQDAAER-RRRIDEllrATGLAPFAD-RPAG----------KLSGGMKQKLGLCCALIHDPDL 157
|
170
....*....|.
gi 1357684105 787 YLLDDPLSAVD 797
Cdd:NF033858 158 LILDEPTTGVD 168
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
671-692 |
3.90e-03 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 39.84 E-value: 3.90e-03
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
767-848 |
4.05e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 767 SGGQKQRVSLARAVYCDRSVYLLDDPLSAVDAHVGKHIFDqvigpqgLLKDKTR------ILVTHGLSYLPQ-ADLVLVM 839
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN-------LLLDLQRdfgiayLFISHDMAVVERiSHRVAVM 537
|
....*....
gi 1357684105 840 VDGEITEIG 848
Cdd:PRK10261 538 YLGQIVEIG 546
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
672-703 |
4.27e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 39.96 E-value: 4.27e-03
10 20 30
....*....|....*....|....*....|....*
gi 1357684105 672 VAVVGHVGSGKSSLLSALLGEM---DKMEGSVAVK 703
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIfslEKYLSTNGVT 40
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
659-690 |
5.35e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 5.35e-03
10 20 30
....*....|....*....|....*....|..
gi 1357684105 659 LKRLNVRVPEGSLVAVVGHVGSGKSSLLSALL 690
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTL 42
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1298-1482 |
5.50e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1298 ISGGEKVGIVGRTGAGKSSLTLGLFRIIEPAEGQISIDgVDIA-KlglhelrsritiiPQ----DpvlFSGT----LRMN 1368
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISyK-------------PQyikpD---YDGTvedlLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 1369 LDPFD-SYSDEDIWKALefshlktfvsGLPDKLSHECSEggenLSVGQRQLLCLARALLRKTKVLVLDEATAAVDLETDN 1447
Cdd:PRK13409 425 TDDLGsSYYKSEIIKPL----------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1357684105 1448 LIQSTIRSQFE--DCTVLTIAHRLnTIMDY--TRVLVLD 1482
Cdd:PRK13409 491 AVAKAIRRIAEerEATALVVDHDI-YMIDYisDRLMVFE 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
765-856 |
6.20e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 765 NLSGGQKQRVSLARAVYCDRSVYLLDDPLSAVDahVGKHI-FDQVIgpQGLLKDKTRILVTHGLS---YLpqADLVLVM- 839
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLnVARLI--RELAEGKYVLVVEHDLAvldYL--ADNVHIAy 285
|
90 100 110
....*....|....*....|....*....|
gi 1357684105 840 ----VDGEITE-------IGSYLQ--LKEE 856
Cdd:PRK13409 286 gepgAYGVVSKpkgvrvgINEYLKgyLPEE 315
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
333-616 |
7.38e-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: 40.09 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 333 FIQDILMFAGPEILRLLIKFVNDPDAPPWQGYFYTALLFVCTCVQSLI--LQRYFhvCFVSGMRLRTAVIGAVYRKALVI 410
Cdd:cd18541 9 ILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFrfLWRYL--IFGASRRIEYDLRNDLFAHLLTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 411 SSAARRTSTVGEIVNLMSVDAQRFMDLVTY-INMIWSAPLQVVLALYFLWeNLGPSV-LAGVAVMILMVPVNAVIAMK-T 487
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPgILYLVDALFLGVLVLVMMF-TISPKLtLIALLPLPLLALLVYRLGKKiH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 488 KTYQVAQmknkdSRIKLMN----EMLNGIKVLKLYAWEMAFRDKVSqiRENElQVLKKAAYLGAVSTFTWVCAPFLVALS 563
Cdd:cd18541 166 KRFRKVQ-----EAFSDLSdrvqESFSGIRVIKAFVQEEAEIERFD--KLNE-EYVEKNLRLARVDALFFPLIGLLIGLS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357684105 564 TFSV------YVLSNDQNVLDaqkaFVS-LALFNILRFPLNMLPMVISSMVQASVSLKRL 616
Cdd:cd18541 238 FLIVlwyggrLVIRGTITLGD----LVAfNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
664-716 |
9.59e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.64 E-value: 9.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1357684105 664 VRVPEGSLVAVVGHVGSGKSSLLSALLGEMDKMEGSVAVKGSVAYVPQQAWIQ 716
Cdd:pfam13191 19 VRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLE 71
|
|
| |
