|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
177-1451 |
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: 1065.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 177 PEEKSSFLSKIFFCWLNPLIRAGAKQPLTNESLHNLNENATSEW----LYTRWRAEFDK-----------EKAGRKSGET 241
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMvvpvLVENWKKECKKtrkqpvsavygKKDPSKPKGS 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 242 SIV-----------------W--PFIRIQRATI----ITLTLARLTADIVHYLNPILLKQLIDYVSLHDQPLSFGIAIAC 298
Cdd:TIGR00957 283 SQLdaneevealivksphkpRkpSLFKVLYKTFgpyfLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 299 IMFSCSTTRSL-LQNYQ----IAGMcrqavYYQTVLSNAILHKILRLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQN 373
Cdd:TIGR00957 363 LLFVCACLQTLiLHQYFhicfVSGM-----RIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINM 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 374 MWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEES 453
Cdd:TIGR00957 438 IWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 454 FEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTCYVLWSPDeNGLTPSVAFVALTIFNQLRQPMRMVANL 533
Cdd:TIGR00957 518 FLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDEN-NILDAEKAFVSLALFNILRFPLNILPMV 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 534 INTLVQARVSNKRLRQFLNDEEM-----ERKT-EVALGNAIVFKNASLNWkGPQNPPVLKDLSATIKPGQLIAIVGSVGG 607
Cdd:TIGR00957 597 ISSIVQASVSLKRLRIFLSHEELepdsiERRTiKPGEGNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGC 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 608 GKSSLLSAVLDEMVLLDGRVKVGGSIAYVPQHSWIFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVG 687
Cdd:TIGR00957 676 GKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIG 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 688 ENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPDGLLRSKTRVLVTHNLQYTKYVDTIYVIE 767
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMS 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 768 DGQIVQHGSFEDIAYVDGPFGRLWSECENSDEDVADEE----AESSEASVTPPVpvlENG----DNGAIEKSSQIDRTNS 839
Cdd:TIGR00957 836 GGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDswtaLVSGEGKEAKLI---ENGmlvtDVVGKQLQRQLSASSS 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 840 HFSEKSRK--SEEKPQKVEKNVEN--------VQLGRVKKSVYQLYIKTMGIFNSSAFLIFFIAHFTVMIMRSLWLSDWS 909
Cdd:TIGR00957 913 DSGDQSRHhgSSAELQKAEAKEETwklmeadkAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWT 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 910 NENAAikkatlssvdylNSTSSvdgpvSVETRLIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISF 989
Cdd:TIGR00957 993 DDPMV------------NGTQN-----NTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSF 1055
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 990 FDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNACMILVLISISTPIFLVCAAPLILIYYFVMIYYIPTSRQLKRL 1068
Cdd:TIGR00957 1056 FERTPSGNLVNRFSKELDTVDSmIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRL 1135
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1069 ESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNRWLATRLELLGNTCVLFASLSATLSTK 1148
Cdd:TIGR00957 1136 ESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRH 1215
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1149 yfGLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEYQKLEPEAPWRIEKSlENEEKWPVKGKIELDGFSM 1228
Cdd:TIGR00957 1216 --SLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQET-APPSGWPPRGRVEFRNYCL 1292
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1229 RYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVF 1308
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLF 1372
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1309 SGTLRFNLDPFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASV 1388
Cdd:TIGR00957 1373 SGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1389 DTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNPDSLYS 1451
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
177-1453 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 803.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 177 PEEKSSFLSKIFFCWLNPLIRAGAKQPLTNESLHNLNENATSEWLYTRWRAEFDKEKAGRKSgetsivwpfiRIQRATII 256
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKP----------WLLRALNN 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 257 TL-------TLARLTADIVHYLNPILLKQLIDYVSLHDqPLSFGIAIACIMFSCSttrsllqnyqIAGMCRQAVYYQTV- 328
Cdd:PLN03130 298 SLggrfwlgGFFKIGNDLSQFVGPLLLNLLLESMQNGE-PAWIGYIYAFSIFVGV----------VLGVLCEAQYFQNVm 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 329 ---------LSNAILHKILRLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAG 399
Cdd:PLN03130 367 rvgfrlrstLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 400 VCIMILFIPLN-LCTSRFIKLSQQKqMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRI 478
Cdd:PLN03130 447 SLMLVLMFPIQtFIISKMQKLTKEG-LQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAF 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 479 VDVANAASPFLVAIGSFTCYVLWSPDengLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRLRQFLNDEEmer 558
Cdd:PLN03130 526 NSFILNSIPVLVTVVSFGVFTLLGGD---LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEE--- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 559 ktEVALGN--------AIVFKNASLNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEM-VLLDGRVKV 629
Cdd:PLN03130 600 --RVLLPNpplepglpAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVI 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 630 GGSIAYVPQHSWIFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQ 709
Cdd:PLN03130 678 RGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYS 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 710 DKDIYLLDDPLSAVDAHVGRALFDKVIgpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYvDGPFGR 789
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NGPLFQ 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 790 LWSECENSDEDVADEEAESsEASVTPPVPVlENGDNGAIEKSSqidrtnshfSEKSRKSEEKPQKVEKnvENVQLGRVKK 869
Cdd:PLN03130 835 KLMENAGKMEEYVEENGEE-EDDQTSSKPV-ANGNANNLKKDS---------SSKKKSKEGKSVLIKQ--EERETGVVSW 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 870 SVYQLYIKTMG-IFNSSAFLIFFIAHFTVMIMRSLWLSDWSNEnaaikkatlssvdylnSTSSVDGPVSVetrLIVYAGF 948
Cdd:PLN03130 902 KVLERYKNALGgAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQ----------------GTPKTHGPLFY---NLIYALL 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 949 G-GLEMLLLALAFTvLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKlqdNIRMCTQTLLNAC 1027
Cdd:PLN03130 963 SfGQVLVTLLNSYW-LIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDR---NVAVFVNMFLGQI 1038
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1028 MIL----VLISISTPIFLVCAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTT--- 1100
Cdd:PLN03130 1039 FQLlstfVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAein 1118
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1101 -TALSTNVdkfaqcRY-LSHMS-NRWLATRLELLGNTCVLFASLSATL----STKYFGLTPGMaGLSVSYALTITEVLNI 1173
Cdd:PLN03130 1119 gRSMDNNI------RFtLVNMSsNRWLAIRLETLGGLMIWLTASFAVMqngrAENQAAFASTM-GLLLSYALNITSLLTA 1191
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1174 CVRSVSEIESNIVSVERVNEYQKLEPEAPWRIEkSLENEEKWPVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGV 1253
Cdd:PLN03130 1192 VLRLASLAENSLNAVERVGTYIDLPSEAPLVIE-NNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGI 1270
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1254 IGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQIWNCLEI 1333
Cdd:PLN03130 1271 VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLER 1350
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1334 CQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIA 1413
Cdd:PLN03130 1351 AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA 1430
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|
gi 392896924 1414 HRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNPDSLYSQL 1453
Cdd:PLN03130 1431 HRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
177-1455 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 750.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 177 PEEKSSFLSKIFFCWLNPLIRAGAKQPLTNESLHNLNENATSEWLYTRWRAEFDKEKAGRKSgetsivWPFIRIQRATII 256
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKP------WLLRALNNSLGG 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 257 TLTLA---RLTADIVHYLNPILLKQLIDYVSLHDqPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAI 333
Cdd:PLN03232 302 RFWLGgifKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 334 LHKILRLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLN-LC 412
Cdd:PLN03232 381 FHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQtLI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 413 TSRFIKLSQQKqMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAI 492
Cdd:PLN03232 461 VRKMRKLTKEG-LQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 493 GSFTCYVLWSPDengLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRLRQFLNDEE--MERKTEVALGN-AIV 569
Cdd:PLN03232 540 VSFGVFVLLGGD---LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEEriLAQNPPLQPGApAIS 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 570 FKNASLNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLL-DGRVKVGGSIAYVPQHSWIFNKTIK 648
Cdd:PLN03232 617 IKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIFNATVR 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVG 728
Cdd:PLN03232 697 ENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 729 RALFDKVIGPDglLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLWSECENSDEDVADEEAES 808
Cdd:PLN03232 777 HQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDE 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 809 SEASVTPPVPV-LENGDNGAIEKSsqidrtnshfseKSRKSEEKPQkveknvENVQLGRVKKSVYQLYIKTMG-IFNSSA 886
Cdd:PLN03232 855 NILKLGPTVTIdVSERNLGSTKQG------------KRGRSVLVKQ------EERETGIISWNVLMRYNKAVGgLWVVMI 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 887 FLIFFIAHFTVMIMRSLWLSDWSNEnaaikkatlssvdylnSTSSVDGPvsvETRLIVYA--GFGGLeMLLLALAFTVLT 964
Cdd:PLN03232 917 LLVCYLTTEVLRVSSSTWLSIWTDQ----------------STPKSYSP---GFYIVVYAllGFGQV-AVTFTNSFWLIS 976
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 965 iGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNACMILVLISISTPIFLVC 1043
Cdd:PLN03232 977 -SSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRnVANLMNMFMNQLWQLLSTFALIGTVSTISLWA 1055
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1044 AAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNRW 1123
Cdd:PLN03232 1056 IMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRW 1135
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1124 LATRLELLGNTCVLfasLSATLSTKYFGLTPGMA------GLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEYQKL 1197
Cdd:PLN03232 1136 LTIRLETLGGVMIW---LTATFAVLRNGNAENQAgfastmGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDL 1212
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1198 EPEAPwRIEKSLENEEKWPVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESG 1277
Cdd:PLN03232 1213 PSEAT-AIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG 1291
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1278 TIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKN 1357
Cdd:PLN03232 1292 RIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGEN 1371
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1358 MSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFD 1437
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
1290
....*....|....*...
gi 392896924 1438 TPSNLLLNPDSLYSQLLN 1455
Cdd:PLN03232 1452 SPQELLSRDTSAFFRMVH 1469
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
262-1455 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 661.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 262 RLTADIVHYLNPILLKQLIDYVSLHDQPLSFGIAIACIMFSCSTTRSL-LQNYQIAGMcRQAVYYQTVLSNAILHKILRL 340
Cdd:PTZ00243 253 KLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVcLHRFYYISI-RCGLQYRSALNALIFEKCFTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 341 SPS--ARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFIK 418
Cdd:PTZ00243 332 SSKslAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQM 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 419 LSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTCY 498
Cdd:PTZ00243 412 AARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVY 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 499 VLWSpdeNGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRLRQFLNDEEMERKT--------------EVAL 564
Cdd:PTZ00243 492 YLLG---HELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATCSTvqdmeeywreqrehSTAC 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 565 GNAIVFKNASLNW----KGPQNPPV------------------------------------------------------- 585
Cdd:PTZ00243 569 QLAAVLENVDVTAfvpvKLPRAPKVktsllsralrmlcceqcrptkrhpspsvvvedtdygspssasrhiveggtggghe 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 ---------------------------LKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGSIAYVPQ 638
Cdd:PTZ00243 649 atptsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQ 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 639 HSWIFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDD 718
Cdd:PTZ00243 729 QAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 719 PLSAVDAHVGRALFDKVIgpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLWSECENSD 798
Cdd:PTZ00243 809 PLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKENKD 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 799 EDVADEEAESSEASVTPPVPVlengdngAIEKSSQIDRTNSHFSEKSRKSEEKPQKVekNVENVQLGRVKKSVYQLYIKT 878
Cdd:PTZ00243 887 SKEGDADAEVAEVDAAPGGAV-------DHEPPVAKQEGNAEGGDGAALDAAAGRLM--TREEKASGSVPWSTYVAYLRF 957
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 879 MGIFNSSAFLIF-FIAHFTVMIMRSLWLSDWSNENAAIKKATLSSVdYLnstssvdgpvsvetrLIVYAGFGGLEmLLLA 957
Cdd:PTZ00243 958 CGGLHAAGFVLAtFAVTELVTVSSGVWLSMWSTRSFKLSAATYLYV-YL---------------GIVLLGTFSVP-LRFF 1020
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 958 LAFTVLTIGSLRasygLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNACMILVLISIS 1036
Cdd:PTZ00243 1021 LSYEAMRRGSRN----MHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNtLPMSYLYLLQCLFSICSSILVTSAS 1096
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1037 TPIFLVCAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYL 1116
Cdd:PTZ00243 1097 QPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYL 1176
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1117 SHMSNRWLATRLELLGNTCVLFASLsATLSTKYFGLTP---GMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNE 1193
Cdd:PTZ00243 1177 ENVANRWLGVRVEFLSNIVVTVIAL-IGVIGTMLRATSqeiGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLY 1255
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1194 Y-----QKLEPEAPWRIEKsLENEEKWP----------------------VKGKIELDGFSMRYRKNLPLVLKNIDLKIE 1246
Cdd:PTZ00243 1256 YtdevpHEDMPELDEEVDA-LERRTGMAadvtgtvviepasptsaaphpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIA 1334
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1247 GGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQ 1326
Cdd:PTZ00243 1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAE 1414
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1327 IWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLL-CLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFP 1405
Cdd:PTZ00243 1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMcMARALLKKGSGFILMDEATANIDPALDRQIQATVMSAFS 1494
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|
gi 392896924 1406 QSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNPDSLYSQLLN 1455
Cdd:PTZ00243 1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVE 1544
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
173-1459 |
1.63e-153 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 504.83 E-value: 1.63e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 173 IEQTPEEKSSFLSKIFFCWLNPLIRAGAKQPLTNESLHNLNENATSEWLYTRWRAEFDKEKAGRKSGETSI-------VW 245
Cdd:TIGR01271 1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKLLnalrrcfFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 246 PFIRIQratiITLTLARLTADIvhylNPILLKQLI-DYVSLHDQPLSFGIAIA---CIMFscsTTRSLLQNYQIAGMCRQ 321
Cdd:TIGR01271 81 RFVFYG----ILLYFGEATKAV----QPLLLGRIIaSYDPFNAPEREIAYYLAlglCLLF---IVRTLLLHPAIFGLHHL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 322 AVYYQTVLSNAILHKILRLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVC 401
Cdd:TIGR01271 150 GMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 402 IMILFIPLNLCTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDV 481
Cdd:TIGR01271 230 FLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 482 ANAASPFLVAIGSFTCYVLwspdENGLTPSVAFVALTIFNQLRQPM-RMVANLINTLVQARVSNKRLRQFLNDEEME--- 557
Cdd:TIGR01271 310 AFFFSGFFVVFLSVVPYAL----IKGIILRRIFTTISYCIVLRMTVtRQFPGAIQTWYDSLGAITKIQDFLCKEEYKtle 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 558 ---RKTEVALGNAI---------VFKNASLNWKGPQNP----------------PVLKDLSATIKPGQLIAIVGSVGGGK 609
Cdd:TIGR01271 386 ynlTTTEVEMVNVTaswdegigeLFEKIKQNNKARKQPngddglffsnfslyvtPVLKNISFKLEKGQLLAVAGSTGSGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 610 SSLLSAVLDEMVLLDGRVKVGGSIAYVPQHSWIFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGEN 689
Cdd:TIGR01271 466 SSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 690 GITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPdgLLRSKTRVLVTHNLQYTKYVDTIYVIEDG 769
Cdd:TIGR01271 546 GITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 770 QIVQHGSFEDI---------------AY----------------------VDGPFGRlWSECE----------------- 795
Cdd:TIGR01271 624 VCYFYGTFSELqakrpdfsslllgleAFdnfsaerrnsiltetlrrvsidGDSTVFS-GPETIkqsfkqpppefaekrkq 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 796 -------------------------NSDEDVADE----------EAESSEASVtPPVPVLENG----------------- 823
Cdd:TIGR01271 703 siilnpiasarkfsfvqmgpqkaqaTTIEDAVREpserkfslvpEDEQGEESL-PRGNQYHHGlqhqaqrrqsvlqlmth 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 824 ----------DNGAIEKSSQIDRTNSHFSE----KSRKSEEKPQKVEKNVENVQLGRV---------KKSVYQLYIKTMG 880
Cdd:TIGR01271 782 snrgenrreqLQTSFRKKSSITQQNELASEldiySRRLSKDSVYEISEEINEEDLKECfaderenvfETTTWNTYLRYIT 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 881 IFNSSAF-LIFFIAHFTVMIMRS---LWL-SDWSNENAAIKKATLSSVDYLNSTSSVDGPVSVETRLIVYAGfggLEMLL 955
Cdd:TIGR01271 862 TNRNLVFvLIFCLVIFLAEVAASllgLWLiTDNPSAPNYVDQQHANASSPDVQKPVIITPTSAYYIFYIYVG---TADSV 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 956 LALAF--------TVLTIgslraSYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNA 1026
Cdd:TIGR01271 939 LALGFfrglplvhTLLTV-----SKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDmLPLTLFDFIQLTLIV 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1027 CMILVLISISTPIFLVCAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTT----A 1102
Cdd:TIGR01271 1014 LGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETlfhkA 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1103 LSTNVDKFAQcrYLSHMsnRWLATRLELLgntCVLFASLSATLSTKYFGLTPGMAGLSVSYALTITEVLNICVRSVSEIE 1182
Cdd:TIGR01271 1094 LNLHTANWFL--YLSTL--RWFQMRIDII---FVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVD 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1183 SNIVSVERVNEYQKLEPEAPwRIEKS-----------LEN---EEKWPVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGG 1248
Cdd:TIGR01271 1167 GLMRSVSRVFKFIDLPQEEP-RPSGGggkyqlstvlvIENphaQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGG 1245
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1249 ERIGVIGRTGSGKSSLTMALYRMIEGEsGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQIW 1328
Cdd:TIGR01271 1246 QRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIW 1324
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1329 NCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQST 1408
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT 1404
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1409 TISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQLLNEKNR 1459
Cdd:TIGR01271 1405 VILSEHRVEALLECQQFLVIEGSSVKQYDSIQK-LLNETSLFKQAMSAADR 1454
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
884-1195 |
1.66e-129 |
|
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: 402.63 E-value: 1.66e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 884 SSAFLIFFIAHFTVMIMRSLWLSDWSNENAAIKKATLSSVDYlnstssvdgpvsvetRLIVYAGFGGLEMLLLALAFTVL 963
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRDY---------------RLGVYGALGLGQAIFVFLGSLAL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 964 TIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNACMILVLISISTPIFLV 1042
Cdd:cd18603 66 ALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNtLPQNIRSFLNCLFQVISTLVVISISTPIFLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1043 CAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNR 1122
Cdd:cd18603 146 VIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1123 WLATRLELLGNTCVLFASLSATLSTKYfgLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEYQ 1195
Cdd:cd18603 226 WLAVRLEFLGNLIVLFAALFAVLSRDS--LSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
259-547 |
6.39e-117 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 368.34 E-value: 6.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 259 TLARLTADIVHYLNPILLKQLIDYVSLHDQPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAILHKIL 338
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 339 RLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFIK 418
Cdd:cd18595 83 RLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 419 LSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTCY 498
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 392896924 499 VLWSPDeNGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18595 243 VLSDPD-NVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1219-1439 |
1.73e-109 |
|
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: 345.25 E-value: 1.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFNLDPFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARI 1378
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1379 VILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTP 1439
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
568-770 |
2.28e-101 |
|
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: 322.11 E-value: 2.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQN--PPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGSIAYVPQHSWIFNK 645
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 TIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392896924 726 HVGRALFDKVIGPDgLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQ 770
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
260-547 |
1.07e-90 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 295.93 E-value: 1.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 260 LARLTADIVHYLNPILLKQLIDYV-SLHDQPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAILHKIL 338
Cdd:cd18579 4 LLKLLEDLLSLAQPLLLGLLISYLsSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 339 RLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFIK 418
Cdd:cd18579 84 RLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 419 LSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTCY 498
Cdd:cd18579 164 KLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFATY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 392896924 499 VLWSpdeNGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18579 244 VLLG---NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
886-1194 |
4.23e-88 |
|
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: 288.63 E-value: 4.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 886 AFLIFFIAHFTVMIMRSLWLSDWSNENAAikkatlssvdylnstssvDGPVSVETRLIVYAGFGGLEMLLLALAFTVLTI 965
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWLDWWSSDWSS------------------SPNSSSGYYLGVYAALLVLASVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 966 -GSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVID-KLQDNIRMCTQTLLNACMILVLISISTPIFLVC 1043
Cdd:cd18580 65 lAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDeELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1044 AAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNRW 1123
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1124 LATRLELLGNTCVLFASLSATLSTKYfgLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEY 1194
Cdd:cd18580 225 LGLRLDLLGALLALVVALLAVLLRSS--ISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
942-1455 |
2.44e-87 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 297.08 E-value: 2.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCT 1020
Cdd:COG1132 64 LLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1021 QTLLNACMILV-LISISTPIFLVCAAPLILIYyFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERT 1099
Cdd:COG1132 144 RSVVTLIGALVvLFVIDWRLALIVLLVLPLLL-LVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1100 TTALSTNVDKFAQCRYLSHMSNRWLATRLELLGNTCVLFASLSATLSTKYFGLTPGMAGLSVSYALTITEVLNICVRSVS 1179
Cdd:COG1132 223 LERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1180 EIESNIVSVERVNEYQKLEPEAPwriEKSLENEEKwPVKGKIELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGS 1259
Cdd:COG1132 303 QLQRALASAERIFELLDEPPEIP---DPPGAVPLP-PVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGS 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1260 GKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNL---DPfnQYSDDQIWNCLEICQL 1336
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1337 KQFAQEDDKTLDRYIAEGGKNMSVGERQllclcrallrgaR------------IVILDEATASVDTVTDGIVQRAIRQHF 1404
Cdd:COG1132 456 HEFIEALPDGYDTVVGERGVNLSGGQRQ------------RiaiarallkdppILILDEATSALDTETEALIQEALERLM 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1405 PQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNpDSLYSQLLN 1455
Cdd:COG1132 524 KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYR 573
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
244-791 |
6.99e-85 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 289.76 E-value: 6.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 244 VWPFIRIQRATIITLTLARLTADIVHYLNPILLKQLIDYVsLHDQPLSFGIAIACIMFSCSTTRSLL---QNYQIAGMCR 320
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL-LAGGDLSALLLLLLLLLGLALLRALLsylQRYLLARLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 321 QAVYYqtvLSNAILHKILRLSPSARSNRTAGEILNHAAVDIEIIVHSV-PYLQNMWSVPFQVTLAMTMLAIT---LGWAA 396
Cdd:COG1132 91 RVVAD---LRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLFVIdwrLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 397 MAGVCIMILFIPLNlctSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEES----FEDQINRLRAKEVKMLRNV 472
Cdd:COG1132 168 LLVLPLLLLVLRLF---GRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 473 CILSRIVDVANAASPFLVAIgsftcYVLWSPDENGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRLRQFLN 552
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLL-----VGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 553 --DEEMERKTEVALGN---AIVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSavldemvLL---- 623
Cdd:COG1132 320 epPEIPDPPGAVPLPPvrgEIEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVN-------LLlrfy 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 624 ---DGRVKVGG-------------SIAYVPQHSWIFNKTIKENILFGNElsNYFYDQVVGSC---QLKTDFRHFQQGENT 684
Cdd:COG1132 391 dptSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRP--DATDEEVEEAAkaaQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 685 MVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIY 764
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRIL 545
|
570 580
....*....|....*....|....*..
gi 392896924 765 VIEDGQIVQHGSFEDIAYVDGPFGRLW 791
Cdd:COG1132 546 VLDDGRIVEQGTHEELLARGGLYARLY 572
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1215-1439 |
1.01e-84 |
|
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: 275.45 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1215 WPVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQL 1294
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1295 RSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQIWNCLEicqlkqfaqeddktldryIAEGGKNMSVGERQLLCLCRALLR 1374
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1375 GARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTP 1439
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
886-1194 |
2.15e-81 |
|
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: 269.72 E-value: 2.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 886 AFLIFFIAHFTVMIMRSLWLSDWSNenaaikkatlssvDYLNSTSSVDGPVSVETRLIVYAGFGGLEMLLLALAFTVLTI 965
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWAS-------------AYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 966 GSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVID-KLQDNIRMCTQTLLNACMILVLISISTPIFLVCA 1044
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDsELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1045 APLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNRWL 1124
Cdd:cd18604 150 VVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1125 ATRLELLGNTCVLFASLSATLSTkyfGLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEY 1194
Cdd:cd18604 230 SVRIDLLGALFSFATAALLVYGP---GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
887-1194 |
2.70e-79 |
|
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: 263.57 E-value: 2.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 887 FLIFFIAHFTV-MIMRSLWLSDWSNenaaiKKATLSSVDYLnstssvdgpvsvetrlIVYAGFGGLEMLLLALAFTVLTI 965
Cdd:cd18606 3 LLLLLLILSQFaQVFTNLWLSFWTE-----DFFGLSQGFYI----------------GIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 966 GSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVID-KLQDNIRMCTQTLLNACMILVLISISTPIFLVCA 1044
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDnELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1045 APLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNRWL 1124
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1125 ATRLELLGNTCVLFASLSATLSTkyFGLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEY 1194
Cdd:cd18606 222 AIRLDLLGSLLVLIVALLCVTRR--FSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
942-1458 |
2.43e-74 |
|
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: 263.23 E-value: 2.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLsRDLDVIDK-LQDNIrmcT 1020
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREfLTGSL---L 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1021 QTLLNACMIL----VLISISTPIFLVCAApLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKT 1096
Cdd:COG2274 275 TALLDLLFVLifliVLFFYSPPLALVVLL-LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1097 ERTTTALSTNVDKFAQCRY-LSHMSNR--WLATRLELLGNTCVLFASLSATLSTKyfgLTPGMAGLSVSYALTITE-VLN 1172
Cdd:COG2274 354 SRFRRRWENLLAKYLNARFkLRRLSNLlsTLSGLLQQLATVALLWLGAYLVIDGQ---LTLGQLIAFNILSGRFLApVAQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1173 IcVRSVSEIESNIVSVERVNEYQKLEPEAPWRIEKSLENEekwpVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIG 1252
Cdd:COG2274 431 L-IGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR----LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1253 VIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNL---DPfnQYSDDQIWN 1329
Cdd:COG2274 506 IVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1330 CLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLcrallrgAR-------IVILDEATASVDTVTDGIVQRAIRQ 1402
Cdd:COG2274 584 AARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAI-------ARallrnprILILDEATSALDAETEAIILENLRR 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 1403 HFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQLLNEKN 1458
Cdd:COG2274 657 LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEE-LLARKGLYAELVQQQL 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
208-793 |
2.91e-73 |
|
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: 260.15 E-value: 2.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 208 SLHNLNENATSEWLYTRWRAEFDKEKagRKSGETSIVWPFIRIQRATIITLTLARLTADIVHYLNPILLKQLIDYVSLHD 287
Cdd:COG2274 113 SLEEFAESWTGVALLLEPTPEFDKRG--EKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 288 Q-----PLSFGIAIAcIMFSCSTTrsLLQNYQIAGMCRQAvyyQTVLSNAILHKILRLSPSARSNRTAGEILNHAAvDIE 362
Cdd:COG2274 191 DlstlwVLAIGLLLA-LLFEGLLR--LLRSYLLLRLGQRI---DLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 363 IIVHSV--PYLQNMWSVPFQVT--LAMTMLAITLGWAAMAGVCIMILFIplnLCTSRFIKLSQQKQMKIKDERTKLSNEM 438
Cdd:COG2274 264 SIREFLtgSLLTALLDLLFVLIflIVLFFYSPPLALVVLLLIPLYVLLG---LLFQPRLRRLSREESEASAKRQSLLVET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 439 LNGIKVVKLYAWEESFEDQINRLRAKEVK-MLRnvciLSRIVDVANAASPFLVAIGSFTCYVL--WSPDENGLTPS--VA 513
Cdd:COG2274 341 LRGIETIKALGAESRFRRRWENLLAKYLNaRFK----LRRLSNLLSTLSGLLQQLATVALLWLgaYLVIDGQLTLGqlIA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 514 FVALtiFNQLRQPMRMVANLINTLVQARVSNKRLRQFLN--DEEMERKTEVALGN---AIVFKNASLNWkGPQNPPVLKD 588
Cdd:COG2274 417 FNIL--SGRFLAPVAQLIGLLQRFQDAKIALERLDDILDlpPEREEGRSKLSLPRlkgDIELENVSFRY-PGDSPPVLDN 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 589 LSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAYVPQHSWIFNKTIKENILFGN 655
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGD 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 656 ELSNYfyDQVVGSCQLK--TDF-RHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALF 732
Cdd:COG2274 574 PDATD--EEIIEAARLAglHDFiEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 733 DKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLWSE 793
Cdd:COG2274 652 ENL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
887-1194 |
8.03e-72 |
|
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: 242.89 E-value: 8.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 887 FLIFFIAHFTVMIMRSLWLSDWSNENAAikkatlSSVDYLNSTSSVDGPVSVETRLIVYAGFGGLEMLLLALAFTVLTIG 966
Cdd:cd18602 4 VLALALLKQGLRVATDFWLADWTEANHD------VASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 967 SLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVID-KLQDNIRMCTQTLLNACMILVLISISTPIFLVCAA 1045
Cdd:cd18602 78 GLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDqKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1046 PLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNRWLA 1125
Cdd:cd18602 158 PIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 1126 TRLELLGNTCVLFASLSATLSTKYFGLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEY 1194
Cdd:cd18602 238 IRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
880-1194 |
7.09e-69 |
|
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: 234.38 E-value: 7.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 880 GIFNSSAFLIFFIAHFTVMIMRSLWLSDWSNENAAiKKATLSSVDYLNSTSSVDGPvSVETRLIVYAGFGGLEMLLLALA 959
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSG-NTTNNVDNSTVDSGNISDNP-DLNFYQLVYGGSILVILLLSLIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 960 FTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVID-KLQDNIRMCTQTLLNACMILVLISISTP 1038
Cdd:cd18599 79 GFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDvRLPFTLENFLQNVLLVVFSLIIIAIVFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1039 IFLVCAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSH 1118
Cdd:cd18599 159 WFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 1119 MSNRWLATRLELLGNTCVLFASLSATLSTKYfgLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEY 1194
Cdd:cd18599 239 CAMRWLAVRLDILAVLITLITALLVVLLKGS--ISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1219-1454 |
1.05e-66 |
|
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: 226.33 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFNLDPFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARI 1378
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 1379 VILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNPDSLYSQLL 1454
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
267-547 |
6.39e-66 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 225.84 E-value: 6.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 267 IVHYLNPILLKQLIDYV-SLHDQPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAILHKILRL----- 340
Cdd:cd18596 11 VLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 341 --------------SPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILF 406
Cdd:cd18596 91 ssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 407 IPLNLCTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAAS 486
Cdd:cd18596 171 LPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLI 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 487 PFLVAIGSFTCYVLWSpdENGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18596 251 PILVTVVTFATYTLVM--GQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
260-547 |
4.39e-65 |
|
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: 222.71 E-value: 4.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 260 LARLTADIVHYLNPILLKQLIDYVSL-----HDQPLSFGIAIACIMFSCSTTRSLLQNY------QIAGMCRqavyyqTV 328
Cdd:cd18597 4 LLKLLADVLQVLSPLLLKYLINFVEDaylggPPPSIGYGIGYAIGLFLLQLLSSLLLNHffyrsmLTGAQVR------AA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 329 LSNAILHKILRLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIP 408
Cdd:cd18597 78 LTKAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 409 LN-LCTSRFIKLsQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASP 487
Cdd:cd18597 158 LQgFLMKKLFKL-RKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 488 FLVAIGSFTCYVLWSpdeNGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18597 237 VLASMLSFITYYATG---HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
887-1194 |
1.80e-63 |
|
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: 218.55 E-value: 1.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 887 FLIFFIAHFTVMIMRSL---WLSDWsnenaaikkatlssVDYLNSTSSVDGPVSVETRLIVYAGFGGLEMLL-LALAFtV 962
Cdd:cd18605 1 LILILLSLILMQASRNLidfWLSYW--------------VSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFtLLRAF-L 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 963 LTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDklqDNIRMCTQTLL----NACMILVLISISTP 1038
Cdd:cd18605 66 FAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTID---DSLPFILNILLaqlfGLLGYLVVICYQLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1039 IFLVCAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSH 1118
Cdd:cd18605 143 WLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQ 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1119 MSNRWLATRLELLGNTCVLFASLSATLS-TKYFGLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEY 1194
Cdd:cd18605 223 AASQWLSIRLQLLGVLIVTFVALTAVVQhFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
258-547 |
9.00e-59 |
|
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: 204.32 E-value: 9.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 258 LTLARLTADIVHYLNPILLKQLIDYVSLHDQPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAILHKI 337
Cdd:cd18598 2 LGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 338 LRLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFI 417
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 418 KLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTC 497
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 392896924 498 YVLWSpdeNGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18598 242 YVLMG---NTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
262-547 |
1.62e-58 |
|
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: 204.39 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 262 RLTADIVHYLNPILLKQLIDYVSLHDQP------------------LSFGIAIACIMFSCS-TTRSLLQNYQ-IAgmCRQ 321
Cdd:cd18591 6 KLLGDLLGFVGPLCISGIVDYVEENTYSssnstdklsvsyvtveefFSNGYVLAVILFLALlLQATFSQASYhIV--IRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 322 AVYYQTVLSNAILHKILRLSPSARSNR--TAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAG 399
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSSWNLSSGsmTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 400 VCIMILFIPLNLCTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIV 479
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 480 DVANAASPFLVAIGSFTCYVLWSpdENGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLE--GEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
336-792 |
1.91e-56 |
|
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: 206.54 E-value: 1.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 336 KILRLSPSARSNRTAGEILNHAAVDIEIIVHS-----VPYLQNMWSVPFqVTLAMTMLAITLGWAAMAGVCIMILFIPLn 410
Cdd:COG4987 97 RLEPLAPAGLARLRSGDLLNRLVADVDALDNLylrvlLPLLVALLVILA-AVAFLAFFSPALALVLALGLLLAGLLLPL- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 411 lctsRFIKLSQQKQMKIKDERTKLSN---EMLNGIKVVKLY----AWEESFEDQINRLRAKEVKMlrnvcilSRIVDVAN 483
Cdd:COG4987 175 ----LAARLGRRAGRRLAAARAALRArltDLLQGAAELAAYgaldRALARLDAAEARLAAAQRRL-------ARLSALAQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 484 AASPFLVAIGSFTCYVLWSP--DENGLTPS----VAFVALTIFnqlrQPMRMVANLINTLVQARVSNKRLRQFLNDE--- 554
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPlvAAGALSGPllalLVLAALALF----EALAPLPAAAQHLGRVRAAARRLNELLDAPpav 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 555 -EMERKTEVALGNAIVFKNASLNWKGpQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-- 631
Cdd:COG4987 320 tEPAEPAPAPGGPSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvd 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 -----------SIAYVPQHSWIFNKTIKENILFGN-ELSNyfyDQVVGSC---QLKTDFRHFQQGENTMVGENGITLSGG 696
Cdd:COG4987 399 lrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARpDATD---EELWAALervGLGDWLAALPDGLDTWLGEGGRRLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 697 QKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGS 776
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL---LEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
490
....*....|....*.
gi 392896924 777 FEDIAYVDGPFGRLWS 792
Cdd:COG4987 553 HEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
253-779 |
3.33e-55 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 202.68 E-value: 3.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 253 ATIITLTLARLTADIVHYLnpillkqLIDYVSLHDQPLSFGIAIACIMFscsttRSLLQNYQ--IAGMCRQAVyyQTVLS 330
Cdd:COG4988 29 SGLLIIAQAWLLASLLAGL-------IIGGAPLSALLPLLGLLLAVLLL-----RALLAWLRerAAFRAAARV--KRRLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 331 NAILHKILRLSPSARSNRTAGEILNhaavdieIIVHSVPYLQNMWS--VPfQVTLAMTM-LAI-----TLGWAAMAGVCI 402
Cdd:COG4988 95 RRLLEKLLALGPAWLRGKSTGELAT-------LLTEGVEALDGYFAryLP-QLFLAALVpLLIlvavfPLDWLSGLILLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 403 MILFIPLnlctsrFIKL-------SQQKQMkikDERTKLSN---EMLNGIKVVKLYAWEESFEDQINR----LRAKEVKM 468
Cdd:COG4988 167 TAPLIPL------FMILvgkgaakASRRQW---RALARLSGhflDRLRGLTTLKLFGRAKAEAERIAEasedFRKRTMKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 469 LRnVCILSRIV-DVANAASPFLVAIgsftcYVLWSPDENGLTPSVAFVALTI----FnqlrQPMRMVAnlinTLVQARVS 543
Cdd:COG4988 238 LR-VAFLSSAVlEFFASLSIALVAV-----YIGFRLLGGSLTLFAALFVLLLapefF----LPLRDLG----SFYHARAN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 544 NK----RLRQFLNDEEME-----RKTEVALGNAIVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLS 614
Cdd:COG4988 304 GIaaaeKIFALLDAPEPAapagtAPLPAAGPPSIELEDVSFSY--PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 615 AVLDEMVLLDGRVKVGG-------------SIAYVPQHSWIFNKTIKENILFGN------ELsnyfyDQVVGSCQLKTDF 675
Cdd:COG4988 382 LLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpdasdeEL-----EAALEAAGLDEFV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 676 RHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQ 755
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLA 533
|
570 580
....*....|....*....|....
gi 392896924 756 YTKYVDTIYVIEDGQIVQHGSFED 779
Cdd:COG4988 534 LLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1219-1444 |
3.51e-55 |
|
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: 192.06 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFNLDPFNQYSDDQIWN-CLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGAR 1377
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1378 IVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLL 1444
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
584-803 |
5.30e-55 |
|
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: 193.53 E-value: 5.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGSIAYVPQHSWIFNKTIKENILFGNELSNYFYD 663
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 664 QVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPdgLLR 743
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 744 SKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLWSECENSDEDVAD 803
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFSAE 268
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
995-1455 |
9.78e-54 |
|
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: 198.45 E-value: 9.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 995 TGRIINRLSRDLDVIDKLQdnIR----MCTQTLLNACMILVLISISTPIFLVCAAPL----ILIYYFVMIYYIPTSRQLK 1066
Cdd:COG4987 111 SGDLLNRLVADVDALDNLY--LRvllpLLVALLVILAAVAFLAFFSPALALVLALGLllagLLLPLLAARLGRRAGRRLA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1067 RLESANRSpilsTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRylshmsnrWLATRLELLGNTCVLFASLSATLS 1146
Cdd:COG4987 189 AARAALRA----RLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQ--------RRLARLSALAQALLQLAAGLAVVA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1147 TKYFG--------LTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEyqkLEPEAPWRIEKslENEEKWPVK 1218
Cdd:COG4987 257 VLWLAaplvaagaLSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNE---LLDAPPAVTEP--AEPAPAPGG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFNL---DPfnQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRG 1375
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRD 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1376 ARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNPdSLYSQLLN 1455
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQ 568
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
887-1194 |
1.22e-52 |
|
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: 187.91 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 887 FLIFFIAHFTVMIMRSLWLSDWSNENAaiKKATLSSVDYLNSTSSVDGPVSVETR-LIVYAGFGGLEMLL-LALAFTVLT 964
Cdd:cd18601 8 LVLLNIAAQVLYVLSDWWLSYWANLEE--KLNDTTDRVQGENSTNVDIEDLDRDFnLGIYAGLTAATFVFgFLRSLLFFH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 965 IgSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKL-----QDNIrmctQTLLNACMILVLISISTPI 1039
Cdd:cd18601 86 V-AVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLlpltfLDFL----QLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1040 FLVCAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHM 1119
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1120 SNRWLATRLELLgntCVLF---ASLSATLSTKyfGLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERVNEY 1194
Cdd:cd18601 241 TSRWLAVRLDAL---CALFvtvVAFGSLFLAE--SLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
942-1443 |
1.62e-52 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 194.98 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLsrdLDVIDKLQDNI----- 1016
Cdd:COG4988 61 LGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEALDGYFarylp 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1017 RMcTQTLLNACMILVLIS----ISTPIFLVCAaPLILIYyFVMIYYIPTSRQLKRLESANRspiLSTI-AESIHGASSIR 1091
Cdd:COG4988 138 QL-FLAALVPLLILVAVFpldwLSGLILLVTA-PLIPLF-MILVGKGAAKASRRQWRALAR---LSGHfLDRLRGLTTLK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1092 AFDKTERTTTALSTNVDKFAQcrylshmsnrwlAT----RLELLgNTCVL--FASLSATLSTKYFGLTPGMAGLSVSYAL 1165
Cdd:COG4988 212 LFGRAKAEAERIAEASEDFRK------------RTmkvlRVAFL-SSAVLefFASLSIALVAVYIGFRLLGGSLTLFAAL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1166 TI----TEVLnICVRSVS----EIESNIVSVERVNEYQKLEPEAPWRIEKSLEneekWPVKGKIELDGFSMRYRKNLPlV 1237
Cdd:COG4988 279 FVlllaPEFF-LPLRDLGsfyhARANGIAAAEKIFALLDAPEPAAPAGTAPLP----AAGPPSIELEDVSFSYPGGRP-A 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLD 1317
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1318 PFN-QYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIV 1396
Cdd:COG4988 433 LGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 392896924 1397 QRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLL 1443
Cdd:COG4988 513 LQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
982-1459 |
7.17e-49 |
|
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: 184.15 E-value: 7.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 982 LLVAPISFFDTTPTGRIINRLSRDLD-VIDKLQDNIRMCTQ---TLLNACMILVLISISTPIFLVCAAPLILiyyFVMIY 1057
Cdd:TIGR02203 97 LLGLPVSFFDRQPTGTLLSRITFDSEqVASAATDAFIVLVRetlTVIGLFIVLLYYSWQLTLIVVVMLPVLS---ILMRR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1058 YiptSRQLKRL--ESANRSPILSTIA-ESIHGASSIRAFD----KTERTTTALSTNVD---KFAQCRYLSHMSNRWLATr 1127
Cdd:TIGR02203 174 V---SKRLRRIskEIQNSMGQVTTVAeETLQGYRVVKLFGgqayETRRFDAVSNRNRRlamKMTSAGSISSPITQLIAS- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1128 lelLGNTCVLFASLSATLSTKyfgLTPG-MAGLSVSYALTITEVlnicvRSVSEI----ESNIVSVERVNEYQKLEPEAP 1202
Cdd:TIGR02203 250 ---LALAVVLFIALFQAQAGS---LTAGdFTAFITAMIALIRPL-----KSLTNVnapmQRGLAAAESLFTLLDSPPEKD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1203 wriEKSLENEEkwpVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKID 1282
Cdd:TIGR02203 319 ---TGTRAIER---ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1283 DVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNL---DPfNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMS 1359
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1360 VGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTP 1439
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTH 551
|
490 500
....*....|....*....|
gi 392896924 1440 SNlLLNPDSLYSQLLNEKNR 1459
Cdd:TIGR02203 552 NE-LLARNGLYAQLHNMQFR 570
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1221-1453 |
3.91e-48 |
|
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: 172.03 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSGTLRFNLdpfnQY-----SDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRG 1375
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1376 ARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQL 1453
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEE-LLAQGGVYAKL 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
956-1443 |
1.20e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 181.07 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 956 LALAFTVLTI--GSL---------RASYG----LHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIdklQDNIRMCT 1020
Cdd:PRK10790 67 LAAAYVGLQLlaAGLhyaqsllfnRAAVGvvqqLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVI---RDLYVTVV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1021 QTLLNA-----CMILVLISISTPIFLVCAA--PLILIyyfVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAF 1093
Cdd:PRK10790 144 ATVLRSaaligAMLVAMFSLDWRMALVAIMifPAVLV---VMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1094 DKTERTTTALStnvdkfAQCRylSHMSNRWLATRLE--LLGNTCVLFASLSATLSTKYFGLTP-GMAGLSVSYALT---- 1166
Cdd:PRK10790 221 RQQARFGERMG------EASR--SHYMARMQTLRLDgfLLRPLLSLFSALILCGLLMLFGFSAsGTIEVGVLYAFIsylg 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1167 -ITEVLNICVRSVSEIESNIVSVERVNEYQklepEAPwriEKSLENEEKWPVKGKIELDGFSMRYRKNLPlVLKNIDLKI 1245
Cdd:PRK10790 293 rLNEPLIELTTQQSMLQQAVVAGERVFELM----DGP---RQQYGNDDRPLQSGRIDIDNVSFAYRDDNL-VLQNINLSV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1246 EGGERIGVIGRTGSGKS---SLTMALYRMIEGEsgtIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQY 1322
Cdd:PRK10790 365 PSRGFVALVGHTGSGKStlaSLLMGYYPLTEGE---IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1323 SDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQ 1402
Cdd:PRK10790 442 SEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 392896924 1403 HFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLL 1443
Cdd:PRK10790 522 VREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1221-1432 |
1.63e-47 |
|
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: 167.56 E-value: 1.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSGTLRFNLdpfnqysddqiwncleicqlkqfaqeddktldryiaeggknMSVGERQLLCLCRALLRGARIVI 1380
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1381 LDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGR 1432
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1221-1453 |
3.34e-46 |
|
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: 166.25 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSGTLRFNLdpfnQY-----SDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRG 1375
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1376 ARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQL 1453
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEE-LLAKGGLYAEM 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1219-1459 |
3.63e-45 |
|
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: 165.03 E-value: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGEsGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFNLDPFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARI 1378
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1379 VILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQLLNEKN 1458
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQK-LLNEKSHFKQAISPSD 238
|
.
gi 392896924 1459 R 1459
Cdd:cd03289 239 R 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
568-769 |
1.32e-44 |
|
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: 161.34 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkGPqNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRV-----------------KVG 630
Cdd:cd03290 1 VQVTNGYFSW-GS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 631 GSIAYVPQHSWIFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQD 710
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 711 KDIYLLDDPLSAVDAHVGRALFDkvigpDGLLR-----SKTRVLVTHNLQYTKYVDTIYVIEDG 769
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
273-547 |
4.39e-44 |
|
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: 162.38 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 273 PILLKQLIDYVSLHDQPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAILHKILRLSPSARSNRTAGE 352
Cdd:cd18559 17 PSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 353 ILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFIKLSQQKQMKIKDERT 432
Cdd:cd18559 97 LVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 433 KLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTCYVLWSpDENGLTPSV 512
Cdd:cd18559 177 KLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRH-SLAGLVALK 255
|
250 260 270
....*....|....*....|....*....|....*
gi 392896924 513 AFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18559 256 VFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1219-1433 |
1.01e-43 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 158.52 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFNLDPFNQYSDDQ-IWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGAR 1377
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 1378 IVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRV 1433
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
568-770 |
1.36e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 150.61 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIA 634
Cdd:cd03228 1 IEFKNVSFSY-PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENIlfgnelsnyfydqvvgscqlktdfrhfqqgentmvgengitLSGGQKARISLARAVYQDKDIY 714
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 715 LLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQ 770
Cdd:cd03228 119 ILDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
568-791 |
3.99e-41 |
|
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: 151.92 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkgPQNP--PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS------------- 632
Cdd:cd03249 1 IEFKNVSFRY--PSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 633 IAYVPQHSWIFNKTIKENILFG-NELSNyfyDQVVGSCQLK--TDF-RHFQQGENTMVGENGITLSGGQKARISLARAVY 708
Cdd:cd03249 79 IGLVSQEPVLFDGTIAENIRYGkPDATD---EEVEEAAKKAniHDFiMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 709 QDKDIYLLDDPLSAVDAH----VGRALfdkvigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVD 784
Cdd:cd03249 156 RNPKILLLDEATSALDAEseklVQEAL-------DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
....*..
gi 392896924 785 GPFGRLW 791
Cdd:cd03249 229 GVYAKLV 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
568-793 |
3.34e-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: 149.30 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIA 634
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENILFGNElsNYFYDQVVGSC---QLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDK 711
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRP--DATDEEVIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 712 DIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLW 791
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
..
gi 392896924 792 SE 793
Cdd:cd03253 234 KA 235
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
954-1453 |
4.30e-40 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 157.94 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 954 LLLALA-----FTVLTIGSlRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKL-QDNIRMCTQTLLNAC 1027
Cdd:TIGR02204 69 LVLALGtaarfYLVTWLGE-RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSViGSSLSMALRNALMCI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1028 MILVLISISTP---IFLVCAAPLILIYYFVMiyyiptSRQLKRL--ESANRSPILSTIA-ESIHGASSIRAFDKTERTTT 1101
Cdd:TIGR02204 148 GGLIMMFITSPkltSLVLLAVPLVLLPILLF------GRRVRKLsrESQDRIADAGSYAgETLGAIRTVQAFGHEDAERS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1102 ALSTNVDKFAQcrylshMSNRWLATRLELLgnTCVLFASLSATLSTKYFG--------LTPGMAGLSVSYAL-------T 1166
Cdd:TIGR02204 222 RFGGAVEKAYE------AARQRIRTRALLT--AIVIVLVFGAIVGVLWVGahdviagkMSAGTLGQFVFYAVmvagsigT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1167 ITEVLNicvrsvsEIESNIVSVERVNEYQKLEPE--APwRIEKSLENeekwPVKGKIELDGFSMRY--RKNLPlVLKNID 1242
Cdd:TIGR02204 294 LSEVWG-------ELQRAAGAAERLIELLQAEPDikAP-AHPKTLPV----PLRGEIEFEQVNFAYpaRPDQP-ALDGLN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1243 LKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFN-Q 1321
Cdd:TIGR02204 361 LTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1322 YSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIR 1401
Cdd:TIGR02204 441 ATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALE 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1402 QHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQL 1453
Cdd:TIGR02204 521 TLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAE-LIAKGGLYARL 571
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
953-1454 |
4.35e-40 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 159.89 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 953 MLLLALAFTV---LTIGSLRASYG-----LHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVI-----DKLQDNIRMC 1019
Cdd:TIGR00958 207 MCLLSIASSVsagLRGGSFNYTMArinlrIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsrslsLNVNVLLRNL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1020 TQTLLNACMILVL---ISISTPIFLvcaAPLILIYYFVMIYYIPTSRQLKrlesanrspilSTIAESIHGASSIRAFDKT 1096
Cdd:TIGR00958 287 VMLLGLLGFMLWLsprLTMVTLINL---PLVFLAEKVFGKRYQLLSEELQ-----------EAVAKANQVAEEALSGMRT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1097 ERTTTALSTNVDKFAQcrYLSHMSNRWLATRLELLGNTCV--LFASLSATLSTKYFG---LTPGMA-GLSVS---YALTI 1167
Cdd:TIGR00958 353 VRSFAAEEGEASRFKE--ALEETLQLNKRKALAYAGYLWTtsVLGMLIQVLVLYYGGqlvLTGKVSsGNLVSfllYQEQL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1168 TEVLNICVRSVSEIESNIVSVERVNEYQKLEPeapwRIEKSLENEEKWpVKGKIELD--GFSMRYRKNLPlVLKNIDLKI 1245
Cdd:TIGR00958 431 GEAVRVLSYVYSGMMQAVGASEKVFEYLDRKP----NIPLTGTLAPLN-LEGLIEFQdvSFSYPNRPDVP-VLKGLTFTL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1246 EGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLD-PFNQYSD 1324
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPD 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1325 DQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAirQHF 1404
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSR 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 392896924 1405 PQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNPDsLYSQLL 1454
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG-CYKHLV 711
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
273-547 |
5.65e-40 |
|
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: 150.40 E-value: 5.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 273 PILLKQLIDYVSLHDQPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAILHKILRLSPSarSNRTAGE 352
Cdd:cd18592 18 TILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSL--GDKSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 353 ILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFIKLSQQKQMKIKDERT 432
Cdd:cd18592 96 LINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 433 KLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTCYVLwspDENGLTPSV 512
Cdd:cd18592 176 RLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVA---LGNDLTAAQ 252
|
250 260 270
....*....|....*....|....*....|....*
gi 392896924 513 AFVALTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18592 253 AFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1221-1453 |
2.58e-39 |
|
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: 146.48 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSGTLRFNLDPFNQYSD-DQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIV 1379
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 1380 ILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEfDTPSNLLLNPDSLYSQL 1453
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE-QGSHDELLAENGLYAYL 233
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
273-547 |
4.07e-38 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 145.08 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 273 PILLKQLIDY-VSLHDQPLSFGIAIACIMFSCSTTRSLLQ-----NYQIAGM-CRQAvyyqtvLSNAILHKILRLSPSAR 345
Cdd:cd18594 17 PLLLGRLVAYfVPDSTVTKTEAYLYALGLSLCAFLRVLLHhpyffGLHRYGMqLRIA------LSSLIYKKTLKLSSSAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 346 SNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLNLCTSRFIKLSQQKQM 425
Cdd:cd18594 91 SKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 426 KIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTCYVLWSpde 505
Cdd:cd18594 171 GLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTG--- 247
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 392896924 506 NGLTPSVAFVALTIFNQLRQPM-RMVANLINTLVQARVSNKRL 547
Cdd:cd18594 248 NTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
568-778 |
8.60e-38 |
|
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: 141.98 E-value: 8.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGpqNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIA 634
Cdd:cd03254 3 IEFENVNFSYDE--KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENILFGNELSNYfyDQVVGSCQLK--TDF-RHFQQGENTMVGENGITLSGGQKARISLARAVYQDK 711
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAgaHDFiMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 712 DIYLLDDPLSAVDAH----VGRALfdkvigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFE 778
Cdd:cd03254 159 KILILDEATSNIDTEteklIQEAL-------EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHD 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
568-791 |
2.79e-37 |
|
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: 140.44 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIA 634
Cdd:cd03251 1 VEFKNVTFRY-PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENILFGNElsNYFYDQVVGSCQLK--TDF-RHFQQGENTMVGENGITLSGGQKARISLARAVYQDK 711
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRP--GATREEVEEAARAAnaHEFiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 712 DIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLW 791
Cdd:cd03251 158 PILILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1221-1453 |
3.01e-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: 137.67 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRY--RKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFN--LDPFNQYSDDQIWNCLEiCQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGA 1376
Cdd:cd03249 80 GLVSQEPVLFDGTIAENirYGKPDATDEEVEEAAKK-ANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1377 RIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNpDSLYSQL 1453
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKL 234
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
263-547 |
7.04e-36 |
|
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: 138.51 E-value: 7.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 263 LTADIVHYLNPILLKQLIDYVSLHDQPLSFGIAIAC--------IMFSCSTTRSLLqNYQIAGM-CRQAVyyqtvlSNAI 333
Cdd:cd18593 7 FLEEAIRVVQPIFLGKLIRYFEGNGSSISLTEAYLYaggvslcsFLFIITHHPYFF-GMQRIGMrLRVAC------SSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 334 LHKILRLSPSARSNRTAGEILNHAAVDI---EIIVHSVPYLqnmWSVPFQVTLAMTMLAITLGWAAMAGVCIMILFIPLN 410
Cdd:cd18593 80 YRKALRLSQAALGKTTVGQIVNLLSNDVnrfDQAVLFLHYL---WVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 411 LCTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLV 490
Cdd:cd18593 157 SFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLI 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 491 AIGSFTCYVLWspdENGLTPSVAFVALTIFNQLRQPMRM-VANLINTLVQARVSNKRL 547
Cdd:cd18593 237 LFLTFLAYILL---GNILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1219-1453 |
7.44e-36 |
|
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: 145.73 E-value: 7.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:COG5265 356 GEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSGTLRFNLdpfnQY-----SDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALL 1373
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1374 RGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNpDSLYSQL 1453
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQM 589
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
979-1455 |
1.16e-35 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 146.42 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 979 IHALLVAPISFFDTTPTGRIINRLSRDLDVIDKLQDNIrmctQTLLNACMILVLISI-----STPIFLvCAAPLILIYYF 1053
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTI----LSLFLDMWILVIVGLflvrqNMLLFL-LSLLSIPVYAV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1054 VMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERT----TTALSTNVDK---FAQCRYLSHMsnrwLAT 1126
Cdd:TIGR01193 311 IIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERyskiDSEFGDYLNKsfkYQKADQGQQA----IKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1127 RLELLGNTCVLFASLSATLSTKyfgLTPGMA---GLSVSYALT-ITEVLNIcvrsVSEIESNIVSVERVNEYQKLEPEap 1202
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGK---LTLGQLitfNALLSYFLTpLENIINL----QPKLQAARVANNRLNEVYLVDSE-- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1203 wrIEKSLENEEKWPVKGKIELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKID 1282
Cdd:TIGR01193 458 --FINKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1283 DVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQ--YSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSV 1360
Cdd:TIGR01193 535 GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISG 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1361 GERQLLCLCRALLRGARIVILDEATASVDTVTDgivQRAIRQHFP--QSTTISIAHRLDTIVDSDRIVVLDAGRVAEfDT 1438
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLNlqDKTIIFVAHRLSVAKQSDKIIVLDHGKIIE-QG 690
|
490
....*....|....*..
gi 392896924 1439 PSNLLLNPDSLYSQLLN 1455
Cdd:TIGR01193 691 SHDELLDRNGFYASLIH 707
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
567-775 |
1.17e-35 |
|
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: 135.41 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWKGPQNPpVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SI 633
Cdd:cd03245 2 RIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 634 AYVPQHSWIFNKTIKENILFGNELSNyfyDQ-VVGSCQLK--TDF--RHfQQGENTMVGENGITLSGGQKARISLARAVY 708
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLAD---DErILRAAELAgvTDFvnKH-PNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHG 775
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
275-766 |
1.84e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 143.20 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 275 LLKQLIDYVSLHDQPLSfGIAIAC-IMFSCSTTRSLLQNYQIAGMCRQAVYYQTVLSNAILHKILRLSPSARSNRTAGEI 353
Cdd:TIGR02857 25 LLARVVDGLISAGEPLA-ELLPALgALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 354 LNHAAVDIEIIVHSV----PYLQNMWSVPfqvtLAMTMLAITLGWAAMAGVCIMILFIPLnlctsrFIKL----SQQKQM 425
Cdd:TIGR02857 104 ATLALEGVEALDGYFarylPQLVLAVIVP----LAILAAVFPQDWISGLILLLTAPLIPI------FMILigwaAQAAAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 426 KIKDERTKLSN---EMLNGIKVVKLYAWEESFEDQINR----LRAKEVKMLRnVCILSRIV-DVANAASPFLVA--IGsF 495
Cdd:TIGR02857 174 KQWAALSRLSGhflDRLRGLPTLKLFGRAKAQAAAIRRsseeYRERTMRVLR-IAFLSSAVlELFATLSVALVAvyIG-F 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 496 TCYVlwspdeNGLTPSVAFVALTIFNQLRQPMRMVANLINTLVQARVSNKRLRQFLNDEEM----ERKTEVALGNAIVFK 571
Cdd:TIGR02857 252 RLLA------GDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRplagKAPVTAAPASSLEFS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 572 NASLNWKGpqNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAYVPQ 638
Cdd:TIGR02857 326 GVSVAYPG--RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 639 HSWIFNKTIKENILFG-NELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLD 717
Cdd:TIGR02857 404 HPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 392896924 718 DPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVI 766
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
580-793 |
3.78e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 143.06 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 580 PQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLlDGRVKVGG-------------SIAYVPQHSWIFNKT 646
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGielreldpeswrkHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGN-ELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:PRK11174 439 LRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 726 H----VGRALFDkvigpdgLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLWSE 793
Cdd:PRK11174 519 HseqlVMQALNA-------ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
956-1443 |
4.28e-35 |
|
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: 144.33 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 956 LALAFTVLTIGSlRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKLQDNIRMCTQTLLNACMILVLI-S 1034
Cdd:TIGR03797 194 LAQSLAVLRLET-RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMfY 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1035 ISTPIFLVCAA-PLILIYYFVMIYYIPTSRQLKRLESANRspILSTIAESIHGASSIRAFDKTERTTTALSTNvdkFAQC 1113
Cdd:TIGR03797 273 YSWKLALVAVAlALVAIAVTLVLGLLQVRKERRLLELSGK--ISGLTVQLINGISKLRVAGAENRAFARWAKL---FSRQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1114 R---YLSHMSNRWLATRLELLG--NTCVLFASLSATLSTKyfGLTPGmAGLSVSYALT--ITEVLNIcVRSVSEIESNIV 1186
Cdd:TIGR03797 348 RkleLSAQRIENLLTVFNAVLPvlTSAALFAAAISLLGGA--GLSLG-SFLAFNTAFGsfSGAVTQL-SNTLISILAVIP 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1187 SVERVNEYQKLEPEApwrieksleNEEKWP---VKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSS 1263
Cdd:TIGR03797 424 LWERAKPILEALPEV---------DEAKTDpgkLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1264 LtmalYRMIEG----ESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQIWnclEICQLKQF 1339
Cdd:TIGR03797 495 L----LRLLLGfetpESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAW---EAARMAGL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1340 AQEDDKT---LDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHfpQSTTISIAHRL 1416
Cdd:TIGR03797 568 AEDIRAMpmgMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRL 645
|
490 500
....*....|....*....|....*..
gi 392896924 1417 DTIVDSDRIVVLDAGRVAEFDTPSNLL 1443
Cdd:TIGR03797 646 STIRNADRIYVLDAGRVVQQGTYDELM 672
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
941-1194 |
5.63e-34 |
|
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: 133.11 E-value: 5.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 941 RLIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKLQDNI-RMC 1019
Cdd:cd18559 40 YLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQViKMW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1020 TQTLLNACMILVLISISTPIFLVcAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERT 1099
Cdd:cd18559 120 MGPLQNVIGLYLLILLAGPMAAV-GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1100 TTALSTNVDKfAQCRYLSHMSNRWLATRLELLGNTCVLFASLSATLSTkyfGLTPGMAGLSVSYALTITEVLNICVRSVS 1179
Cdd:cd18559 199 IRQVDAKRDN-ELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSR---HSLAGLVALKVFYSLALTTYLNWPLNMSP 274
|
250
....*....|....*
gi 392896924 1180 EIESNIVSVERVNEY 1194
Cdd:cd18559 275 EVITNIVAAEVSLER 289
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
568-790 |
7.80e-34 |
|
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: 130.68 E-value: 7.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIA 634
Cdd:cd03252 1 ITFEHVRFRYK-PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENILFGNELSNYfyDQVVGSCQLKT--DF-RHFQQGENTMVGENGITLSGGQKARISLARAVYQDK 711
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSM--ERVIEAAKLAGahDFiSELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 712 DIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRL 790
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
995-1416 |
8.04e-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: 135.18 E-value: 8.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 995 TGRIINRLSRDldvIDKLQDnirMCTQTLLNACMILVLISIST---PIFLVCAAPLILIYYFVMIYYIP-----TSRQLK 1066
Cdd:TIGR02868 109 RGDLLGRLGAD---VDALQD---LYVRVIVPAGVALVVGAAAVaaiAVLSVPAALILAAGLLLAGFVAPlvslrAARAAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1067 RLESANRSPILSTIAESIHGASSIRAFDKTERTTTALStnvdkfAQCRYLSHMSNRwlATRLELLGNTCVLFASLSATLS 1146
Cdd:TIGR02868 183 QALARLRGELAAQLTDALDGAAELVASGALPAALAQVE------EADRELTRAERR--AAAATALGAALTLLAAGLAVLG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1147 TKYFGLTPGMAG--------LSVSYALTITEVLNICVRSVSEIESNIVSVERVNEyqkLEPEAPWRIEKSLENEEKWPVK 1218
Cdd:TIGR02868 255 ALWAGGPAVADGrlapvtlaVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVE---VLDAAGPVAEGSAPAAGAVGLG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 G-KIELDGFSMRYRKNlPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSK 1297
Cdd:TIGR02868 332 KpTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1298 LIIIPQEPVVFSGTLRFNL---DPfnQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLR 1374
Cdd:TIGR02868 411 VSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 392896924 1375 GARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRL 1416
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
404-790 |
1.44e-32 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 135.15 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 404 ILFIPLNLCTSRFIKLSQQKQMKIkDERTKLSNEMLNGIKVVKLYAW----EESFEDQINRLRAKEVKMLRNVCILSRIV 479
Cdd:PRK11176 177 IVSIAIRVVSKRFRNISKNMQNTM-GQVTTSAEQMLKGHKEVLIFGGqeveTKRFDKVSNRMRQQGMKMVSASSISDPII 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 480 D-VANAASPFLVAIGSFTcyvlwSPDENgLTPSVAFValtIFNQLRQPMRMVANLINTLVQAR---VSNKRLRQFLnDEE 555
Cdd:PRK11176 256 QlIASLALAFVLYAASFP-----SVMDT-LTAGTITV---VFSSMIALMRPLKSLTNVNAQFQrgmAACQTLFAIL-DLE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 556 ME-----RKTEVALGNaIVFKNASLNWKGPQNPpVLKDLSATIKPGQLIAIVGSVGGGKS---SLLSAVLDEM---VLLD 624
Cdd:PRK11176 326 QEkdegkRVIERAKGD-IEFRNVTFTYPGKEVP-ALRNINFKIPAGKTVALVGRSGSGKStiaNLLTRFYDIDegeILLD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 625 GR-------VKVGGSIAYVPQHSWIFNKTIKENILFGNElSNYFYDQVVGSCQLK--TDF-RHFQQGENTMVGENGITLS 694
Cdd:PRK11176 404 GHdlrdytlASLRNQVALVSQNVHLFNDTIANNIAYART-EQYSREQIEEAARMAyaMDFiNKMDNGLDTVIGENGVLLS 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 695 GGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQH 774
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
410
....*....|....*.
gi 392896924 775 GSFEDIAYVDGPFGRL 790
Cdd:PRK11176 560 GTHAELLAQNGVYAQL 575
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
934-1428 |
1.64e-32 |
|
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: 134.34 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 934 GPVSVETRLIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLsrdLDVIDKLQ 1013
Cdd:TIGR02857 39 PLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA---LEGVEALD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1014 DNIRMCTQTLLNACMILVLI-------SISTPIFLVCAAPLILIYyFVMIYYIPTSRQLKRLESANRspiLST-IAESIH 1085
Cdd:TIGR02857 116 GYFARYLPQLVLAVIVPLAIlaavfpqDWISGLILLLTAPLIPIF-MILIGWAAQAAARKQWAALSR---LSGhFLDRLR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1086 GASSIRAFDKTERTTTALSTNVDKFAQcrylshmsnRWLAT-RLELLgNTCVL--FASLSATLSTKYFGLTPGMAGLSVS 1162
Cdd:TIGR02857 192 GLPTLKLFGRAKAQAAAIRRSSEEYRE---------RTMRVlRIAFL-SSAVLelFATLSVALVAVYIGFRLLAGDLDLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1163 YALTI----TEVLnICVRSVS-------EIESNIVSVERVNEyqklEPEAPWRIEKSLENEEKWPvkgkIELDGFSMRYR 1231
Cdd:TIGR02857 262 TGLFVlllaPEFY-LPLRQLGaqyharaDGVAAAEALFAVLD----AAPRPLAGKAPVTAAPASS----LEFSGVSVAYP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1232 KNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGT 1311
Cdd:TIGR02857 333 GRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1312 LRFNL---DPfnQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASV 1388
Cdd:TIGR02857 412 IAENIrlaRP--DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 392896924 1389 DTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVL 1428
Cdd:TIGR02857 490 DAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1185-1453 |
6.37e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 133.03 E-value: 6.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1185 IVSVERVNEYQKLEPEAPWRiekslENEEKWPVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSL 1264
Cdd:PRK11160 308 IASARRINEITEQKPEVTFP-----TTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1265 TMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTLRFNL---DPfnQYSDDQIWNCLEICQLKQFAq 1341
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLL- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1342 EDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVD 1421
Cdd:PRK11160 460 EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
|
250 260 270
....*....|....*....|....*....|..
gi 392896924 1422 SDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQL 1453
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQE-LLAQQGRYYQL 570
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
512-790 |
1.18e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 126.23 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 512 VAFVALTifNQLRQPMRMVANLINTLVQARvsnKRLRQFLNDEEM-----ERKTEVALGN---AIVFKNASLNWKGpqNP 583
Cdd:PRK13657 276 VAFVGFA--TLLIGRLDQVVAFINQVFMAA---PKLEEFFEVEDAvpdvrDPPGAIDLGRvkgAVEFDDVSFSYDN--SR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKS---SLLSAVLDEMVlldGRVKVGG-------------SIAYVPQHSWIFNKTI 647
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKStliNLLQRVFDPQS---GRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 648 KENILFGNElsNYFYDQVVGSCQLK--TDFRHFQ-QGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVD 724
Cdd:PRK13657 426 EDNIRVGRP--DATDEEMRAAAERAqaHDFIERKpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 725 ----AHVGRALfdkvigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRL 790
Cdd:PRK13657 504 veteAKVKAAL-------DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
525-780 |
1.30e-29 |
|
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: 126.02 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 525 QPMRMVANLINTLVQARVSNKRLRQFLNDEEMERKTeVAL----GNaIVFKNASLnwkGP--QNPPVLKDLSATIKPGQL 598
Cdd:COG4618 286 APIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPER-MPLprpkGR-LSVENLTV---VPpgSKRPILRGVSFSLEPGEV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 599 IAIVGSVGGGKSSL---LSAVLDEM---VLLDG-------RVKVGGSIAYVPQHSWIFNKTIKENI-LFGNELSnyfyDQ 664
Cdd:COG4618 361 LGVIGPSGSGKSTLarlLVGVWPPTagsVRLDGadlsqwdREELGRHIGYLPQDVELFDGTIAENIaRFGDADP----EK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 665 VVGSCQLK--TDF-RHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGpdgl 741
Cdd:COG4618 437 VVAAAKLAgvHEMiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA---- 512
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 392896924 742 LRS--KTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG4618 513 LKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1217-1437 |
1.80e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.84 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1217 VKGKIELDGFSMRYrKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRS 1296
Cdd:PRK13657 331 VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1297 KLIIIPQEPVVFSGTLRFNL-----DPfnqySDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRA 1371
Cdd:PRK13657 410 NIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 1372 LLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAE---FD 1437
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFD 554
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
336-791 |
2.69e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 124.94 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 336 KILRLSPSARSNRTAGEILNHAAVDIEIIVHSvpYLQNMwsVPFQVTLAMTM------------LAITLGWAAMAGVCIM 403
Cdd:PRK11160 102 KLLPLSPAGLARYRQGDLLNRLVADVDTLDHL--YLRLI--SPLVAALVVILvltiglsffdltLALTLGGILLLLLLLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 404 -ILFIPLNLCTSRfiKLSQQKQmkikDERTKLSnEMLNGIKVVKLYAWEESFEDQINrlrAKEVKMLRNVCILSRIVDVA 482
Cdd:PRK11160 178 pLLFYRLGKKPGQ--DLTHLRA----QYRVQLT-EWLQGQAELTLFGAEDRYRQQLE---QTEQQWLAAQRRQANLTGLS 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 483 NAAspfLVAIGSFT-CYVLW--SPDENGLTPSVAFVALTIFNQLRQ-PMRM-VANLINTLVQARVSNKRLrqflnDEEME 557
Cdd:PRK11160 248 QAL---MILANGLTvVLMLWlaAGGVGGNAQPGALIALFVFAALAAfEALMpVAGAFQHLGQVIASARRI-----NEITE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 558 RKTEVALGN---------AIVFKNASLNWKGpQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVK 628
Cdd:PRK11160 320 QKPEVTFPTtstaaadqvSLTLNNVSFTYPD-QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 629 VGG-------------SIAYVPQHSWIFNKTIKENILFGNELSNyfyD-------QVVG-SCQLKTDfrhfqQGENTMVG 687
Cdd:PRK11160 399 LNGqpiadyseaalrqAISVVSQRVHLFSATLRDNLLLAAPNAS---DealievlQQVGlEKLLEDD-----KGLNAWLG 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 688 ENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS----KTRVLVTHNLQYTKYVDTI 763
Cdd:PRK11160 471 EGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILE-------LLAEhaqnKTVLMITHRLTGLEQFDRI 543
|
490 500
....*....|....*....|....*...
gi 392896924 764 YVIEDGQIVQHGSFEDIAYVDGPFGRLW 791
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
567-780 |
3.11e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWkgpQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG--------SIAYVPQ 638
Cdd:COG1121 6 AIELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 639 HS---WIFNKTIKENILFG--------NELSNYFYDQV------VGScqlkTDFRHFQqgentmVGEngitLSGGQKARI 701
Cdd:COG1121 83 RAevdWDFPITVRDVVLMGrygrrglfRRPSRADREAVdealerVGL----EDLADRP------IGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 702 SLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS-----KTRVLVTHNL-QYTKYVDTIYVIeDGQIVQHG 775
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRElrregKTILVVTHDLgAVREYFDRVLLL-NRGLVAHG 220
|
....*
gi 392896924 776 SFEDI 780
Cdd:COG1121 221 PPEEV 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
570-775 |
4.61e-29 |
|
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: 116.09 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 570 FKNASLNWkgpQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG--------SIAYVPQHS- 640
Cdd:cd03235 2 VEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 641 --WIFNKTIKENILFGnelsnyFYDQVVGSCQLK----------------TDFRHFQQGEntmvgengitLSGGQKARIS 702
Cdd:cd03235 79 idRDFPISVRDVVLMG------LYGHKGLFRRLSkadkakvdealervglSELADRQIGE----------LSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 703 LARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS-----KTRVLVTHNL-QYTKYVDTIYVIeDGQIVQHG 775
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYE-------LLRElrregMTILVVTHDLgLVLEYFDRVLLL-NRTVVASG 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1216-1453 |
6.52e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 123.98 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1216 PVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLR 1295
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1296 SKLIIIPQEPVVFSGTLRFNL--DPFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALL 1373
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1374 RGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNlLLNPDSLYSQL 1453
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE-LLAQNGVYAQL 575
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
336-754 |
1.10e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 122.47 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 336 KILRLSPSARSNRTAGEILNHAAVDIEiivhsvpYLQNMW-------SVPFQVTLAMTMLAITLGWAA--MAGVCIMILF 406
Cdd:TIGR02868 95 RLARQALAGRRRLRRGDLLGRLGADVD-------ALQDLYvrvivpaGVALVVGAAAVAAIAVLSVPAalILAAGLLLAG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 407 IPLNLCTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIvdvaNAAS 486
Cdd:TIGR02868 168 FVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATAL----GAAL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 487 PFLVAiGSFTCYVLW----SPDENGLTPS----VAFVALTIFNqlrqPMRMVANLINTLVQARVSNKRLRQFLNDEEM-- 556
Cdd:TIGR02868 244 TLLAA-GLAVLGALWaggpAVADGRLAPVtlavLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDAAGPva 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 557 -----ERKTEVALGNAIVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG 631
Cdd:TIGR02868 319 egsapAAGAVGLGKPTLELRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 S-------------IAYVPQHSWIFNKTIKENILFGN------ELSnyfydQVVGSCQLKTDFRHFQQGENTMVGENGIT 692
Cdd:TIGR02868 397 VpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARpdatdeELW-----AALERVGLADWLRALPDGLDTVLGEGGAR 471
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 693 LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPDgllRSKTRVLVTHNL 754
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL---SGRTVVLITHHL 530
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
886-1168 |
1.83e-28 |
|
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: 116.59 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 886 AFLIFFIAHFTVMIMrSLWLSDWsnenaaikkatlssVDYLNSTSSVDgPVSVETRLIVYAGFGGLEMLLLALAFTVLTI 965
Cdd:pfam00664 4 AILLAILSGAISPAF-PLVLGRI--------------LDVLLPDGDPE-TQALNVYSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 966 GSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNACMILVLISISTPIFLVCA 1044
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDgLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1045 APLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSNRWL 1124
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 392896924 1125 ATRLELLGNTCVLFASLSATLSTKYFGLTPGMAGLSVSYALTIT 1168
Cdd:pfam00664 228 FGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
255-527 |
2.94e-28 |
|
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: 115.82 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 255 IITLTLARLTADIVHYLNPILLKQLIDYVSLHDQPLSFGIAIACIMFS----CSTTRSLLQNYqiaGMCRQAVYYQTVLS 330
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLllglAQFILSFLQSY---LLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 331 NAILHKILRLSPSARSNRTAGEILNHAAVDIEIIVHSVPYLQNMWSVPFQVTLAMTMLAITLGWA-AMAGVCIMILFIPL 409
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 410 NLCTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFL 489
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 392896924 490 VAIGSFtCYVLWSPDENGLTPSVAFVALTIFNQLRQPM 527
Cdd:pfam00664 238 SYALAL-WFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1238-1458 |
4.40e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 121.49 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMAL-----YRmiegesGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSGTL 1312
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpYQ------GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1313 RFNL---DPfnQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVD 1389
Cdd:PRK11174 440 RDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1390 TVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAE---FDTpsnlLLNPDSLYSQLLNEKN 1458
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAHRQ 585
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
875-1191 |
6.18e-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: 116.44 E-value: 6.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 875 YIKTMGIFNSSAF-LIFFIAHFTVMIMRSL-WLsdWSNENAAIKKATLSSVDYLNSTSSVDGPVSVETRLIVYAGfggLE 952
Cdd:cd18600 6 YLRYITSHKSLIFvLILCLVIFAIEVAASLvGL--WLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVG---VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 953 MLLLALAF---TVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNACM 1028
Cdd:cd18600 81 DSLLAMGFfrgLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDlLPLTIFDFIQLFLIVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1029 ILVLISISTPIFLVCAAPLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERTTTALSTNVD 1108
Cdd:cd18600 161 AITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1109 KFAQCRYLSHMSNRWLATRLELLgntCVLFASLSATLSTKYFGLTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSV 1188
Cdd:cd18600 241 LHTANWFLYLSTLRWFQMRIEMI---FVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSV 317
|
...
gi 392896924 1189 ERV 1191
Cdd:cd18600 318 SRI 320
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
568-775 |
1.23e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 110.87 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS------------IAY 635
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 636 VPQHSWIFNKTIKENIlfgnelsnyfydqvvgscqlktdfrhfqqgentmvgenGITLSGGQKARISLARAVYQDKDIYL 715
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 716 LDDPLSAVDAHVGRALFDKVIgpdGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHG 775
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1217-1433 |
1.70e-27 |
|
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: 112.18 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1217 VKGKIELDGFSMRYRkNLP--LVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQL 1294
Cdd:cd03248 8 LKGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1295 RSKLIIIPQEPVVFSGTLRFNLD-PFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALL 1373
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1374 RGARIVILDEATASVDTVTDGIVQRAIRQhFPQSTTIS-IAHRLDTIVDSDRIVVLDAGRV 1433
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLvIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
568-777 |
1.74e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.60 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLD------EMVLLDGR-------VKVGGSIA 634
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyqptgGQVLLDGVplvqydhHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENILFGneLSNYFYDQVVGSCQLKT--DF-RHFQQGENTMVGENGITLSGGQKARISLARAVYQDK 711
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYG--LTDTPDEEIMAAAKAANahDFiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 712 DIYLLDDPLSAVDAHVGRALFDkvigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSF 777
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQE-----SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1221-1433 |
1.24e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.14 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSmrYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:COG4619 1 LELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSGTLRFNLDPFNQYSDDQIWNCLEICQLKQFAQEDDkTLDRYIAEggknMSVGERQLLCLCRALLRGARIVI 1380
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPD-ILDKPVER----LSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1381 LDEATASVDTVTDGIVQRAIRQHF--PQSTTISIAH------RLdtivdSDRIVVLDAGRV 1433
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
568-776 |
7.01e-26 |
|
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: 107.19 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIA 634
Cdd:cd03244 3 IEFKNVSLRYR-PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIY 714
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 715 LLDDPLSAVD----AHVGRALFDKvigpdglLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGS 776
Cdd:cd03244 162 VLDEATASVDpetdALIQKTIREA-------FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
570-771 |
8.33e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 107.17 E-value: 8.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 570 FKNASLNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS-------------IAYV 636
Cdd:cd03248 14 FQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 637 PQHSWIFNKTIKENILFGneLSNYFYDQVVGSCQ---LKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDI 713
Cdd:cd03248 94 GQEPVLFARSLQDNIAYG--LQSCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 714 YLLDDPLSAVDAH----VGRALFDKvigpdglLRSKTRVLVTHNLQYTKYVDTIYVIEDGQI 771
Cdd:cd03248 172 LILDEATSALDAEseqqVQQALYDW-------PERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
582-771 |
9.14e-26 |
|
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: 105.38 E-value: 9.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 582 NPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS-------------IAYVPQHSWIFNKTIK 648
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENIlfgnelsnyfydqvvgscqlktdfrhfqqgentmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVG 728
Cdd:cd03246 94 ENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 392896924 729 RALFDKVIGPDglLRSKTRVLVTHNLQYTKYVDTIYVIEDGQI 771
Cdd:cd03246 133 RALNQAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
586-721 |
1.02e-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: 104.27 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEM------VLLDGRV-------KVGGSIAYVPQHSWIFN-KTIKENI 651
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsptegtILLDGQDltdderkSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 652 LFGNELSNYFYDQVvgSCQLKTDFRHFQQGE--NTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLS 721
Cdd:pfam00005 81 RLGLLLKGLSKREK--DARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1238-1386 |
1.07e-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: 104.27 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSG-TLRFNL 1316
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1317 -------DPFNQYSDDQIWNcleicQLKQFAQEDDktLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATA 1386
Cdd:pfam00005 81 rlglllkGLSKREKDARAEE-----ALEKLGLGDL--ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1221-1433 |
1.60e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 104.61 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSGTLRFNLdpfnqysddqiwncleicqlkqfaqeddktldryiaeggknMSVGERQLLCLCRALLRGARIVI 1380
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 392896924 1381 LDEATASVDTVTDGIVQRAIRQ-HFPQSTTISIAHRLDTIVDSDRIVVLDAGRV 1433
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
508-785 |
4.99e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 111.73 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 508 LTPSVAFVALTIFnqlrqPMRMVANLINTLVQARVSNKRLRQFLNDE-EMERKTEVALGNAIVFKNASLNWKGPQN-PPV 585
Cdd:PRK10789 256 LTSFVMYLGLMIW-----PMLALAWMFNIVERGSAAYSRIRAMLAEApVVKDGSEPVPEGRGELDVNIRQFTYPQTdHPA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVG-------------GSIAYVPQHSWIFNKTIKENIL 652
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 653 FGN-ELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRAL 731
Cdd:PRK10789 411 LGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 732 FDKvigpdglLRS----KTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIAYVDG 785
Cdd:PRK10789 491 LHN-------LRQwgegRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
584-775 |
5.46e-25 |
|
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: 104.52 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEM----VLLDGRVKVG-----GSIAYVPQHSWIF-NKTIKENI 651
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIagLERPdsgeILIDGRDVTGvpperRNIGMVFQDYALFpHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 LFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRAL 731
Cdd:cd03259 94 AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392896924 732 FDKVigpDGLLRS--KTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHG 775
Cdd:cd03259 170 REEL---KELQRElgITTIYVTHDQEEAlALADRIAVMNEGRIVQVG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1221-1435 |
6.03e-25 |
|
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: 103.16 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGlHQLRSKLII 1300
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSGTLRFNLdpfnqysddqiwncleicqlkqfaqeddktldryiaegGKNMSVGERQLLCLCRALLRGARIVI 1380
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1381 LDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAE 1435
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
568-771 |
1.60e-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: 100.26 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQNP-PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAvldeMVLLD----GRVKVGG----------- 631
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNI----LGGLDrptsGEVRVDGtdisklsekel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 ------SIAYVPQ-HSWIFNKTIKENILFGNELSNyfydqvVGSCQLKTDFRH------FQQGENTMVGEngitLSGGQK 698
Cdd:cd03255 77 aafrrrHIGFVFQsFNLLPDLTALENVELPLLLAG------VPKKERRERAEEllervgLGDRLNHYPSE----LSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 699 ARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS------KTRVLVTHNLQYTKYVDTIYVIEDGQI 771
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVME-------LLRElnkeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
565-791 |
2.09e-23 |
|
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: 106.83 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 565 GNAIVFKNASLNWKGpqNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSavldemvLL-------DGRVKVGG------ 631
Cdd:COG5265 355 GGEVRFENVSFGYDP--ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR-------LLfrfydvtSGRILIDGqdirdv 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 -------SIAYVPQHSWIFNKTIKENILFGNELSNYfyDQVVGSCQLK--TDF-RHFQQGENTMVGENGITLSGGQKARI 701
Cdd:COG5265 426 tqaslraAIGIVPQDTVLFNDTIAYNIAYGRPDASE--EEVEAAARAAqiHDFiESLPDGYDTRVGERGLKLSGGEKQRV 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 702 SLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDIA 781
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAAL---REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
250
....*....|
gi 392896924 782 YVDGPFGRLW 791
Cdd:COG5265 581 AQGGLYAQMW 590
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
568-754 |
2.41e-23 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 99.85 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQNP-PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDE----MVLLDGRVKVGGS--IAYVPQ 638
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIagLERptsgEVLVDGEPVTGPGpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 639 HS----WifnKTIKENILFGNELsnyfydQVVGSCQLKTDFRHFQQgentMVGENGI------TLSGGQKARISLARAVY 708
Cdd:cd03293 81 QDallpW---LTVLDNVALGLEL------QGVPKAEARERAEELLE----LVGLSGFenayphQLSGGMRQRVALARALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDKVIgpdGLLRS--KTRVLVTHNL 754
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELL---DIWREtgKTVLLVTHDI 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
568-1452 |
5.45e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.04 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS--------------I 633
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 634 AYVPQHSWIFNKTIKENILFG--------------NELSNYFYD--QVVGSC---------------------QLKTDFR 676
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGNDSQEnkNKRNSCrakcagdlndmsnttdsneliEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 677 HFQQGE---------------------NTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDaHVGRALFDKV 735
Cdd:PTZ00265 543 TIKDSEvvdvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKT 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 736 IGPDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQiVQHGSFEDIAYVDGPFGRLWSECENSDEDVADEEAESSEASVTP 815
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE-RGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNA 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 816 PVPVLENG--------------------------------DNGAIEKSS---------QIDRTNS---HFSEKSRKSEEK 851
Cdd:PTZ00265 701 GSYIIEQGthdalmknkngiyytminnqkvsskkssnndnDKDSDMKSSaykdsergyDPDEMNGnskHENESASNKKSC 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 852 PQKVEKNVENVQLGRV----------KKSVYQLYIKTMGIFNSSAFLIffIAHFTVMIMRSLWlsdwsnenaaikkaTLS 921
Cdd:PTZ00265 781 KMSDENASENNAGGKLpflrnlfkrkPKAPNNLRIVYREIFSYKKDVT--IIALSILVAGGLY--------------PVF 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 922 SVDYLNSTSSVDGPVSVETRLIVYAgfggLEMLLLALAFTVLTigSLRASYG----------LHSPLIHALLVAPISFFD 991
Cdd:PTZ00265 845 ALLYAKYVSTLFDFANLEANSNKYS----LYILVIAIAMFISE--TLKNYYNnvigekvektMKRRLFENILYQEISFFD 918
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 992 T---TPtGRIINRLSRDLDVIDK-LQDNIRMCTQTLlnacmILVLISISTPIFL--VCAAPLILIYYFVMIYYIPTSR-- 1063
Cdd:PTZ00265 919 QdkhAP-GLLSAHINRDVHLLKTgLVNNIVIFTHFI-----VLFLVSMVMSFYFcpIVAAVLTGTYFIFMRVFAIRARlt 992
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1064 -----QLKRLESANRSPILST-----------IAESIHGASSI--------------RAFD---KTERTTTALSTNVDKF 1110
Cdd:PTZ00265 993 ankdvEKKEINQPGTVFAYNSddeifkdpsflIQEAFYNMNTViiygledyfcnlieKAIDysnKGQKRKTLVNSMLWGF 1072
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1111 AQCRYLSHMS-NRWLATRLELLGNTCV--LFASLSATLST-KYFGLTPGMAGLSVSYALTITEVLNICVRsvseiESNIv 1186
Cdd:PTZ00265 1073 SQSAQLFINSfAYWFGSFLIRRGTILVddFMKSLFTFLFTgSYAGKLMSLKGDSENAKLSFEKYYPLIIR-----KSNI- 1146
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1187 svervneyqKLEPEAPWRIEKSLEneekwpVKGKIELDGFSMRY--RKNLPlVLKNIDLKIEGGERIGVIGRTGSGKS-- 1262
Cdd:PTZ00265 1147 ---------DVRDNGGIRIKNKND------IKGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKStv 1210
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1263 -SLTMALY---------------------RMIEGE------------------------------SGTIKIDDVEIDTIG 1290
Cdd:PTZ00265 1211 mSLLMRFYdlkndhhivfknehtndmtneQDYQGDeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYN 1290
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1291 LHQLRSKLIIIPQEPVVFSGTLRFNLDpFNQySDDQIWNCLEICQ---LKQFAQEDDKTLDRYIAEGGKNMSVGERQLLC 1367
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIK-FGK-EDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1368 LCRALLRGARIVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAHRLDTIVDSDRIVVL-DAGRVAEF----DTPS 1440
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFnNPDRTGSFvqahGTHE 1448
|
1130
....*....|..
gi 392896924 1441 NLLLNPDSLYSQ 1452
Cdd:PTZ00265 1449 ELLSVQDGVYKK 1460
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1221-1449 |
6.45e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 104.60 E-value: 6.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGE---SGTIKIDDVEIDTIGLHQLRSK 1297
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1298 LIIIPQEPVVfsgtlrfNLDPFNqySDDQIWNCLEICQLKQFAQED-----------DKTLDRYIAEggknMSVGERQLL 1366
Cdd:COG1123 85 IGMVFQDPMT-------QLNPVT--VGDQIAEALENLGLSRAEARArvlelleavglERRLDRYPHQ----LSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1367 CLCRALLRGARIVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLL 1443
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
....*.
gi 392896924 1444 LNPDSL 1449
Cdd:COG1123 232 AAPQAL 237
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
581-771 |
1.94e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.81 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 581 QNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAYVPQHSWIFNKTI 647
Cdd:COG4619 11 GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 648 KENILFGNELSNYFYDQVvgscQLKTDFRHFQQGENTM---VGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVD 724
Cdd:COG4619 91 RDNLPFPFQLRERKFDRE----RALELLERLGLPPDILdkpVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392896924 725 AHVGRALFDKVigpDGLLRSKTR--VLVTHNL-QYTKYVDTIYVIEDGQI 771
Cdd:COG4619 163 PENTRRVEELL---REYLAEEGRavLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
567-754 |
2.60e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.24 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWKGPQNP-PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDE----MVLLDGRV--KVGGSIAYVP 637
Cdd:COG1116 7 ALELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIagLEKptsgEVLVDGKPvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 638 QHS----WifnKTIKENILFGNELSNYFYDQV----------VGscqLkTDFRH---FQqgentmvgengitLSGGQKAR 700
Cdd:COG1116 87 QEPallpW---LTVLDNVALGLELRGVPKAERrerarellelVG---L-AGFEDaypHQ-------------LSGGMRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 701 ISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIgpdGLLRS--KTRVLVTHNL 754
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELL---RLWQEtgKTVLFVTHDV 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
569-770 |
4.57e-22 |
|
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: 96.00 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 569 VFKNASLNWKGpQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAY 635
Cdd:cd03225 1 ELKNLSFSYPD-GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 636 VPQH--SWIFNKTIKENILFGneLSNYFYD-----QVVGSCQLKTDFRHFQQgentmvgENGITLSGGQKARISLARAVY 708
Cdd:cd03225 80 VFQNpdDQFFGPTVEEEVAFG--LENLGLPeeeieERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDKVIGpdglLRS--KTRVLVTHNLQYTK-YVDTIYVIEDGQ 770
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK----LKAegKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1222-1432 |
7.74e-22 |
|
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: 95.23 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIII 1301
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1302 PQEP------------VVFSgtLRfNLdpfnQYSDDQIW----NCLEICQLKQFaqeddktLDRYIAEggknMSVGERQL 1365
Cdd:cd03225 81 FQNPddqffgptveeeVAFG--LE-NL----GLPEEEIEerveEALELVGLEGL-------RDRSPFT----LSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 1366 LCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQ-HFPQSTTISIAHRLDTIVD-SDRIVVLDAGR 1432
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1222-1432 |
1.22e-21 |
|
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: 93.08 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIII 1301
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1302 PQepvvfsgtlrfnldpfnqysddqiwncleicqlkqfaqeddktldryiaeggknMSVGERQLLCLCRALLRGARIVIL 1381
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1382 DEATASVDTVTDGIVQRAIRQHFPQ-STTISIAHRLDTIVD-SDRIVVLDAGR 1432
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
579-775 |
1.30e-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: 93.65 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 579 GPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS-------------IAYVPQhswifnk 645
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 tikenILfgnelsnyfydQVVGSCQLKtdFRHFQqgentmvgengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:cd03214 81 -----AL-----------ELLGLAHLA--DRPFN------------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 726 HVGRALFDkvigpdgLLRS------KTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHG 775
Cdd:cd03214 131 AHQIELLE-------LLRRlarergKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1221-1454 |
1.77e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 99.98 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRY---RKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIG---LHQL 1294
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1295 RSKLIIIPQEPV--------VFSgTLRFNLDPFNQYSDDQIWNC----LEICQLkqfaqeDDKTLDRYIAEggknMSVGE 1362
Cdd:COG1123 341 RRRVQMVFQDPYsslnprmtVGD-IIAEPLRLHGLLSRAERRERvaelLERVGL------PPDLADRYPHE----LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1363 RQllclcrallrgaRI------------VILDEATASVD-TVTDGIVQ--RAIRQHFpQSTTISIAHRLDTIVD-SDRIV 1426
Cdd:COG1123 410 RQ------------RVaiaralalepklLILDEPTSALDvSVQAQILNllRDLQREL-GLTYLFISHDLAVVRYiADRVA 476
|
250 260
....*....|....*....|....*...
gi 392896924 1427 VLDAGRVAEFDTPSNLLLNPDSLYSQLL 1454
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFANPQHPYTRAL 504
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
273-547 |
3.22e-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: 92.61 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 273 PILLKQLIDYVsLHDQPLSFGIAIACIMFSCSTTRSLLQNYQ--IAGMCRQAVYYQtvLSNAILHKILRLSPSARSNRTA 350
Cdd:cd07346 19 PLLTKLLIDDV-IPAGDLSLLLWIALLLLLLALLRALLSYLRryLAARLGQRVVFD--LRRDLFRHLQRLSLSFFDRNRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 351 GEILNHAAVDIEII---VHSVpyLQNMWSVPFQVTLAMTMLaITLGWA-AMAGVCIMILFIPLNLCTSRFIKLSQQKQMK 426
Cdd:cd07346 96 GDLMSRLTSDVDAVqnlVSSG--LLQLLSDVLTLIGALVIL-FYLNWKlTLVALLLLPLYVLILRYFRRRIRKASREVRE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 427 IKDERTKLSNEMLNGIKVVKLYAWEES----FEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFLV-AIGSFTcyVLw 501
Cdd:cd07346 173 SLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVlLYGGYL--VL- 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 392896924 502 spdENGLTPS--VAFVALTifNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd07346 250 ---QGSLTIGelVAFLAYL--GMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
568-776 |
4.46e-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: 90.16 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIA 634
Cdd:cd03369 7 IEVENLSVRY-APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQHSWIFNKTIKENILFGNELSNyfyDQVVGSCQlktdfrhfqqgentmVGENGITLSGGQKARISLARAVYQDKDIY 714
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLDPFDEYSD---EEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 715 LLDDPLSAVDAHVGrALFDKVIgpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGS 776
Cdd:cd03369 148 VLDEATASIDYATD-ALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1445 |
8.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.82 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPvvfsgtlrfnlDpfNQY----SDDQIWNCLEICQLKQfaQEDDKTLDRYIAEGG---------KNMSVGERQLLC 1367
Cdd:PRK13632 88 IFQNP-----------D--NQFigatVEDDIAFGLENKKVPP--KKMKDIIDDLAKKVGmedyldkepQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1368 LCRALLRGARIVILDEATASVD-----TVTDGIVQraIRQHfPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNL 1442
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDpkgkrEIKKIMVD--LRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
...
gi 392896924 1443 LLN 1445
Cdd:PRK13632 230 LNN 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
581-770 |
9.50e-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: 87.69 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 581 QNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGsiayvPQHSWIFNKTIKENILFGnelsny 660
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-----KDIAKLPLEELRRRIGYV------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 661 fydqvvgscqlktdfrhFQqgentmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIgpDG 740
Cdd:cd00267 79 -----------------PQ-------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR--EL 126
|
170 180 190
....*....|....*....|....*....|.
gi 392896924 741 LLRSKTRVLVTHNLQYT-KYVDTIYVIEDGQ 770
Cdd:cd00267 127 AEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
584-780 |
1.14e-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: 90.10 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAYVPQHSWI-FNKTIKE 649
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPApFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGnelsnyfydqvvgscqlktdfRHFQQGENTMVGEN------------GI---------TLSGGQKARISLARAVY 708
Cdd:COG1120 95 LVALG---------------------RYPHLGLFGRPSAEdreaveealertGLehladrpvdELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 709 QDKDIYLLDDPLSAVD-AHVGRALfdkvigpdGLLRSKTR------VLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlAHQLEVL--------ELLRRLARergrtvVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
568-780 |
1.52e-19 |
|
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: 89.31 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVldeMVLL---DGRVKVGG------------- 631
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL---NGLLkptSGEVLVDGkditkknlrelrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 SIAYVPQHSW--IFNKTIKENILFGneLSNYFY---------DQVVGSCQLkTDFRHfqqgENTMvgengiTLSGGQKAR 700
Cdd:COG1122 76 KVGLVFQNPDdqLFAPTVEEDVAFG--PENLGLpreeirervEEALELVGL-EHLAD----RPPH------ELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 701 ISLARAVYQDKDIYLLDDPLSAVDAHvGRALFDKVIgpDGLLRS-KTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFE 778
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPR-GRRELLELL--KRLNKEgKTVIIVTHDLDLvAELADRVIVLDDGRIVADGTPR 219
|
..
gi 392896924 779 DI 780
Cdd:COG1122 220 EV 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
575-772 |
2.48e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 87.70 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 575 LNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSL---LSAVLDEMvllDGRVKVGG----------SIAYVPQHS- 640
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLakiLAGLIKES---SGSILLNGkpikakerrkSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 641 -WIFNKTIKENILFGNELSNYFYDQVvgSCQLKTdfrhfqQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:cd03226 82 yQLFTDSVREELLLGLKELDAGNEQA--ETVLKD------LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 720 LSAVDAH----VGRaLFDKVIGpdgllRSKTRVLVTHNLQY-TKYVDTIYVIEDGQIV 772
Cdd:cd03226 154 TSGLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFlAKVCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
584-789 |
3.45e-19 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 88.33 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS----------------IAYVPQHSWIFN-KT 646
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDsLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFG-NELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:cd03261 94 VFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE----LSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 726 hVGRALFDKVIgpdglLRSK-----TRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDIAYVDGPFGR 789
Cdd:cd03261 170 -IASGVIDDLI-----RSLKkelglTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASDDPLVR 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1218-1446 |
4.37e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.85 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1218 KGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSK 1297
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1298 LIIIPQEPVVFSGTLRFNLDPFNQYSDDQiwnclEICQLKQFAQEDDKTL------DRYIAEGGKNMSVGERQLLCLCRA 1371
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALGRPDATQQ-----EIEHVARLASVHDDILrlpqgyDTEVGERGVMLSGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1372 LLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNP 1446
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
568-780 |
4.43e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.13 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQnpPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSaVLDEMVLLD-GRVKVGG-------------SI 633
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLIEPTsGEIFIDGedireqdpvelrrKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 634 AYVPQHSWIF-NKTIKENILFGNELSNYF-------YDQVVGSCQLK-TDFRHFQQGEntmvgengitLSGGQKARISLA 704
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIALVPKLLKWPkekirerADELLALVGLDpAEFADRYPHE----------LSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 705 RAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPDGLLRsKTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELG-KTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1221-1454 |
5.45e-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: 87.94 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNL--PLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKL 1298
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPvvfSGTL--RFNLD-----PFN----QYSDDQIWNCLEICQLkqfaqeDDKTLDRYIAEggknMSVGERQLLC 1367
Cdd:COG1124 82 QMVFQDP---YASLhpRHTVDrilaePLRihglPDREERIAELLEQVGL------PPSFLDRYPHQ----LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1368 LcrallrgAR-------IVILDEATASVDTVT-DGIV---QRAIRQHfpQSTTISIAHRLDtIVD--SDRIVVLDAGRVA 1434
Cdd:COG1124 149 I-------ARalilepeLLLLDEPTSALDVSVqAEILnllKDLREER--GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIV 218
|
250 260
....*....|....*....|
gi 392896924 1435 EFDTPSNLLLNPDSLYSQLL 1454
Cdd:COG1124 219 EELTVADLLAGPKHPYTREL 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1221-1436 |
7.87e-19 |
|
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: 87.18 E-value: 7.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRY--RKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQL---R 1295
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1296 SKLIIIPQEPvvFSgtlrfNLDP------------FNQYSDDQIWNCLEICQLKQFAQEDDKT-LDRYIAEggknMSVGE 1362
Cdd:cd03257 82 KEIQMVFQDP--MS-----SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1363 RQLLCLCRALLRGARIVILDEATASVDTVT-DGIVQ--RAIRQHFpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEF 1436
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
584-780 |
8.02e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.82 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDE----MVLLDGRV----------KVGgsiaYVPQHSWIF-NKT 646
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagLETpdsgRIVLNGRDlftnlpprerRVG----FVFQHYALFpHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFG---NELSNYFYDQVVgSCQLKtdfrhfqqgentMVGENGI------TLSGGQKARISLARAVYQDKDIYLLD 717
Cdd:COG1118 92 VAENIAFGlrvRPPSKAEIRARV-EELLE------------LVQLEGLadrypsQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 718 DPLSAVDAHVG-------RALFDKVIGpdgllrskTRVLVTHNLQ--YTkYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG1118 159 EPFGALDAKVRkelrrwlRRLHDELGG--------TTVFVTHDQEeaLE-LADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1221-1446 |
9.02e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 87.36 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVlKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSG-TLRFN--LDP-FNQYSDDQI----WNCLEICQLkqfaqEDDKTLDRYIAEggknMSVGERQLLCLCRAL 1372
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIreraDELLALVGL-----DPAEFADRYPHE----LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1373 LRGARIVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAHRLD-TIVDSDRIVVLDAGRVAEFDTPSNLLLNP 1446
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1221-1456 |
1.07e-18 |
|
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: 86.85 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYrKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIG---LHQLRSK 1297
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1298 -------LIIIPQEPV---VFSGtlRFNLDP-----FNQYSDDQIWNCLEIcqLKQFAqeddktLDRYIAEGGKNMSVGE 1362
Cdd:cd03256 80 igmifqqFNLIERLSVlenVLSG--RLGRRStwrslFGLFPKEEKQRALAA--LERVG------LLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1363 RQLLCLCRALLRGARIVILDEATASVDTVTDGIVQ---RAIRQHFPQSTTISIaHRLDTIVD-SDRIVVLDAGRVAeFDT 1438
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMdllKRINREEGITVIVSL-HQVDLAREyADRIVGLKDGRIV-FDG 227
|
250
....*....|....*...
gi 392896924 1439 PsnlllnPDSLYSQLLNE 1456
Cdd:cd03256 228 P------PAELTDEVLDE 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
584-780 |
1.09e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 87.04 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDemvLLD---GRVKVGG------------SIAYVPQHSWIFNK-TI 647
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG---LLRptsGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 648 KENILF--------GNELSNYFyDQVVGSCQLkTDFRHfqqgenTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:COG1131 91 RENLRFfarlyglpRKEARERI-DELLELFGL-TDAAD------RKVG----TLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 720 LSAVDAHVGRALFDkvigpdgLLRS-----KTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG1131 159 TSGLDPEARRELWE-------LLRElaaegKTVLLSTHYLEEaERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1235-1432 |
1.34e-18 |
|
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: 85.60 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1235 PLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIkiddveidtiglhQLRSKLIIIPQEPVVFSGTLRF 1314
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQEPWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NL---DPFNQYSDDQIwncLEICQLKQ-FAQ--EDDKTLdryIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASV 1388
Cdd:cd03250 85 NIlfgKPFDEERYEKV---IKACALEPdLEIlpDGDLTE---IGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 392896924 1389 DT-VTDGIVQRAIRQHFPQS-TTISIAHRLDTIVDSDRIVVLDAGR 1432
Cdd:cd03250 159 DAhVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
581-780 |
2.35e-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: 86.06 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 581 QNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEM------VLLDGRVKVGGS------IAYVPQ--HSWiFNKT 646
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkpdsgsILIDGEDVRKEPrearrqIGVLPDerGLY-DRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELS-------NYFYDQVVGSCQLkTDFRHFQQGEntmvgengitLSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:COG4555 91 VRENIRYFAELYglfdeelKKRIEELIELLGL-EEFLDRRVGE----------LSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 720 LSAVDAHVGRALFDkvigpdgLLRS-----KTRVLVTHNLQ-YTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG4555 160 TNGLDVMARRLLRE-------ILRAlkkegKTVLFSSHIMQeVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1222-1433 |
2.83e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 84.02 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIII 1301
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1302 PQepvvfsgtlrfnldpfnqysddqiwnCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLCLCRALLRGARIVIL 1381
Cdd:cd03214 79 PQ--------------------------ALELLGLAHLA-------DRPFNE----LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1382 DEATASVD-----TVTDgIVQRAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRV 1433
Cdd:cd03214 122 DEPTSHLDiahqiELLE-LLRRLARER--GKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
566-772 |
3.04e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.48 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 566 NAIVFKNASLNWK-GPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAvldeMVLLD----GRVKVGG--------- 631
Cdd:COG1136 3 PLLELRNLTKSYGtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNI----LGGLDrptsGEVLIDGqdisslser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 --------SIAYVPQHswiFN----KTIKENILFGNELSNYFYDQV----------VGscqLkTDFRHFQQGEntmvgen 689
Cdd:COG1136 79 elarlrrrHIGFVFQF---FNllpeLTALENVALPLLLAGVSRKERrerarellerVG---L-GDRLDHRPSQ------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 690 gitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS------KTRVLVTHNLQYTKYVDTI 763
Cdd:COG1136 145 ---LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRElnrelgTTIVMVTHDPELAARADRV 214
|
....*....
gi 392896924 764 YVIEDGQIV 772
Cdd:COG1136 215 IRLRDGRIV 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
585-780 |
9.57e-18 |
|
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: 83.77 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSaVLDEMVLLDGRVKVGGSIAY---------------------VPQHSWIF 643
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLR-LLNRLNDLIPGAPDEGEVLLdgkdiydldvdvlelrrrvgmVFQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENILFG----NELSNYFYDQVVGSCQLKTDFrhfqqGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:cd03260 94 PGSIYDNVAYGlrlhGIKLKEELDERVEEALRKAAL-----WDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 720 LSAVDAhVGRALFDKVIgpDGLLRSKTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:cd03260 169 TSALDP-ISTAKIEELI--AELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
537-811 |
1.38e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.24 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 537 LVQARVSNKRLRQfLNDEEMER---KTEVALGNAIVFKNASLNWKGPQnpPVLKDLSATIKPGQLIAIVGSVGGGKSSLL 613
Cdd:PRK10790 308 LQQAVVAGERVFE-LMDGPRQQygnDDRPLQSGRIDIDNVSFAYRDDN--LVLQNINLSVPSRGFVALVGHTGSGKSTLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 614 SAVLDEMVLLDGRVKVGG-------------SIAYVPQHSWIFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQ 680
Cdd:PRK10790 385 SLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 681 GENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA----HVGRALfdkvigpdGLLRSKTR-VLVTHNLQ 755
Cdd:PRK10790 465 GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSgteqAIQQAL--------AAVREHTTlVVIAHRLS 536
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 756 YTKYVDTIYVIEDGQIVQHGSFEDIAYVDGPFGRLWSECENSDEDVADEEAESSEA 811
Cdd:PRK10790 537 TIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1221-1446 |
1.66e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.27 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEI-DTIGLHQLRSKLI 1299
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 IIPQEP-VVFSG-TLRFNL--DPFNQysddqiwnCLEICQLKqfaqeddKTLDRYIAEGG---------KNMSVGERQLL 1366
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLafGPENL--------CLPPIEIR-------KRVDRALAEIGlekyrhrspKTLSGGQGQCV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1367 CLCRALLRGARIVILDEATASVDTVT-DGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLN 1445
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
.
gi 392896924 1446 P 1446
Cdd:PRK13644 226 V 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1221-1449 |
2.25e-17 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 83.55 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVV-FSGTL-------RFN-LDPFNQYSDD---QIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLCL 1368
Cdd:COG1120 80 VPQEPPApFGLTVrelvalgRYPhLGLFGRPSAEdreAVEEALERTGLEHLA-------DRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1369 crallrgAR-------IVILDEATASVD-----TVTDgIVQRAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAE 1435
Cdd:COG1120 149 -------ARalaqeppLLLLDEPTSHLDlahqlEVLE-LLRRLARER--GRTVVMVLHDLNLAARyADRLVLLKDGRIVA 218
|
250
....*....|....
gi 392896924 1436 FDTPSNlLLNPDSL 1449
Cdd:COG1120 219 QGPPEE-VLTPELL 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
585-770 |
2.79e-17 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 81.08 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDE----MVLLDGRVKVGG---------SIAYVPQHSWIF-NKTIK 648
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIagLEEpdsgSILIDGEDLTDLedelpplrrRIGMVFQDFALFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENILFGnelsnyfydqvvgscqlktdfrhfqqgentmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVG 728
Cdd:cd03229 95 ENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 392896924 729 RALFDkvigpdgLLRS------KTRVLVTHNLQYTKYV-DTIYVIEDGQ 770
Cdd:cd03229 137 REVRA-------LLKSlqaqlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
584-754 |
3.17e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG--SIAYVPQHS---WIFNKTIKENILFG---- 654
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVAMGrwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 655 -NELSNYFYD--QVVGSCQLK---TDFRHFQQGEntmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVG 728
Cdd:NF040873 86 rGLWRRLTRDdrAAVDDALERvglADLAGRQLGE----------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|.
gi 392896924 729 RALFDkvigpdgLL-----RSKTRVLVTHNL 754
Cdd:NF040873 156 ERIIA-------LLaeehaRGATVVVVTHDL 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
578-780 |
4.29e-17 |
|
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: 86.50 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 578 KGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDemvLLD---GRVKVGG----------------SIAYVPQ 638
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG---LLRptsGSILFDGkdltklsrrslrelrrRVQMVFQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 639 ---HSwiFN--KTIKENILFGneLSNYFY----------DQVVGSCQLKTDFRH---FQqgentmvgengitLSGGQKAR 700
Cdd:COG1123 350 dpySS--LNprMTVGDIIAEP--LRLHGLlsraerrervAELLERVGLPPDLADrypHE-------------LSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 701 ISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS------KTRVLVTHNLQYTKYV-DTIYVIEDGQIVQ 773
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILN-------LLRDlqrelgLTYLFISHDLAVVRYIaDRVAVMYDGRIVE 485
|
....*..
gi 392896924 774 HGSFEDI 780
Cdd:COG1123 486 DGPTEEV 492
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1220-1440 |
4.68e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.14 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1220 KIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLI 1299
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 IIPQEP-VVFSGT-----LRFNLDPfNQYSDDQ----IWNCLEICQLKQFAQEDDKTLdryiaeggknmSVGERQLLCLC 1369
Cdd:PRK13635 85 MVFQNPdNQFVGAtvqddVAFGLEN-IGVPREEmverVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1370 RALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQS--TTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPS 1440
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1221-1446 |
4.95e-17 |
|
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: 81.86 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRY--RKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEG----ESGTIKIDDVEIDTI---GL 1291
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLI----RCINGlerpTSGSVLVDGTDLTLLsgkEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1292 HQLRSKLIIIPQEPVVFSG-TLRFNLD-PF------NQYSDDQIWNCLEICQLKQFAqeddktlDRYIAeggkNMSVGER 1363
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKA-------DAYPA----QLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1364 QLLCLCRALLRGARIVILDEATASVD-TVTDGIVQ--RAIRQHFpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTP 1439
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDpETTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*..
gi 392896924 1440 SNLLLNP 1446
Cdd:cd03258 226 EEVFANP 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
595-775 |
5.17e-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: 81.57 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 595 PGQLIAIVGSVGGGKSSLLSA------------VLDEMVLLDGRVKVGGS-----IAYVPQHSWIF-NKTIKENILFG-- 654
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCiaglekpdggtiVLNGTVLFDSRKKINLPpqqrkIGLVFQQYALFpHLNVRENLAFGlk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 655 ---NELSNYFYDQVVGSCQL-KTDFRHFQQgentmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRA 730
Cdd:cd03297 102 rkrNREDRISVDELLDLLGLdHLLNRYPAQ------------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 731 LFdkvigpdGLLRS-KTR-----VLVTHNLQYTKYV-DTIYVIEDGQIVQHG 775
Cdd:cd03297 170 LL-------PELKQiKKNlnipvIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1221-1440 |
7.18e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 81.46 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGE-----SGTIKIDDVEIDTIGLH--Q 1293
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1294 LRSKLIIIPQEPVVFSGTLRFNLD--------PFNQYSDDQIWNCLEICQLkqfaqeDDKTLDRYIAEGgknMSVGERQL 1365
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAAL------WDEVKDRLHALG---LSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1366 LCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQhFPQSTTISI-------AHRLdtivdSDRIVVLDAGRVAEFDT 1438
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIvthnmqqAARV-----ADRTAFLLNGRLVEFGP 223
|
..
gi 392896924 1439 PS 1440
Cdd:cd03260 224 TE 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1221-1442 |
7.89e-17 |
|
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: 81.39 E-value: 7.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDT---IGLHQLRSK 1297
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1298 LIIIPQEPVVFSG-TLR----FNLDPFNQYSDDQIWN----CLEICQLKQFAqeddktlDRYIAE--GGKNMSVGErqll 1366
Cdd:cd03261 79 MGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEIREivleKLEAVGLRGAE-------DLYPAElsGGMKKRVAL---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1367 clcrallrgAR-------IVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEF 1436
Cdd:cd03261 148 ---------ARalaldpeLLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAE 218
|
....*.
gi 392896924 1437 DTPSNL 1442
Cdd:cd03261 219 GTPEEL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
579-780 |
9.09e-17 |
|
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: 81.09 E-value: 9.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 579 GPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV-LDEM-----VLLDGR--VKVGGS--------IAYVPQHswi 642
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInGLERptsgsVLVDGTdlTLLSGKelrkarrrIGMIFQH--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 643 FN----KTIKENILFGNELSNYFYDQV----------VGScqlkTDFRHFQQGEntmvgengitLSGGQKARISLARAVY 708
Cdd:cd03258 91 FNllssRTVFENVALPLEIAGVPKAEIeervlellelVGL----EDKADAYPAQ----------LSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRSKTR------VLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILA-------LLRDINRelgltiVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
584-780 |
1.06e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.58 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEM----VLLDGRVkVGG------SIAYVPQhSWIF--NKTIKE 649
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLEDPtsgeILIGGRD-VTDlppkdrNIAMVFQ-SYALypHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGnelsnyfydqvvgscqLKtdFRHFQQGE-NTMVGEN----GIT---------LSGGQKARISLARAVYQDKDIYL 715
Cdd:COG3839 95 NIAFP----------------LK--LRKVPKAEiDRRVREAaellGLEdlldrkpkqLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 716 LDDPLSAVDAHvgralfdkvigpdglLRSKTR--------------VLVTHNlqytkYV------DTIYVIEDGQIVQHG 775
Cdd:COG3839 157 LDEPLSNLDAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVMNDGRIQQVG 216
|
....*
gi 392896924 776 SFEDI 780
Cdd:COG3839 217 TPEEL 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1237-1436 |
1.22e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLtmalYRMIEG----ESGTIKIDDVEidtiglhqlrsKLIIIPQEPVVFSGTL 1312
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTL----LRAIAGlwpyGSGRIARPAGA-----------RVLFLPQRPYLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1313 RFNL---DPFNQYSDDQIWNCLEICQLKQFAQEDDKTLDRyiaegGKNMSVGERQLLCLcrallrgARI-------VILD 1382
Cdd:COG4178 443 REALlypATAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQQRLAF-------ARLllhkpdwLFLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 392896924 1383 EATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEF 1436
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
584-780 |
1.61e-16 |
|
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: 84.57 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV---LDEMVLLDGRVKVGG-------------SIAYVPQH--SWIFNK 645
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALmglLPHGGRISGEVLLDGrdllelsealrgrRIGMVFQDpmTQLNPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 TIKENILFGNELSNYFYDQV----------VGSCQLKTDFRHfqqgentmvgengiTLSGGQKARISLARAVYQDKDIYL 715
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEArarvlelleaVGLERRLDRYPH--------------QLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 716 LDDPLSAVDAHVGRALFDkvigpdgLLRSKTR------VLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG1123 166 ADEPTTALDVTTQAEILD-------LLRELQRergttvLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
584-771 |
1.73e-16 |
|
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: 78.59 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------SIAYVPQHswifnktikeni 651
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEE------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 lfgnelsNYFYdqvvgscqlktdfrhfqqgENTMVGENgITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAhVGRAL 731
Cdd:cd03230 82 -------PSLY-------------------ENLTVREN-LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392896924 732 FDKVIgpDGLLRS-KTRVLVTHNLQ-YTKYVDTIYVIEDGQI 771
Cdd:cd03230 134 FWELL--RELKKEgKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
578-781 |
3.09e-16 |
|
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: 79.85 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 578 KGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAvldeMVLLD----GRVKVGGS-------------IAYVPQHS 640
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRA----LAGLErpwsGEVTFDGRpvtrrrrkafrrrVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 641 W-IFN--KTIKENILfgnE-LSNYFYDQV----------VGscqLKTDFR----HfqqgentmvgengiTLSGGQKARIS 702
Cdd:COG1124 89 YaSLHprHTVDRILA---EpLRIHGLPDReeriaelleqVG---LPPSFLdrypH--------------QLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 703 LARAVYQDKDIYLLDDPLSAVDAHVgRA----LFDKVIGPDGLlrskTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSF 777
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSV-QAeilnLLKDLREERGL----TYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTV 223
|
....
gi 392896924 778 EDIA 781
Cdd:COG1124 224 ADLL 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1218-1436 |
3.13e-16 |
|
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: 84.03 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1218 KGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEG----ESGTIKIDDVEIDTIGLHQ 1293
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLVGvwppTAGSVRLDGADLSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1294 LRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQIwncLE----------ICQLKQfaqeddkTLDRYIAEGGKNMSVGER 1363
Cdd:COG4618 404 LGRHIGYLPQDVELFDGTIAENIARFGDADPEKV---VAaaklagvhemILRLPD-------GYDTRIGEGGARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1364 QLLclcrallrG-AR-------IVILDEATASVDTVTDGIVQRAI---RQHfpQSTTISIAHRLDTIVDSDRIVVLDAGR 1432
Cdd:COG4618 474 QRI--------GlARalygdprLVVLDEPNSNLDDEGEAALAAAIralKAR--GATVVVITHRPSLLAAVDKLLVLRDGR 543
|
....
gi 392896924 1433 VAEF 1436
Cdd:COG4618 544 VQAF 547
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
584-775 |
3.33e-16 |
|
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: 79.47 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKV----------------GGSIAYVPQHS------- 640
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsrrlrkirRKEIQMVFQDPmsslnpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 641 -----------WIFNKTIKENILfgNELSNYFYDQVVGSCQLKTDFRHfqqgentmvgengiTLSGGQKARISLARAVYQ 709
Cdd:cd03257 99 mtigeqiaeplRIHGKLSKKEAR--KEAVLLLLVGVGLPEEVLNRYPH--------------ELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 710 DKDIYLLDDPLSAVDAHVgRA----LFDKvigpdglLRSK---TRVLVTHNLQYTKYV-DTIYVIEDGQIVQHG 775
Cdd:cd03257 163 NPKLLIADEPTSALDVSV-QAqildLLKK-------LQEElglTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
584-780 |
5.60e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.30 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEmvLLDGRVKVGG-----------SIAYVPQHSWIF-NKTIKE 649
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFET--PDSGRILLDGrdvtglppekrNVGMVFQDYALFpHLTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGneLSNYFY---------DQVVGSCQLkTDFrhfqqgENTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPL 720
Cdd:COG3842 97 NVAFG--LRMRGVpkaeirarvAELLELVGL-EGL------ADRYPHQ----LSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 721 SAVDAHvgralfdkvigpdglLRSKTR--------------VLVTHNLQ--YTkYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG3842 164 SALDAK---------------LREEMReelrrlqrelgitfIYVTHDQEeaLA-LADRIAVMNDGRIEQVGTPEEI 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
584-787 |
6.85e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 78.87 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAvldeMVLL----DGRVKVGG----------------SIAYVPQHSWIF 643
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKL----IIGLlrpdSGEILVDGqditglsekelyelrrRIGMLFQGGALF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 -NKTIKENILFG-NELSNYFYDQV----------VGscqlktdFRHFqqgENTMVGEngitLSGGQKARISLARAVYQDK 711
Cdd:COG1127 95 dSLTVFENVAFPlREHTDLSEAEIrelvleklelVG-------LPGA---ADKMPSE----LSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 712 DIYLLDDPLSAVDAhVGRALFDKVIgpdgL-LRSK---TRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDIAYVDGP 786
Cdd:COG1127 161 EILLYDEPTAGLDP-ITSAVIDELI----ReLRDElglTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLASDDP 235
|
.
gi 392896924 787 F 787
Cdd:COG1127 236 W 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
567-780 |
9.08e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.54 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASlnwKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLS--AVLDEMVllDGRVKVGG-----------SI 633
Cdd:cd03296 2 SIEVRNVS---KRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRliAGLERPD--SGTILFGGedatdvpvqerNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 634 AYVPQHSWIF-NKTIKENILFGnelsnyfydqvvgscqLKTDFRHFQQGENT----------MVGENGIT------LSGG 696
Cdd:cd03296 77 GFVFQHYALFrHMTVFDNVAFG----------------LRVKPRSERPPEAEirakvhellkLVQLDWLAdrypaqLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 697 QKARISLARAVYQDKDIYLLDDPLSAVDAHVG-------RALFDKVigpdgllrSKTRVLVTHNLQYTKYV-DTIYVIED 768
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRkelrrwlRRLHDEL--------HVTTVFVTHDQEEALEVaDRVVVMNK 212
|
250
....*....|..
gi 392896924 769 GQIVQHGSFEDI 780
Cdd:cd03296 213 GRIEQVGTPDEV 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
568-780 |
1.25e-15 |
|
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: 77.99 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSaVLDEMVLLD-GRVKVGGS-------------- 632
Cdd:cd03256 1 IEVENLSKTY--PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLR-CLNGLVEPTsGSVLIDGTdinklkgkalrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 633 --IAYVPQHSWIFNK-TIKENILFG--------NELSNYFYD---QVVGSCQLKTDFRHFqqgENTMVGEngitLSGGQK 698
Cdd:cd03256 78 rqIGMIFQQFNLIERlSVLENVLSGrlgrrstwRSLFGLFPKeekQRALAALERVGLLDK---AYQRADQ----LSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 699 ARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRSKTR------VLVTHNLQY-TKYVDTIYVIEDGQI 771
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMD-------LLKRINReegitvIVSLHQVDLaREYADRIVGLKDGRI 223
|
....*....
gi 392896924 772 VQHGSFEDI 780
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
562-790 |
1.65e-15 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 78.03 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 562 VALGNAIVFKNASLNWKGPQNPpVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-SIAYVPQHS 640
Cdd:cd03288 14 VGLGGEIKIHDLCVRYENNLKP-VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 641 W------------IFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVY 708
Cdd:cd03288 93 LrsrlsiilqdpiLFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDKVIGPdglLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDI-AYVDGPF 787
Cdd:cd03288 173 RKSSILIMDEATASIDMATENILQKVVMTA---FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVF 249
|
...
gi 392896924 788 GRL 790
Cdd:cd03288 250 ASL 252
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
584-781 |
2.05e-15 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 77.20 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSL------LSAVLDEMVLLDG----------RVKVGgsIAYVPQHSWIFNK-T 646
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTfymivgLVKPDSGKILLDGqditklpmhkRARLG--IGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELSNYFYDQVVGSC-QLKTDFrHFQQGENTMvgenGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:cd03218 92 VEENILAVLEIRGLSKKEREEKLeELLEEF-HITHLRKSK----ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 726 -------HVGRALFDKVIGpdgllrsktrVLVT-HNLQYT-KYVDTIYVIEDGQIVQHGSFEDIA 781
Cdd:cd03218 167 iavqdiqKIIKILKDRGIG----------VLITdHNVRETlSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
538-779 |
2.63e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 538 VQARVsnKRLRQFLNDE--------EMERKTEVALGN-AIVFKNASlnwKGPQNPPVLKDLSATIKPGQLIAIVGSVGGG 608
Cdd:COG0488 279 AQSRI--KALEKLEREEpprrdktvEIRFPPPERLGKkVLELEGLS---KSYGDKTLLDDLSLRIDRGDRIGLIGPNGAG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 609 KSSLLSAVLDEMVLLDGRVKVGG--SIAYVPQHSWIF--NKTIKENIL-FGNELSNYFYDQVVGSCQLKTDfRHFQQgen 683
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKLGEtvKIGYFDQHQEELdpDKTVLDELRdGAPGGTEQEVRGYLGRFLFSGD-DAFKP--- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 684 tmVGengiTLSGGQKARISLARAVYQDKDIYLLDDP-----LSAVDahvgrALFDKVIGPDGllrskTRVLVTHN---LQ 755
Cdd:COG0488 430 --VG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLE-----ALEEALDDFPG-----TVLLVSHDryfLD 493
|
250 260
....*....|....*....|....*
gi 392896924 756 ytKYVDTIYVIEDGQIVQH-GSFED 779
Cdd:COG0488 494 --RVATRILEFEDGGVREYpGGYDD 516
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
585-726 |
2.73e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.54 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV---LDEMVLLDGRVKVGG----------SIAYVPQHS-WIFNKTIKEN 650
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 651 ILF------GNELSNYFYDQVVGSCQLKtdfrhfqQGENTMVGENGIT-LSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:cd03234 102 LTYtailrlPRKSSDAIRKKRVEDVLLR-------DLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
...
gi 392896924 724 DAH 726
Cdd:cd03234 175 DSF 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
567-778 |
3.63e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWKGPQNppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS----------IAYV 636
Cdd:PRK15056 6 GIVVNDVTVTWRNGHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 637 PQHS---WIFNKTIKENILFGN-------ELSNYFYDQVVGSCQLKTD---FRHFQQGEntmvgengitLSGGQKARISL 703
Cdd:PRK15056 84 PQSEevdWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDmveFRHRQIGE----------LSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 704 ARAVYQDKDIYLLDDPLSAVDAHVGRalfdKVIGPDGLLRS--KTRVLVTHNL-QYTKYVDTIYVIEdGQIVQHGSFE 778
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEA----RIISLLRELRDegKTMLVSTHNLgSVTEFCDYTVMVK-GTVLASGPTE 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
568-775 |
3.63e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 75.67 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQNP---PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--------LDEMVLLDGR----VKVGGS 632
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrrtglgVSGEVLINGRpldkRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 633 IAYVPQHSWIF-NKTIKENILFGNELSNyfydqvvgscqlktdfrhfqqgentmvgengitLSGGQKARISLARAVYQDK 711
Cdd:cd03213 84 IGYVPQDDILHpTLTVRETLMFAAKLRG---------------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 712 DIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS-----KTRVLVTHNLQYTKY--VDTIYVIEDGQIVQHG 775
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMS-------LLRRladtgRTIICSIHQPSSEIFelFDKLLLLSQGRVIYFG 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
577-775 |
5.81e-15 |
|
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: 75.37 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 577 WKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLS--AVLDEMVllDGRVKVGG-----------SIAYVPQHSWIF 643
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRmiAGLEEPT--SGRIYIGGrdvtdlppkdrDIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 -NKTIKENILFGNELSNYFYDQV---VGSCQLKTDFRHFQQGENTmvgengiTLSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:cd03301 85 pHMTVYDNIAFGLKLRKVPKDEIderVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 720 LSAVDAHVGRALFDKVIgpdGLLR--SKTRVLVTHN-LQYTKYVDTIYVIEDGQIVQHG 775
Cdd:cd03301 158 LSNLDAKLRVQMRAELK---RLQQrlGTTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
579-780 |
8.17e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 8.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 579 GPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAYVPQHSWIFNK 645
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 -TIKENILFGNELSNYFYDQVVGSCQLKTDfRHFQQGENTMVGENGIT-LSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:PRK11231 91 iTVRELVAYGRSPWLSLWGRLSAEDNARVN-QAMEQTRINHLADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 724 DAHVGRALFDkvigpdgLLR-----SKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK11231 170 DINHQVELMR-------LMRelntqGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
590-780 |
1.64e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 590 SATIKPGQLIAIVGSVGGGKSSLLSAV---LDEM---VLLDGRvkvggSIAYVPQH----SWIFNktikENILFgNELSN 659
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIagfLPPDsgrILWNGQ-----DLTALPPAerpvSMLFQ----ENNLF-PHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 660 YfydQVVG-----SCQLKTDFRhfQQGENTM--VGENGI------TLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA- 725
Cdd:COG3840 89 A---QNIGlglrpGLKLTAEQR--AQVEQALerVGLAGLldrlpgQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 726 --HVGRALFDKVIGPDGLlrskTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:COG3840 164 lrQEMLDLVDELCRERGL----TVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1221-1451 |
2.11e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.47 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPL---VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEI--DTIGLHQLR 1295
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1296 SKLIIIPQEP--VVFSGTLRFNLD--PFN-QYSDDQIWN----CLEICQLKQfaqedDKTLDRYIAEggknMSVGERQLL 1366
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAfgPINlGLSEEEIENrvkrAMNIVGLDY-----EDYKDKSPFE----LSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1367 CLCRALLRGARIVILDEATASVDTVT-DGIVQ--RAIRQHFpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNL 1442
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGrDEILNkiKELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
....*....
gi 392896924 1443 LLNPDSLYS 1451
Cdd:PRK13637 233 FKEVETLES 241
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
584-776 |
3.62e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 73.31 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------SIAYVPQHSWIFNK-TIKEN 650
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 651 ILFGNEL---SNYFYDQVVGSCQLKTDFRHFQqgeNTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHV 727
Cdd:cd03263 96 LRFYARLkglPKSEIKEEVELLLRVLGLTDKA---NKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392896924 728 GRALFDKVigpDGLLRSKTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGS 776
Cdd:cd03263 169 RRAIWDLI---LEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGS 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
568-780 |
5.28e-14 |
|
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: 73.14 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQnppvLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS-----------IAYV 636
Cdd:cd03299 1 LKVENLSKDWKEFK----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 637 PQHSWIF-NKTIKENILFGneLSNYFYDQvvgscqlKTDFRHFQQ-----GENTMVGENGITLSGGQKARISLARAVYQD 710
Cdd:cd03299 77 PQNYALFpHMTVYKNIAYG--LKKRKVDK-------KEIERKVLEiaemlGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 711 KDIYLLDDPLSAVDAHVGRALFD--KVIGPDgllrSKTRVL-VTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREelKKIRKE----FGVTVLhVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1221-1432 |
5.93e-14 |
|
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: 71.45 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLH--QLRSKL 1298
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSG-TLRFNldpfnqysddqiwncleicqlkqfaqeddktldryIAEGgknMSVGERQLLCLCRALLRGAR 1377
Cdd:cd03229 79 GMVFQDFALFPHlTVLEN-----------------------------------IALG---LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1378 IVILDEATASVDTVTDGIVQRAIRQHFPQS--TTISIAHRLDTIVD-SDRIVVLDAGR 1432
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
588-775 |
8.26e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 72.14 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 588 DLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-SIAYVPQHSWIFNKTIKENILFgnelSNYFYDQVV 666
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLF----AHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 667 G---SCQLKTDFRHfQQGENTMVGENGI---------TLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDK 734
Cdd:cd03298 92 GlglSPGLKLTAED-RQAIEVALARVGLaglekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392896924 735 VIGPDGlLRSKTRVLVTHNLQYTKYVDT-IYVIEDGQIVQHG 775
Cdd:cd03298 171 VLDLHA-ETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
568-770 |
9.57e-14 |
|
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: 69.78 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPqnpPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG--SIAYVPQhswifnk 645
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 tikenilfgnelsnyfydqvvgscqlktdfrhfqqgentmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392896924 726 HVGRALfdkvigPDGLLRSK-TRVLVTHNLQYTKYV-DTIYVIEDGQ 770
Cdd:cd03221 104 ESIEAL------EEALKEYPgTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
271-547 |
1.14e-13 |
|
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: 73.23 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 271 LNPILLKQLIDYVsLHDQPLSFGIAIACIMFSCSTTRSL---LQNYQIAGMCRQAVyyqTVLSNAILHKILRLSPSARSN 347
Cdd:cd18552 17 ALAWLLKPLLDDI-FVEKDLEALLLVPLAIIGLFLLRGLasyLQTYLMAYVGQRVV---RDLRNDLFDKLLRLPLSFFDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 348 RTAGEILNHAAVDIEIIVHSVP-YLQNMWSVPFQVtLAMTMLAITLGW--AAMAGVCIMILFIPLNLCTSRFIKLSQQKQ 424
Cdd:cd18552 93 NSSGDLISRITNDVNQVQNALTsALTVLVRDPLTV-IGLLGVLFYLDWklTLIALVVLPLAALPIRRIGKRLRKISRRSQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 425 MKIkDERTKLSNEMLNGIKVVKLYAWEES----FEDQINRLRAKEVKMLRNVCILSRIVDVANAaspflVAIGSFTCYVL 500
Cdd:cd18552 172 ESM-GDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPLMELLGA-----IAIALVLWYGG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 392896924 501 WSPDENGLTPSvAFVA-LTIFNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18552 246 YQVISGELTPG-EFISfITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
584-776 |
1.66e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 72.07 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAYVPQHSWI-FNKTIKE 649
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHSSLaFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGneLSNYFY-----DQVVGSCQLKTDFRHFQQGENTmvgengiTLSGGQKARISLARA---VYQDKD----IYLLD 717
Cdd:COG4559 95 VVALG--RAPHGSsaaqdRQIVREALALVGLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqLWEPVDggprWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 718 DPLSAVD-AHVGRALfdkvigpdGLLRSKTR-----VLVTHNLQYT-KYVDTIYVIEDGQIVQHGS 776
Cdd:COG4559 166 EPTSALDlAHQHAVL--------RLARQLARrgggvVAVLHDLNLAaQYADRILLLHQGRLVAQGT 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1222-1434 |
1.82e-13 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 71.03 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIdtiglHQLRSKLIII 1301
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1302 PQ------------EPVVFSGTLRFnLDPFNQYSDDQ---IWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLL 1366
Cdd:cd03235 74 PQrrsidrdfpisvRDVVLMGLYGH-KGLFRRLSKADkakVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1367 CLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQ-HFPQSTTISIAHRLDTIVDS-DRIVVLDAGRVA 1434
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVVA 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
585-771 |
2.11e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 71.02 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEM----VLLDGRV---------KVGGSIAYVPQHSWIF-NKTIK 648
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPdsgtIIIDGLKltddkkninELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENILFG------------NELSNYFYDQVvgscQLKtDFRHFQQGEntmvgengitLSGGQKARISLARAVYQDKDIYLL 716
Cdd:cd03262 95 ENITLApikvkgmskaeaEERALELLEKV----GLA-DKADAYPAQ----------LSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 717 DDPLSAVDAHVGRALFD--KVIGPDGLlrskTRVLVTHNLQYTKYV-DTIYVIEDGQI 771
Cdd:cd03262 160 DEPTSALDPELVGEVLDvmKDLAEEGM----TMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
584-781 |
2.13e-13 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 70.93 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVldeM---------VLLDG----------RVKVGgsIAYVPQHSWIF- 643
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MgllpprsgsIRFDGrditglppheRARAG--IGYVPEGRRIFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENILfgneLSNYFYDQVVGSCQLKTDFRHF---QQGENTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDP- 719
Cdd:cd03224 89 ELTVEENLL----LGAYARRRAKRKARLERVYELFprlKERRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPs 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 720 --LSAVdahVGRALFDKVIGpdglLRSK--TRVLVTHNLQYT-KYVDTIYVIEDGQIVQHGSFEDIA 781
Cdd:cd03224 161 egLAPK---IVEEIFEAIRE----LRDEgvTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELL 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
584-736 |
2.75e-13 |
|
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: 70.20 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------SIAYVPQHSWIFNK-TIKEN 650
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 651 ILF-----GNELSNYFYDQVVGSCQLktdfRHFqqgENTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:COG4133 96 LRFwaalyGLRADREAIDEALEAVGL----AGL---ADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170
....*....|.
gi 392896924 726 HvGRALFDKVI 736
Cdd:COG4133 165 A-GVALLAELI 174
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
568-775 |
2.87e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.85 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG---------------- 631
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 SIAYVPQ-HSWIFNKTIKENILFGNELSNYFYDQV----------VGscqLKtdfrHFqqgENTMVGEngitLSGGQKAR 700
Cdd:COG2884 80 RIGVVFQdFRLLPDRTVYENVALPLRVTGKSRKEIrrrvrevldlVG---LS----DK---AKALPHE----LSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 701 ISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS-----KTRVLVTHNL----QYTKYVdtiYVIEDGQI 771
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIME-------LLEEinrrgTTVLIATHDLelvdRMPKRV---LELEDGRL 215
|
....
gi 392896924 772 VQHG 775
Cdd:COG2884 216 VRDE 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
585-788 |
3.50e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.22 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAvLDEM------------VLLDG-------------RVKVGgsiaYVPQH 639
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMndlipgarvegeILLDGediydpdvdvvelRRRVG----MVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 640 SWIFNKTIKENILFG---------NELsnyfyDQVVGSCqLKtdfrhfqqgentMVG----------ENGITLSGGQKAR 700
Cdd:COG1117 101 PNPFPKSIYDNVAYGlrlhgikskSEL-----DEIVEES-LR------------KAAlwdevkdrlkKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 701 ISLARAVYQDKDIYLLDDPLSAVD----AHVGRALFDkvigpdglLRSK-TRVLVTHNLQYTKYV-DTIYVIEDGQIVQH 774
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTHNMQQAARVsDYTAFFYLGELVEF 234
|
250 260
....*....|....*....|....
gi 392896924 775 GSFEDI----------AYVDGPFG 788
Cdd:COG1117 235 GPTEQIftnpkdkrteDYITGRFG 258
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1233-1454 |
3.83e-13 |
|
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: 71.43 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1233 NLPL----VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKiddveidtiglHQLRskLIIIPQEPVVF 1308
Cdd:cd03291 44 NLCLvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HSGR--ISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1309 SGTLRFNLDPFNQYSDDQIWNCLEICQLKQ----FAQEDDKTLdryiAEGGKNMSVGERQLLCLCRALLRGARIVILDEA 1384
Cdd:cd03291 111 PGTIKENIIFGVSYDEYRYKSVVKACQLEEditkFPEKDNTVL----GEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1385 TASVDTVTDG-IVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLL-LNPDslYSQLL 1454
Cdd:cd03291 187 FGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQsLRPD--FSSKL 256
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
585-780 |
5.64e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.04 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLS--AVLDEMVllDGRVKVGGS-----------IAYVPQHSWIF-NKTIKEN 650
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRiiAGLEHQT--SGHIRFHGTdvsrlhardrkVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 651 ILFG-------NELSNYFYDQVVGSCQLKTDFRHFQQGENTMvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:PRK10851 95 IAFGltvlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 724 DAHVGRALfdkvigpDGLLRSK------TRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK10851 168 DAQVRKEL-------RRWLRQLheelkfTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
586-780 |
6.15e-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: 70.75 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLS--------------------AVLDEMVLLDGRVKvggSIAYVPQHSWIF-N 644
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRcinrlieptsgkvlidgqdiAAMSRKELRELRRK---KISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 645 KTIKENILFGNELSnyfydqvvGSCQLKTDFRHFQQGEntMVGENGIT------LSGGQKARISLARAVYQDKDIYLLDD 718
Cdd:cd03294 117 RTVLENVAFGLEVQ--------GVPRAEREERAAEALE--LVGLEGWEhkypdeLSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 719 PLSAVDAHVGRALFDKVIGPDGLLRsKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1221-1442 |
7.73e-13 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDtiglhqlRSKLII 1300
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 --IPQEP------------VVFSGTLRFN--LDPFNQYSDDQIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQ 1364
Cdd:COG1121 78 gyVPQRAevdwdfpitvrdVVLMGRYGRRglFRRPSRADREAVDEALERVGLEDLA-------DRPIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1365 llclcrallrGARIVILDEATASVDTVT-DGIVQ--RAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRVA-----E 1435
Cdd:COG1121 147 rvllaralaqDPDLLLLDEPFAGVDAATeEALYEllRELRRE--GKTILVVTHDLGAVREyFDRVLLLNRGLVAhgppeE 224
|
....*..
gi 392896924 1436 FDTPSNL 1442
Cdd:COG1121 225 VLTPENL 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
584-780 |
8.29e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.11 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSavldeMV--LLD---GRVKVGG-------------SIAYVPQHSWIFNK 645
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLS-----MIsrLLPpdsGEVLVDGldvattpsrelakRLAILRQENHINSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 -TIKENILFG---------NELSNYFYDQVVGSCQLkTDFRHFQQGEntmvgengitLSGGQKARISLARAVYQDKDIYL 715
Cdd:COG4604 90 lTVRELVAFGrfpyskgrlTAEDREIIDEAIAYLDL-EDLADRYLDE----------LSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 716 LDDPLSAVDAHVGRALFdkvigpdGLLRS------KTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG4604 159 LDEPLNNLDMKHSVQMM-------KLLRRladelgKTVVIVLHDINFaSCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
585-782 |
8.62e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLL---SAVL--DEmvlldGRVKVGGSIAYVPQHSWIFNK--TIKENILF---- 653
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLkliAGILepTS-----GRVEVNGRVSALLELGAGFHPelTGRENIYLngrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 654 -GneLSNYFYDQVVGSCQlktDF----RHFqqgeNTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVG 728
Cdd:COG1134 116 lG--LSRKEIDEKFDEIV---EFaelgDFI----DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 729 R---ALFDKVIGpdgllRSKTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI--AY 782
Cdd:COG1134 183 KkclARIRELRE-----SGRTVIFVSHSMGAvRRLCDRAIWLEKGRLVMDGDPEEViaAY 237
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
585-778 |
9.39e-13 |
|
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: 70.27 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLdEMVLLDGRVKVGG-------------SIAYVPQHSWIFNKTIKENI 651
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 LFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAhVGRAL 731
Cdd:cd03289 98 DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392896924 732 FDKVIgpDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFE 778
Cdd:cd03289 177 IRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQ 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
584-776 |
9.50e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------SIAYVPQHSWI-FNKTIKE 649
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFG---NELSNYFYDQVVGSCQLKTDFRHFQQGENTmvgengiTLSGGQKARISLARAVYQ------DKDIYLLDDPL 720
Cdd:PRK13548 96 VVAMGrapHGLSRAEDDALVAAALAQVDLAHLAGRDYP-------QLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 721 SAVD-AHVGRALfdkvigpdGLLRSKTR------VLVTHNL-QYTKYVDTIYVIEDGQIVQHGS 776
Cdd:PRK13548 169 SALDlAHQHHVL--------RLARQLAHerglavIVVLHDLnLAARYADRIVLLHQGRLVADGT 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
584-780 |
1.00e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEM------VLLDGR-------VKVGGSIAYVPQHSWI-FNKTIKE 649
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtptagtVLVAGDdvealsaRAASRRVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGNELSNYFYDQVVGSCQLKTDfRHFQQGENTMVGENGIT-LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAH-- 726
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLDINhq 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 727 -----VGRALFDkvigpDGllrsKTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK09536 176 vrtleLVRRLVD-----DG----KTAVAAIHDLDLaARYCDELVLLADGRVRAAGPPADV 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
585-780 |
1.01e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMV--LLDGRVKVGGSI-------------------AYVPQHSW-I 642
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVtlngeplaaidaprlarlrAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 643 FNKTIKENILFG--------NELSNYfyDQVVGSCQLKtdfrhfQQGENTMVGENGITLSGGQKARISLARAVYQ----- 709
Cdd:PRK13547 96 FAFSAREIVLLGrypharraGALTHR--DGEIAWQALA------LAGATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 710 ----DKDIYLLDDPLSAVD-AHVGRaLFDKVigpdgllRSKTR-----VL-VTH--NLQyTKYVDTIYVIEDGQIVQHGS 776
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDlAHQHR-LLDTV-------RRLARdwnlgVLaIVHdpNLA-ARHADRIAMLADGAIVAHGA 238
|
....
gi 392896924 777 FEDI 780
Cdd:PRK13547 239 PADV 242
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
571-780 |
1.02e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 571 KNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVL--------------DEMVLLDGRVKVGGSIAYV 636
Cdd:PRK10895 7 KNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVgivprdagniiiddEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 637 PQHSWIFNKtikenilfgneLSnyFYDQVVGSCQLKTDFRHFQQGE--NTMVGENGIT---------LSGGQKARISLAR 705
Cdd:PRK10895 84 PQEASIFRR-----------LS--VYDNLMAVLQIRDDLSAEQREDraNELMEEFHIEhlrdsmgqsLSGGERRRVEIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 706 AVYQDKDIYLLDDPLSAVDAhVGRALFDKVIgpDGLLRSKTRVLVT-HNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDP-ISVIDIKRII--EHLRDSGLGVLITdHNVRETLAVcERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1221-1435 |
1.44e-12 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 68.65 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLP--LVLKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEG----ESGTIKIDDVEIDtiglhQL 1294
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLL----RIIAGlerpTSGEVLVDGEPVT-----GP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1295 RSKLIIIPQEPVVFS----------GtLRFNLDPFNQySDDQIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQ 1364
Cdd:cd03293 72 GPDRGYVFQQDALLPwltvldnvalG-LELQGVPKAE-ARERAEELLELVGLSGFE-------NAYPHQ----LSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1365 LLCLCRALLRGARIVILDEATASVDTVTDGIVQRAI----RQHfpQSTTISIAHRLD-TIVDSDRIVVLDA--GRVAE 1435
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRET--GKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1221-1434 |
1.71e-12 |
|
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: 66.68 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQ-LRSKLI 1299
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 IIPQepvvfsgtlrfnldpfnqysddqiwncleicqlkqfaqeddktldryiaeggknMSVGERQLLCLCRALLRGARIV 1379
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1380 ILDEATAS-----VDTVTDgIVQRAIRQHfpqSTTISIAHRLDTIVD-SDRIVVLDAGRVA 1434
Cdd:cd03216 105 ILDEPTAAltpaeVERLFK-VIRRLRAQG---VAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1213-1461 |
1.78e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1213 EKWPVKGKIELDGFSMRY--RKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVE-IDTI 1289
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1290 GLHQLRSKLIIIPQEPVVFSGTLRFNL-------------------DPFNQYSD-DQIWNCLEICQL------------- 1336
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQENkNKRNSCRAKCAGdlndmsnttdsne 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1337 -----KQFAQEDDKTL-----------------DRYIAEGGKN---MSVGERQLLCLCRALLRGARIVILDEATASVDTV 1391
Cdd:PTZ00265 534 liemrKNYQTIKDSEVvdvskkvlihdfvsalpDKYETLVGSNaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1392 TDGIVQRAIR--QHFPQSTTISIAHRLDTIVDSDRIVVLdAGRVAEFDTPSNLLLNPDSLYSQLLNEKNRKQ 1461
Cdd:PTZ00265 614 SEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVL-SNRERGSTVDVDIIGEDPTKDNKENNNKNNKD 684
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
568-780 |
1.88e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQNP-PVLKDLSATIKPGQLIAIVGSVGGGKSSLLsavldEMV-LLD----GRVKVGG---------- 631
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLI-----RCInLLErptsGSVLVDGvdltalsere 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 ------SIAYVPQHswiFN----KTIKENILFGNELSNYFYDQV----------VGscqLkTDFRH---FQqgentmvge 688
Cdd:COG1135 77 lraarrKIGMIFQH---FNllssRTVAENVALPLEIAGVPKAEIrkrvaellelVG---L-SDKADaypSQ--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 689 ngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRS------KTRVLVTHNLQYTKYV-D 761
Cdd:COG1135 141 ----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILD-------LLKDinrelgLTIVLITHEMDVVRRIcD 209
|
250
....*....|....*....
gi 392896924 762 TIYVIEDGQIVQHGSFEDI 780
Cdd:COG1135 210 RVAVLENGRIVEQGPVLDV 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
584-780 |
1.89e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 68.42 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-SIAYVPQHSWIFNK-----------TIKENI 651
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPPHKRPVNTvfqnyalfphlTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 LFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVG--- 728
Cdd:cd03300 94 AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRkdm 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 729 ----RALFDKVigpdGLlrskTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:cd03300 170 qlelKRLQKEL----GI----TFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1449 |
2.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPV-VFSGTL-----RFNLDPFNQYSDDQIWNCLEicqlkqfAQEDDKTLDRYIAEgGKNMSVGERQLLCLCRALLR 1374
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDEMHRRVSE-------ALKQVDMLERADYE-PNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1375 GARIVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLNPDSL 1449
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
566-775 |
2.24e-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: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 566 NAIVFKNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAvldeMVLLD----GRVKVG-----GSIAYV 636
Cdd:PRK11264 2 SAIEVKNLVKKFHGQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRC----INLLEqpeaGTIRVGditidTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 637 PQHSWIfnKTIKENILFGNELSNYFYDQVV------GSCQLKTDFRH--FQQGENTM--VGENGIT------LSGGQKAR 700
Cdd:PRK11264 75 QQKGLI--RQLRQHVGFVFQNFNLFPHRTVleniieGPVIVKGEPKEeaTARARELLakVGLAGKEtsyprrLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 701 ISLARAVYQDKDIYLLDDPLSAVDAH-VGRALfdkvigpdGLLRS-----KTRVLVTHNLQYTKYV-DTIYVIEDGQIVQ 773
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPElVGEVL--------NTIRQlaqekRTMVIVTHEMSFARDVaDRAIFMDQGRIVE 224
|
..
gi 392896924 774 HG 775
Cdd:PRK11264 225 QG 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
584-755 |
2.24e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.89 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV---LDEMVLLDGRVKVGGS-----------IAYVPQHSWIF-NKTIK 648
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVLLNGRrltalpaeqrrIGILFQDDLLFpHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENILFGnelsnyfydqvvgscqLKTDFRHFQQGENTM-----VGENGI------TLSGGQKARISLARAVYQDKDIYLLD 717
Cdd:COG4136 95 ENLAFA----------------LPPTIGRAQRRARVEqaleeAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 718 DPLSAVDAHvgralfdkvigpdglLRSKTR--------------VLVTHNLQ 755
Cdd:COG4136 159 EPFSKLDAA---------------LRAQFRefvfeqirqrgipaLLVTHDEE 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1221-1449 |
2.35e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.99 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLP-LVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLI 1299
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 IIPQEP-VVFSGT-----LRFNLDpfNQ---YSD--DQIWNCLEICQLKQFAQEDDKTLdryiaeggknmSVGERQLLCL 1368
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLE--NKgipHEEmkERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1369 CRALLRGARIVILDEATASVD---------TVtdgivqRAIRQHFpQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTP 1439
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDpegrlelikTI------KGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTP 224
|
250
....*....|
gi 392896924 1440 SNLLLNPDSL 1449
Cdd:PRK13650 225 RELFSRGNDL 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
567-725 |
2.79e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.74 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWKGP-QNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLS------AVLDEMVLLDGRVKVGGSI--AYVP 637
Cdd:COG4525 3 MLTVRHVSVRYPGGgQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNliagflAPSSGEITLDGVPVTGPGAdrGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 638 QHS----WifnKTIKENILFGNELsnyfydQVVGSCQlktdfRHFQQGEN-TMVGENGI------TLSGGQKARISLARA 706
Cdd:COG4525 83 QKDallpW---LNVLDNVAFGLRL------RGVPKAE-----RRARAEELlALVGLADFarrriwQLSGGMRQRVGIARA 148
|
170
....*....|....*....
gi 392896924 707 VYQDKDIYLLDDPLSAVDA 725
Cdd:COG4525 149 LAADPRFLLMDEPFGALDA 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
580-776 |
2.95e-12 |
|
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: 71.97 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 580 PQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------SIAYVPQHSWIFNK-T 646
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELSNYFYDQVvgscQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAH 726
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEA----QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 727 VGRALFDKVIGpdglLRS-KTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGS 776
Cdd:TIGR01257 1096 SRRSIWDLLLK----YRSgRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1231-1450 |
2.97e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1231 RKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIG---LHQLRSKLIiipqePVV 1307
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKI-----AMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1308 FSGtlrFNLDPFNQYSDDQIWNcLEICQLKQfAQEDDKTLDRYIAEGGKN--------MSVGERQLLCLCRALLRGARIV 1379
Cdd:PRK10070 112 FQS---FALMPHMTVLDNTAFG-MELAGINA-EERREKALDALRQVGLENyahsypdeLSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 1380 ILDEATASVDTVTDGIVQRAI--RQHFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNPDSLY 1450
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
584-780 |
3.35e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.71 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEM----VLLDGrVKVGGS----------IAYVPQHswiFN--- 644
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPdsgtITVDG-EDLTDSkkdinklrrkVGMVFQQ---FNlfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 645 -KTIKENILFG------------NELSNYFYDQVvgscQL--KTDFRHFQqgentmvgengitLSGGQKARISLARAVYQ 709
Cdd:COG1126 91 hLTVLENVTLApikvkkmskaeaEERAMELLERV----GLadKADAYPAQ-------------LSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 710 DKDIYLLDDPLSAVDAH-VGRALfdKVIGpdGLLRSK-TRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:COG1126 154 EPKVMLFDEPTSALDPElVGEVL--DVMR--DLAKEGmTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
585-775 |
4.00e-12 |
|
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: 67.56 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSaVLDEMVLLD-GRVKVGGSIAYVPQHSWIFNK--TIKENILFGNELSNY- 660
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLR-LLAGIYPPDsGTVTVRGRVSSLLGLGGGFNPelTGRENIYLNGRLLGLs 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 661 ------FYDQVVGSCQLKTDFrhfqqgeNTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAH----VGRA 730
Cdd:cd03220 116 rkeideKIDEIIEFSELGDFI-------DLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 392896924 731 LFDKVigpdglLRSKTRVLVTHNLQYTK-YVDTIYVIEDGQIVQHG 775
Cdd:cd03220 185 LRELL------KQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1221-1437 |
6.24e-12 |
|
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: 66.39 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEG----ESGTIKIDDVEIDTIGLHQLRS 1296
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLL----RLIAGlerpDSGEILIDGRDVTGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1297 KLIIipQEPVVFS-----GTLRFNLDPFNQYSDDQIWNCLEIcqLKQFaqEDDKTLDRYIAEggknMSVGERQLLCLCRA 1371
Cdd:cd03259 75 GMVF--QDYALFPhltvaENIAFGLKLRGVPKAEIRARVREL--LELV--GLEGLLNRYPHE----LSGGQQQRVALARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1372 LLRGARIVILDEATASVDT-VTDGI---VQRAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFD 1437
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAkLREELreeLKELQREL--GITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
568-780 |
7.58e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSL---LSAVLDEM---VL-----------LDGRVKVG 630
Cdd:PRK13644 2 IRLENVSYSY--PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQkgkVLvsgidtgdfskLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 631 GSIAYVPQHSWIfNKTIKENILFGNElsnyfydqvvGSCQLKTDFRhfqQGENTMVGENGI---------TLSGGQKARI 701
Cdd:PRK13644 80 GIVFQNPETQFV-GRTVEEDLAFGPE----------NLCLPPIEIR---KRVDRALAEIGLekyrhrspkTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 702 SLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPDGllRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
568-780 |
7.80e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGPQNP-PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVldemVLLD----GRVKVGG----------- 631
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGqdltalsekel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 -----SIAYVPQHswiFN----KTIKENILFGNELSNYFYDQV----------VGscqLkTDFRHFQQGEntmvgengit 692
Cdd:PRK11153 78 rkarrQIGMIFQH---FNllssRTVFDNVALPLELAGTPKAEIkarvtellelVG---L-SDKADRYPAQ---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 693 LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRSKTR------VLVTHNLQYTKYV-DTIYV 765
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKDINRelgltiVLITHEMDVVKRIcDRVAV 213
|
250
....*....|....*
gi 392896924 766 IEDGQIVQHGSFEDI 780
Cdd:PRK11153 214 IDAGRLVEQGTVSEV 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
586-788 |
8.14e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.11 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLSAvLDEMVLLDGRVKVGGSIAY---------------------VPQHSWIFN 644
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 645 KTIKENILFGNELS----NYFYDQVVgscqlktdfrhfqqgENTMVG------------ENGITLSGGQKARISLARAVY 708
Cdd:PRK14239 100 MSIYENVVYGLRLKgikdKQVLDEAV---------------EKSLKGasiwdevkdrlhDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDKVIGpdglLRSK-TRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI------ 780
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLG----LKDDyTMLLVTRSMQQaSRISDRTGFFLDGDLIEYNDTKQMfmnpkh 240
|
250
....*....|..
gi 392896924 781 ----AYVDGPFG 788
Cdd:PRK14239 241 keteDYISGKFG 252
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
567-775 |
9.70e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.32 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASlnwKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS------------IA 634
Cdd:PRK13536 41 AIDLAGVS---KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQhswiFNK-----TIKENIL-FGN--ELSNYFYDQVVGSCqlkTDFRHFQQGENTMVGEngitLSGGQKARISLARA 706
Cdd:PRK13536 118 VVPQ----FDNldlefTVRENLLvFGRyfGMSTREIEAVIPSL---LEFARLESKADARVSD----LSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 707 VYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPdgLLRSKTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHG 775
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSL--LARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEG 254
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
568-735 |
1.00e-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: 64.87 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNwkGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVK--VGGSIAYVPQHSWIFNK 645
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGmpEGEDLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 TIKENILfgnelsnYFYDQVvgscqlktdfrhfqqgentmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:cd03223 79 TLREQLI-------YPWDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170
....*....|
gi 392896924 726 HVGRALFDKV 735
Cdd:cd03223 125 ESEDRLYQLL 134
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
568-780 |
1.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.35 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNAS--LNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLL------------SAVLDEMVLLDG-------- 625
Cdd:PRK13634 3 ITFQKVEhrYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlngllqptsgTVTIGERVITAGkknkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 626 -RVKVGgsIAY-VPQHSwIFNKTIKENILFGNelSNYfydqvvGSCQLKTdfrhfQQGENTMVGENGIT----------L 693
Cdd:PRK13634 83 lRKKVG--IVFqFPEHQ-LFEETVEKDICFGP--MNF------GVSEEDA-----KQKAREMIELVGLPeellarspfeL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 694 SGGQKARISLARAVYQDKDIYLLDDPLSAVDAHvGRA----LFDKVIGPDGLlrskTRVLVTHNLQ-YTKYVDTIYVIED 768
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK-GRKemmeMFYKLHKEKGL----TTVLVTHSMEdAARYADQIVVMHK 221
|
250
....*....|..
gi 392896924 769 GQIVQHGSFEDI 780
Cdd:PRK13634 222 GTVFLQGTPREI 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
592-776 |
1.38e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 592 TIKPGQLIAIVGSVGGGKSSLL----------SAVLDEMVLLDGRVKVGGSIA-----------YVPQHSWIFNK-TIKE 649
Cdd:PRK09984 26 NIHHGEMVALLGPSGSGKSTLLrhlsglitgdKSAGSHIELLGRTVQREGRLArdirksrantgYIFQQFNLVNRlSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGNELSNYFYdqvvgscqlKTDFRHFQQGEN-------TMVG------ENGITLSGGQKARISLARAVYQDKDIYLL 716
Cdd:PRK09984 106 NVLIGALGSTPFW---------RTCFSWFTREQKqralqalTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 717 DDPLSAVDAHVGRALFDK---VIGPDGLlrskTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHGS 776
Cdd:PRK09984 177 DEPIASLDPESARIVMDTlrdINQNDGI----TVVVTLHQVDYAlRYCERIVALRQGHVFYDGS 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1171-1454 |
1.40e-11 |
|
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: 69.59 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1171 LNICVRSVSEIESNIVSVERVNEY---QKLEPEapwriekSLENEEKWPVKG-KIELDGFSMRYRKNLPLVLKNIDLKIE 1246
Cdd:TIGR00957 590 LNILPMVISSIVQASVSLKRLRIFlshEELEPD-------SIERRTIKPGEGnSITVHNATFTWARDLPPTLNGITFSIP 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1247 GGERIGVIGRTGSGKSSLTMALYrmieGEsgtikIDDVEidtiGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQ 1326
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLSALL----AE-----MDKVE----GHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKY 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1327 IWNCLEICQLK---QFAQEDDKTldrYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDT-VTDGIVQRAI-- 1400
Cdd:TIGR00957 730 YQQVLEACALLpdlEILPSGDRT---EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIgp 806
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 392896924 1401 RQHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDtPSNLLLNPDSLYSQLL 1454
Cdd:TIGR00957 807 EGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG-SYQELLQRDGAFAEFL 859
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
584-780 |
1.85e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.58 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLlSAVLDEMVLLD-GRVKVGGsIAYVPQHSW--------IFNK--------T 646
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTL-AKLLNGLLLPEaGTITVGG-MVLSEETVWdvrrqvgmVFQNpdnqfvgaT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELSNYFYDQVVGSCQ--LK----TDFRHFQQGEntmvgengitLSGGQKARISLARAVYQDKDIYLLDDPL 720
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDqaLRqvgmEDFLNREPHR----------LSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 721 SAVDAhVGRAlfdKVIGPDGLLRSKTRVLV---THNLQYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK13635 169 SMLDP-RGRR---EVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
585-780 |
2.17e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLS-------------AVLDEMVLL----DGRVKVGGS---------IAYVPQ 638
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegsiVVNGQTINLvrdkDGQLKVADKnqlrllrtrLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 639 HswiFN----KTIKENILFGNElsnyfydQVVGSCQLKTDFRHFQQGENTMVGENG-----ITLSGGQKARISLARAVYQ 709
Cdd:PRK10619 100 H---FNlwshMTVLENVMEAPI-------QVLGLSKQEARERAVKYLAKVGIDERAqgkypVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 710 DKDIYLLDDPLSAVDAH-VGRAL-FDKVIGPDGllrsKTRVLVTHNLQYTKYVDT-IYVIEDGQIVQHGSFEDI 780
Cdd:PRK10619 170 EPEVLLFDEPTSALDPElVGEVLrIMQQLAEEG----KTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1237-1446 |
2.24e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDT-IGLHQLRSKLIIIPQE-PVVFSGtlrF 1314
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTaRSLSQQKGLIRQLRQHvGFVFQN---F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLDPFNQYSDDQIWNCLeicQLKQFAQEDDKTLDR-YIAEGG---------KNMSVGERQLLCLCRALLRGARIVILDEA 1384
Cdd:PRK11264 95 NLFPHRTVLENIIEGPV---IVKGEPKEEATARAReLLAKVGlagketsypRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 1385 TASVDTVTDGIVQRAIRQHFPQSTTISI-AHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNP 1446
Cdd:PRK11264 172 TSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
567-780 |
2.61e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAvLDEMVLLDGRVKVGGSIAYVPQHSW----- 641
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 642 ----------------IFNKTIKENILFGNELSNYF----YDQVVGSCQLKTDFrhFQQGENTmVGENGITLSGGQKARI 701
Cdd:PRK14258 83 lnrlrrqvsmvhpkpnLFPMSVYDNVAYGVKIVGWRpkleIDDIVESALKDADL--WDEIKHK-IHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 702 SLARAVYQDKDIYLLDDPLSAVDAhVGRALFDKVIGPDGLLRSKTRVLVTHNL-QYTKYVDTIYVIED-----GQIVQHG 775
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDP-IASMKVESLIQSLRLRSELTMVIVSHNLhQVSRLSDFTAFFKGnenriGQLVEFG 238
|
....*
gi 392896924 776 SFEDI 780
Cdd:PRK14258 239 LTKKI 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1221-1304 |
2.68e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.07 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNlPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTI---GLHQLRSK 1297
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
....*..
gi 392896924 1298 LIIIPQE 1304
Cdd:COG2884 81 IGVVFQD 87
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1237-1437 |
2.81e-11 |
|
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: 64.86 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDD-----VEIdTIGLHqlrskliiiPQ----EPVV 1307
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsslLGL-GGGFN---------PEltgrENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1308 FSGTLrFNLDPfnQYSDDQIWNCLEICQLKQFaqeddktLDRYIaeggKNMSVGERQLLCLCRALLRGARIVILDEATAS 1387
Cdd:cd03220 107 LNGRL-LGLSR--KEIDEKIDEIIEFSELGDF-------IDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1388 VDTVTDGIVQRAIRQHFPQSTTISIA-HRLDTIVD-SDRIVVLDAGRVAEFD 1437
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
382-772 |
3.21e-11 |
|
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: 67.90 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 382 TLAMTMLAITLGWAAMAGVCIMILfiplnlcTSRFIKLSQQkqmkIKDERTKLSN---EMLNGIKVVKLYA------WEE 452
Cdd:COG4615 144 WLSPPLFLLTLVLLGLGVAGYRLL-------VRRARRHLRR----AREAEDRLFKhfrALLEGFKELKLNRrrrrafFDE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 453 SFEDQINRLRAKEVKMLRnvcILSRIVDVANAAspFLVAIGSFtcyVLWSPDENGLTPSVAF-VALTI-FnqLRQPMRMV 530
Cdd:COG4615 213 DLQPTAERYRDLRIRADT---IFALANNWGNLL--FFALIGLI---LFLLPALGWADPAVLSgFVLVLlF--LRGPLSQL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 531 ANLINTLVQARVSNKRLRQF---LNDEEMERKTEVALG-----NAIVFKNASLNWKGPQNPP--VLKDLSATIKPGQLIA 600
Cdd:COG4615 283 VGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPapadfQTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 601 IVGSVGGGKSSLLsavldeMVLL------DGRVKVGGSIayVPQHSW---------IFnktikenilfgnelSNYF-YDQ 664
Cdd:COG4615 363 IVGGNGSGKSTLA------KLLTglyrpeSGEILLDGQP--VTADNReayrqlfsaVF--------------SDFHlFDR 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 665 VVGSCQLKTD------FRHFQQGENTMVGENGIT---LSGGQKARISLARAVYQDKDIYLLD------DPlsavdahVGR 729
Cdd:COG4615 421 LLGLDGEADPararelLERLELDHKVSVEDGRFSttdLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFR 493
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 392896924 730 ALFDKVIGPDglLRS--KTRVLVTHNLQYTKYVDTIYVIEDGQIV 772
Cdd:COG4615 494 RVFYTELLPE--LKArgKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
585-771 |
3.23e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLL-----------------SAVLDE------MVLLDGRVkvggsiayVPqhsW 641
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLrllagletpsagellagTAPLAEaredtrLMFQDARL--------LP---W 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 642 ifnKTIKENILFGnelsnyfydqvvgscqLKTDFRHFQQGENTMVG------ENGITLSGGQKARISLARAVYQDKDIYL 715
Cdd:PRK11247 96 ---KKVIDNVGLG----------------LKGQWRDAALQALAAVGladranEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 716 LDDPLSAVDAhVGRALFDKVIgpDGLLRSK--TRVLVTHNL-QYTKYVDTIYVIEDGQI 771
Cdd:PRK11247 157 LDEPLGALDA-LTRIEMQDLI--ESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1221-1433 |
3.35e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 64.35 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVeiDTIGLHQ-----LR 1295
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ--DVSDLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1296 SKLIIIPQEpvvfsgtlrFNLDP-FNQYsdDQIWNCLEICQL--KQFAQEDDKTLDRYIAEGGKN-----MSVGERQLLC 1367
Cdd:cd03292 78 RKIGVVFQD---------FRLLPdRNVY--ENVAFALEVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1368 LCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVD--SDRIVVLDAGRV 1433
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
567-780 |
4.35e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.54 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWKG--PQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS----------IA 634
Cdd:PRK13649 2 GINLQNVSYTYQAgtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQH---------SWIFNKTIKENILFGNElsNYFYDQVVGSCQLKTDFRHFQQGENtMVGENGITLSGGQKARISLAR 705
Cdd:PRK13649 82 QIRKKvglvfqfpeSQLFEETVLKDVAFGPQ--NFGVSQEEAEALAREKLALVGISES-LFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 706 AVYQDKDIYLLDDPLSAVDAHVGRALFD--KVIGPDGLlrskTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTlfKKLHQSGM----TIVLVTHLMdDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1221-1449 |
4.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPL-VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLI 1299
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 IIPQepvvfsgtlrfnlDPFNQYS----DDQIWNCLE---ICQLKQFAQEDD-----KTLDRYIAEGGKnMSVGERQLLC 1367
Cdd:PRK13642 85 MVFQ-------------NPDNQFVgatvEDDVAFGMEnqgIPREEMIKRVDEallavNMLDFKTREPAR-LSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1368 LCRALLRGARIVILDEATASVDTVTDGIVQRAIRQ-----HFpqsTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNL 1442
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEikekyQL---TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
....*..
gi 392896924 1443 LLNPDSL 1449
Cdd:PRK13642 228 FATSEDM 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
585-775 |
4.56e-11 |
|
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: 63.84 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS---------IAYVPQHSWIFNK-TIKENILFG 654
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLYPKmKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 655 NELSNYfydqvvgscqLKTDFRH--------FQQGE--NTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVD 724
Cdd:cd03269 95 AQLKGL----------KKEEARRridewlerLELSEyaNKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392896924 725 AhVGRALFDKVIgpDGLLRS-KTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHG 775
Cdd:cd03269 161 P-VNVELLKDVI--RELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
586-755 |
4.87e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLSAV-----LDEMVLLDGRVKVGGSIAYVP---------------QHSWIFNK 645
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 TIKENILFGNELSNYF--YDQVVGscqlktdfRHFQQGE-----NTMVGENGITLSGGQKARISLARAVYQDKDIYLLDD 718
Cdd:PRK14243 106 SIYDNIAYGARINGYKgdMDELVE--------RSLRQAAlwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 392896924 719 PLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNLQ 755
Cdd:PRK14243 178 PCSALDPISTLRIEELM---HELKEQYTIIIVTHNMQ 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1221-1318 |
5.44e-11 |
|
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: 63.70 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEI--DTIGLHQLRSKL 1298
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100
....*....|....*....|
gi 392896924 1299 IIIPQepvvfsgtlRFNLDP 1318
Cdd:cd03262 79 GMVFQ---------QFNLFP 89
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
585-773 |
7.53e-11 |
|
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: 63.61 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLS--AVLD-----EMVLL---------DGRVKV-GGSIAYVPQHswiF---- 643
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGllAGLDrptsgTVRLAgqdlfaldeDARARLrARHVGFVFQS---Fqllp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENI-----LFGN---------ELsnyfydQVVGscqLKTDFRHF-QQgentmvgengitLSGGQKARISLARAVY 708
Cdd:COG4181 104 TLTALENVmlpleLAGRrdarararaLL------ERVG---LGHRLDHYpAQ------------LSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDkvigpdgLLRSKTR------VLVTHNLQYTKYVDTIYVIEDGQIVQ 773
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIID-------LLFELNRergttlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
942-1191 |
8.07e-11 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 64.88 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKL-QDNIRMCT 1020
Cdd:cd07346 42 ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLvSSGLLQLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1021 QTLLNACMILV-LISISTPIFLVCAApLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERT 1099
Cdd:cd07346 122 SDVLTLIGALViLFYLNWKLTLVALL-LLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEERE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1100 TTALSTNVDKFAQCRYLSHMSNRWLATRLEL---LGNTCVLFASLSATLSTKyfgLTPGMAGLSVSYALTITEVLNICVR 1176
Cdd:cd07346 201 IERFREANRDLRDANLRAARLSALFSPLIGLltaLGTALVLLYGGYLVLQGS---LTIGELVAFLAYLGMLFGPIQRLAN 277
|
250
....*....|....*
gi 392896924 1177 SVSEIESNIVSVERV 1191
Cdd:cd07346 278 LYNQLQQALASLERI 292
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1238-1454 |
1.24e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 65.86 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGEsGTIKIDDVEIDTIG---LHQLRSKLIIIPQEPvvFSgtlrf 1314
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FG----- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLDP---------------FNQYSDDQIWNclEICQLKQFAQEDDKTLDRYIAEggknMSVGERQllclcrallrgaRI- 1378
Cdd:COG4172 374 SLSPrmtvgqiiaeglrvhGPGLSAAERRA--RVAEALEEVGLDPAARHRYPHE----FSGGQRQ------------RIa 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1379 -----------VILDEATASVDtVTdgiVQRAI--------RQHfpQSTTISIAHRLdTIVD--SDRIVVLDAGRVAEFD 1437
Cdd:COG4172 436 iaralilepklLVLDEPTSALD-VS---VQAQIldllrdlqREH--GLAYLFISHDL-AVVRalAHRVMVMKDGKVVEQG 508
|
250
....*....|....*..
gi 392896924 1438 TPSNLLLNPDSLYSQLL 1454
Cdd:COG4172 509 PTEQVFDAPQHPYTRAL 525
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
585-772 |
1.32e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-SIAYVPQH---SWI---F---------NKTIK 648
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvFqdpmmgtapSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENIL--------FG------NELSNYFYDQVvgscqlktdfRHFQQG-EN---TMVGengiTLSGGQKARISLARAVYQD 710
Cdd:COG1101 101 ENLAlayrrgkrRGlrrgltKKRRELFRELL----------ATLGLGlENrldTKVG----LLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 711 KDIYLLDDPLSAVD---AHVGRALFDKVIGPDGLlrskTRVLVTHNLQY-TKYVDTIYVIEDGQIV 772
Cdd:COG1101 167 PKLLLLDEHTAALDpktAALVLELTEKIVEENNL----TTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
584-719 |
1.78e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKV--GGSIAYVPQHSWIF-NKTIKENILFGN-ELSn 659
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkGLRIGYLPQEPPLDdDLTVLDTVLDGDaELR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 660 yfydqvvgscQLKTDFRHFQQGENTMVGEN-----------------------------GI----------TLSGGQKAR 700
Cdd:COG0488 91 ----------ALEAELEELEAKLAEPDEDLerlaelqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRR 160
|
170
....*....|....*....
gi 392896924 701 ISLARAVYQDKDIYLLDDP 719
Cdd:COG0488 161 VALARALLSEPDLLLLDEP 179
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
588-780 |
1.95e-10 |
|
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: 64.35 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 588 DLSATIKPGQLIAIVGSVGGGKSSLLSAV------------LDEMVLLDGRVKV-----GGSIAYVPQHSWIF-NKTIKE 649
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglerpdsgrirLGGEVLQDSARGIflpphRRRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFG-----NELSNYFYDQVVgscqlktdfrhfqqgenTMVGengI---------TLSGGQKARISLARAVYQDKDIYL 715
Cdd:COG4148 97 NLLYGrkrapRAERRISFDEVV-----------------ELLG---IghlldrrpaTLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 716 LDDPLSAVDAHVGRALfdkvigpdgL-----LRSKTR---VLVTHNLQytkYV----DTIYVIEDGQIVQHGSFEDI 780
Cdd:COG4148 157 MDEPLAALDLARKAEI---------LpylerLRDELDipiLYVSHSLD---EVarlaDHVVLLEQGRVVASGPLAEV 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
586-776 |
2.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSL---LSAVL---------------DEMV-LLDGRVKVGGSIAYvPQHSwIFNKT 646
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLiqhLNGLLkptsgkiiidgvditDKKVkLSDIRKKVGLVFQY-PEYQ-LFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFG--------NELSNYFYD--QVVGscqLKTDfrhfqqgenTMVGENGITLSGGQKARISLARAVYQDKDIYLL 716
Cdd:PRK13637 101 IEKDIAFGpinlglseEEIENRVKRamNIVG---LDYE---------DYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 717 DDPLSAVDAHvGRalfDKVIGPDGLLRSK---TRVLVTHNLQ-YTKYVDTIYVIEDGQIVQHGS 776
Cdd:PRK13637 169 DEPTAGLDPK-GR---DEILNKIKELHKEynmTIILVSHSMEdVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1221-1442 |
2.37e-10 |
|
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: 62.14 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTiGLHQLRSKLII 1300
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSG-TLRFNLDPF-------NQYSDDQIWNCLEICQLKQFAqeddktlDRYIaeggKNMSVGERQLLCLCRAL 1372
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYarlkglpKSEIKEEVELLLRVLGLTDKA-------NKRA----RTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1373 LRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTI-VDSDRIVVLDAGRVAEFDTPSNL 1442
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
584-781 |
3.31e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.97 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVL-----DE-MVLLDG----------RVKVGgsIAYVPQHSWIFNK-T 646
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVglvkpDSgRIFLDGedithlpmhkRARLG--IGYLPQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELSNYFYDQVVGSC-QLKTDFR--HFQqgeNTMvgenGITLSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:COG1137 95 VEDNILAVLELRKLSKKEREERLeELLEEFGitHLR---KSK----AYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 724 D--AhVG------RALFDKVIGpdgllrsktrVLVT-HNLQYT-KYVDTIYVIEDGQIVQHGSFEDIA 781
Cdd:COG1137 168 DpiA-VAdiqkiiRHLKERGIG----------VLITdHNVRETlGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1236-1415 |
3.59e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 60.25 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1236 LVLKNIDLKIEGGERIGVIGRTGSGKSSLtmalYRMIEG--ESGTikiddveiDTIGLHQlRSKLIIIPQEPVVFSGTLR 1313
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALAGlwPWGS--------GRIGMPE-GEDLLFLPQRPYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1314 fnldpfnqysdDQI---WncleicqlkqfaqedDKTLdryiaeggknmSVGERQLLCLCRALLRGARIVILDEATASVDT 1390
Cdd:cd03223 82 -----------EQLiypW---------------DDVL-----------SGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*
gi 392896924 1391 VTDGIVQRAIRQHFpqSTTISIAHR 1415
Cdd:cd03223 125 ESEDRLYQLLKELG--ITVISVGHR 147
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
584-797 |
4.27e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGSIAYVP--------QHS----WifnKTIKENI 651
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfQNEgllpW---RNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 LFGNELSNyfydqvVGscqlKTDFRHFQQGENTMVGENGI------TLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:PRK11248 92 AFGLQLAG------VE----KMQRLEIAHQMLKKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 726 hvgralFDKVIGPDGLLR-----SKTRVLVTHNLQYTKYVDTIYVI---EDGQIVQHGSFediayvdgPFGRLWSECENS 797
Cdd:PRK11248 162 ------FTREQMQTLLLKlwqetGKQVLLITHDIEEAVFMATELVLlspGPGRVVERLPL--------NFARRFVAGESS 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1221-1449 |
4.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEG-------ESGTIKIDDVEIDTIGLHQ 1293
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLINGlllpddnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1294 LRSKLIIIPQepvvfsgtlrfnlDPFNQY-----SDDQIWNC-------LEICQLKQFAQEDDKTLDrYIAEGGKNMSVG 1361
Cdd:PRK13640 82 IREKVGIVFQ-------------NPDNQFvgatvGDDVAFGLenravprPEMIKIVRDVLADVGMLD-YIDSEPANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1362 ERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAHRLDTIVDSDRIVVLDAGRVAEFDTP 1439
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
250
....*....|
gi 392896924 1440 SNLLLNPDSL 1449
Cdd:PRK13640 228 VEIFSKVEML 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1237-1448 |
4.61e-10 |
|
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: 61.58 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTigLHQLRSKLIIIPQEPVVFSgtlrfNL 1316
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFP-----HM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1317 DPFNQYS---DDQIWNCLEI-CQLKQFAQ--EDDKTLDRYIAeggkNMSVGERQLLCLCRALLRGARIVILDEATASVDT 1390
Cdd:cd03299 87 TVYKNIAyglKKRKVDKKEIeRKVLEIAEmlGIDHLLNRKPE----TLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1391 VTDGIVQRAIR--QHFPQSTTISIAHRLDTI-VDSDRIVVLDAGRVAEFDTPSNLLLNPDS 1448
Cdd:cd03299 163 RTKEKLREELKkiRKEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1224-1431 |
4.78e-10 |
|
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: 61.19 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1224 DGFsMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSK----LI 1299
Cdd:cd03290 5 NGY-FSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 IIPQEPVVFSGTLRFNL---DPFNQYSDDQIwncLEICQLK---QFAQEDDKTldrYIAEGGKNMSVGERQLLCLCRALL 1373
Cdd:cd03290 83 YAAQKPWLLNATVEENItfgSPFNKQRYKAV---TDACSLQpdiDLLPFGDQT---EIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1374 RGARIVILDEATASVDT-VTDGIVQRAIRQHF--PQSTTISIAHRLDTIVDSDRIVVLDAG 1431
Cdd:cd03290 157 QNTNIVFLDDPFSALDIhLSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
585-778 |
5.45e-10 |
|
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: 60.62 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVldeMVLLDGRVkVGGSIAYvpQHSWIFNKTIKENILFGNELSnyfydq 664
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI---MGHPKYEV-TEGEILF--KGEDITDLPPEERARLGIFLA------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 665 vvgscqlktdfrhFQ-----QGENTM-----VGENgitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDK 734
Cdd:cd03217 83 -------------FQyppeiPGVKNAdflryVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392896924 735 VigpDGLLRSKTRVL-VTHNLQYTKYV--DTIYVIEDGQIVQHGSFE 778
Cdd:cd03217 147 I---NKLREEGKSVLiITHYQRLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
568-780 |
5.50e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.26 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkGPQnpPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSA------------VLDEMVLLDGRVKVGG---S 632
Cdd:PRK09493 2 IEFKNVSKHF-GPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCinkleeitsgdlIVDGLKVNDPKVDERLirqE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 633 IAYVPQHSWIFNK-TIKENILFGNElsnyfydQVVGSCqlKTDFRhfQQGEnTMVGENGIT---------LSGGQKARIS 702
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPL-------RVRGAS--KEEAE--KQAR-ELLAKVGLAerahhypseLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 703 LARAVYQDKDIYLLDDPLSAVDAH-------VGRALFDkvigpDGLlrskTRVLVTHNLQYTKYVDT-IYVIEDGQIVQH 774
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPElrhevlkVMQDLAE-----EGM----TMVIVTHEIGFAEKVASrLIFIDKGRIAED 217
|
....*.
gi 392896924 775 GSFEDI 780
Cdd:PRK09493 218 GDPQVL 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1237-1445 |
5.83e-10 |
|
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: 60.91 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQ-LRSKLIIIPQEPVVFSG-TLRF 1314
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLD--PFNQYSDDQIWNCLEICQ----LKQFaqeddktLDRYiaegGKNMSVGERQLLCLCRALLRGARIVILDEATAS- 1387
Cdd:cd03224 95 NLLlgAYARRRAKRKARLERVYElfprLKER-------RKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGl 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 1388 ----VDTVTDGIvqRAIRQhfpQSTTISIA-HRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLN 1445
Cdd:cd03224 164 apkiVEEIFEAI--RELRD---EGVTILLVeQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
978-1191 |
6.12e-10 |
|
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: 62.19 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 978 LIHALLVAPISFFDTTPTGRIINRLSRDLDVI-----DKLQDNIRMCTQTLlnaCMILVLISISTPIFLVCAAPLILIYY 1052
Cdd:cd18557 75 LFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqsavtDNLSQLLRNILQVI---GGLIILFILSWKLTLVLLLVIPLLLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1053 FVMIYyiptSRQLKRLESANRSPI--LSTIA-ESIHGASSIRAFDKTERTTTALSTNVDkfaQCRYLSHMSNRWLATrLE 1129
Cdd:cd18557 152 ASKIY----GRYIRKLSKEVQDALakAGQVAeESLSNIRTVRSFSAEEKEIRRYSEALD---RSYRLARKKALANAL-FQ 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1130 LLGNtcvlFASLSATLSTKYFG--------LTPGMAGLSVSYALTITEVLNICVRSVSEIESNIVSVERV 1191
Cdd:cd18557 224 GITS----LLIYLSLLLVLWYGgylvlsgqLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
270-547 |
7.23e-10 |
|
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: 61.68 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 270 YLNPILLKQLIDYVsLHDQPLSFGIAIACIMFSCSTTRSL---LQNYQIAGMCRQAVYYqtvLSNAILHKILRLSPSARS 346
Cdd:cd18542 16 LLIPLLIRRIIDSV-IGGGLRELLWLLALLILGVALLRGVfryLQGYLAEKASQKVAYD---LRNDLYDHLQRLSFSFHD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 347 NRTAGEILNHAAVDIEIIVHSVPY-LQNMWSVPFQVTLAMTMLaITLGWAaMAgvCIMILFIPLNLCTS-RFIKLSQQKQ 424
Cdd:cd18542 92 KARTGDLMSRCTSDVDTIRRFLAFgLVELVRAVLLFIGALIIM-FSINWK-LT--LISLAIIPFIALFSyVFFKKVRPAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 425 MKIKDERTKLSN---EMLNGIKVVKLYAWE----ESFEDQINRLRAKEVKMLRnvcILSR---IVD-VANAASPFLVAIG 493
Cdd:cd18542 168 EEIREQEGELNTvlqENLTGVRVVKAFAREdyeiEKFDKENEEYRDLNIKLAK---LLAKywpLMDfLSGLQIVLVLWVG 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 494 SFTCYvlwspdENGLTPS--VAFVALTifNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18542 245 GYLVI------NGEITLGelVAFISYL--WMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1221-1433 |
8.41e-10 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 60.58 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLP--LVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQL---- 1294
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1295 RSKLIIIPQEpvvfsgtlrFNLDPFnqysddqiWNCLE----ICQLKQFAQEDDKT--------------LDRYIAEggk 1356
Cdd:cd03255 81 RRHIGFVFQS---------FNLLPD--------LTALEnvelPLLLAGVPKKERREraeellervglgdrLNHYPSE--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1357 nMSVGERQLLCLcrallrgAR-------IVILDEATASVDTVTDGIVQRAIRQ-HFPQSTTISIA-HRLDTIVDSDRIVV 1427
Cdd:cd03255 141 -LSGGQQQRVAI-------ARalandpkIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVtHDPELAEYADRIIE 212
|
....*.
gi 392896924 1428 LDAGRV 1433
Cdd:cd03255 213 LRDGKI 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
566-780 |
1.03e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 566 NAIVFKNASLNWKGPQNPpVLKDLSATIKPGQLIAIVGSVGGGKSS---LLSAVL------DEMVLLDG----------- 625
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLlpddnpNSKITVDGitltaktvwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 626 RVKVGgsIAYVPQHSWIFNKTIKENILFGNE---LSNYFYDQVVGSCQLKTDFRHFQQGENTmvgengiTLSGGQKARIS 702
Cdd:PRK13640 83 REKVG--IVFQNPDNQFVGATVGDDVAFGLEnraVPRPEMIKIVRDVLADVGMLDYIDSEPA-------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 703 LARAVYQDKDIYLLDDPLSAVDAHvGRALFDKVIGPDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
584-780 |
1.41e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV------LDEMVLLDGRvkvggSIAYVPQHSWIFNK-----------T 646
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLagfeqpTAGQIMLDGV-----DLSHVPPYQRPINMmfqsyalfphmT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQgentMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAH 726
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE----FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 727 VGRALFDKVIgpDGLLR-SKTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK11607 184 LRDRMQLEVV--DILERvGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
567-787 |
1.42e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWkGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSS---LLSAVL---DEMVLLDG-----------RVKV 629
Cdd:PRK13632 7 MIKVENVSFSY-PNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqSGEIKIDGitiskenlkeiRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 630 gGSIAYVPQHSWIfNKTIKENILFGneLSNYFYD-----QVVGSCQLKTDFRHFQQGENtmvgENgitLSGGQKARISLA 704
Cdd:PRK13632 86 -GIIFQNPDNQFI-GATVEDDIAFG--LENKKVPpkkmkDIIDDLAKKVGMEDYLDKEP----QN---LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 705 RAVYQDKDIYLLDDPLSAVDAHvGRALFDKVIGPDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDI---- 780
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIlnnk 233
|
250
....*....|..
gi 392896924 781 -----AYVDGPF 787
Cdd:PRK13632 234 eilekAKIDSPF 245
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
918-1296 |
1.46e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 62.51 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 918 ATLSSVDYLNSTSSVDGPVSvetrLIVYAGFGGLemLLLALAFTVLTIGSL-----RASYGLHSPLIHALLVAPISFFDT 992
Cdd:COG4615 28 ANAGLIALINQALNATGAAL----ARLLLLFAGL--LVLLLLSRLASQLLLtrlgqHAVARLRLRLSRRILAAPLERLER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 993 TPTGRIINRLSRDLDVIdklQDNIRMCTQTLLNACMILV----LISISTPIFLVCAAPLILIyyfVMIYYIPTSRQLKRL 1068
Cdd:COG4615 102 IGAARLLAALTEDVRTI---SQAFVRLPELLQSVALVLGclayLAWLSPPLFLLTLVLLGLG---VAGYRLLVRRARRHL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1069 ESAN----------RSpILSTIAE-SIHGASSIRAFDKTERTTTALSTNVDKFAQCRYLSHMSnrwlatrlelLGNTcVL 1137
Cdd:COG4615 176 RRAReaedrlfkhfRA-LLEGFKElKLNRRRRRAFFDEDLQPTAERYRDLRIRADTIFALANN----------WGNL-LF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1138 FASLSATLstkyFGLtPGMAGLS----VSYALTITEV---LNICVRSVSEIESNIVSVERVNEYQkLEPEAPWRIEKSLE 1210
Cdd:COG4615 244 FALIGLIL----FLL-PALGWADpavlSGFVLVLLFLrgpLSQLVGALPTLSRANVALRKIEELE-LALAAAEPAAADAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1211 NEEKWPVKGKIELDGFSMRYRKNL---PLVLKNIDLKIEGGERIGVIGRTGSGKSSLTM---ALYRmieGESGTIKIDDV 1284
Cdd:COG4615 318 APPAPADFQTLELRGVTYRYPGEDgdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKlltGLYR---PESGEILLDGQ 394
|
410
....*....|..
gi 392896924 1285 EIDTIGLHQLRS 1296
Cdd:COG4615 395 PVTADNREAYRQ 406
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
263-547 |
1.46e-09 |
|
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: 60.89 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 263 LTADIVHYLNPILLKQLIDYVSLHDQPLSFGIAIACIMFSCSTTRSLL---QNYQIAGMCRQAVYYqtvLSNAILHKILR 339
Cdd:cd18541 9 ILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFrflWRYLIFGASRRIEYD---LRNDLFAHLLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 340 LSPSA-RSNRTaGEILNHAAVDIEIIVHSV-PYLQNMWSVPFQVTLAMT-MLAITLGWAAMAgvciMILFIPLNLCTSRF 416
Cdd:cd18541 86 LSPSFyQKNRT-GDLMARATNDLNAVRMALgPGILYLVDALFLGVLVLVmMFTISPKLTLIA----LLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 417 IKLSQQKQMKIKDERTKLSN---EMLNGIKVVKLYAWEES----FEDQINRLRAKEVKMLRNVCILSRIVDVANAASPFL 489
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDrvqESFSGIRVIKAFVQEEAeierFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 490 V-AIGSFtcYVLwspdENGLTPSvAFVALTI-FNQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18541 241 VlWYGGR--LVI----RGTITLG-DLVAFNSyLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1221-1436 |
1.89e-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: 59.13 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGeRIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIdTIGLHQLRSKLII 1300
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEpvvfsgtlrfnldpFNQYSDDQIWNCLE-ICQLKQFAQED-DKTLDRYIAEGG---------KNMSVGERQLLCLC 1369
Cdd:cd03264 77 LPQE--------------FGVYPNFTVREFLDyIAWLKGIPSKEvKARVDEVLELVNlgdrakkkiGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1370 RALLRGARIVILDEATASVDtvtdgIVQR-AIRQHFPQ--STTISI--AHRLDTIVDS-DRIVVLDAGRVAEF 1436
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLD-----PEERiRFRNLLSElgEDRIVIlsTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1221-1403 |
2.03e-09 |
|
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: 59.03 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGlHQLRSKLII 1300
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSG-TLRFNLDpF------NQYSDDQIWNCLEICQLKQFAqeddktlDRYIaeggKNMSVGERQLLCLCRALL 1373
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGLA-------DLPV----RQLSAGQKRRVALARLLL 147
|
170 180 190
....*....|....*....|....*....|
gi 392896924 1374 RGARIVILDEATASVDTVTDGIVQRAIRQH 1403
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
585-780 |
2.06e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 60.24 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSL---LSAVLD----EMvLLDGRVKVGGSIAYVPQH-SWIF---NKTIKENILF 653
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLakmLAGIIEptsgEI-LINGHKLEYGDYKYRCKHiRMIFqdpNTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 654 GNELSnyfydqvvGSCQLKTDF----RHfQQGENT--MVG---ENGI----TLSGGQKARISLARAVYQDKDIYLLDDPL 720
Cdd:COG4167 107 GQILE--------EPLRLNTDLtaeeRE-ERIFATlrLVGllpEHANfyphMLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 721 SAVDAHVgRA----LFDKVIGPDGLlrskTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:COG4167 178 AALDMSV-RSqiinLMLELQEKLGI----SYIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEV 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1190-1281 |
2.10e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1190 RVNEYQKLEPEAPWRIEKSLE---NEEkwPVKGK--IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSl 1264
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTVEirfPPP--ERLGKkvLELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST- 356
|
90 100
....*....|....*....|.
gi 392896924 1265 tmaLYRMIEGE----SGTIKI 1281
Cdd:COG0488 357 ---LLKLLAGElepdSGTVKL 374
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1221-1449 |
2.30e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:PRK13548 3 LEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQepvvfSGTLRFnldPF----------------NQYSDDQIWNCLEICQLKQFAQEDDKTLdryiaeggknmSVGERQ 1364
Cdd:PRK13548 81 LPQ-----HSSLSF---PFtveevvamgraphglsRAEDDALVAAALAQVDLAHLAGRDYPQL-----------SGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1365 ------LLCLCRALLRGARIVILDEATASVDtvtdgivqraIRQhfpQSTTISIAHRL-----DTIV----D-------S 1422
Cdd:PRK13548 142 rvqlarVLAQLWEPDGPPRWLLLDEPTSALD----------LAH---QHHVLRLARQLahergLAVIvvlhDlnlaaryA 208
|
250 260
....*....|....*....|....*..
gi 392896924 1423 DRIVVLDAGRVAEFDTPSNlLLNPDSL 1449
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAE-VLTPETL 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
568-778 |
2.34e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNW--KGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVG--------------- 630
Cdd:PRK13645 7 IILDNVSYTYakKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipanlkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 631 ------GSIAYVPQHSwIFNKTIKENILFG----NELSNYFYDQV---VGSCQLKTDFrhfqqgentmVGENGITLSGGQ 697
Cdd:PRK13645 87 rlrkeiGLVFQFPEYQ-LFQETIEKDIAFGpvnlGENKQEAYKKVpelLKLVQLPEDY----------VKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 698 KARISLARAVYQDKDIYLLDDPLSAVDAHvGRALFDKVIGPDGLLRSKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGS 776
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
...
gi 392896924 777 -FE 778
Cdd:PRK13645 235 pFE 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
570-772 |
2.43e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 570 FKNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG--------------SIAY 635
Cdd:PRK11614 8 FDKVSAHYGKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 636 VPQHSWIFNK-TIKENILFGNelsnYFYDQVVGSCQLKTDFRHFQQGENTMVGENGiTLSGGQKARISLARAVYQDKDIY 714
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGG----FFAERDQFQERIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 715 LLDDPLSAVDAHVGRALFDKVigpdGLLRSK--TRVLVTHNL-QYTKYVDTIYVIEDGQIV 772
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTI----EQLREQgmTIFLVEQNAnQALKLADRGYVLENGHVV 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1222-1434 |
2.64e-09 |
|
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: 58.33 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSMRYRKnlpLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMAL--YRMIEGESGTIKIDDVEIDtigLHQLRSKLI 1299
Cdd:cd03213 12 TVKSSPSKSGK---QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 IIPQEPVVFSG-TLRFNLDpfnqysddqiwncleicqlkqfaqeddktldrYIAEgGKNMSVGERQLLCLCRALLRGARI 1378
Cdd:cd03213 86 YVPQDDILHPTlTVRETLM--------------------------------FAAK-LRGLSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 1379 VILDEATASVDTVTDGIVQRAIRQHFPQSTTISIA-HRLDTIVDS--DRIVVLDAGRVA 1434
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSiHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1221-1448 |
3.04e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.48 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLV--LKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEG-E---SGTIKIDDVEIDTI---GL 1291
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLlErptSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1292 HQLRSKLIIIPQepvvfsgtlRFNLdpFNQ---------------YSDDQIwncleicqlKQFAQE-------DDKtLDR 1349
Cdd:COG1135 78 RAARRKIGMIFQ---------HFNL--LSSrtvaenvalpleiagVPKAEI---------RKRVAEllelvglSDK-ADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1350 YIAEggknMSVGERQllclcrallrgaRI-----------VIL-DEATASVD--TvTDGIVQ--RAIRQHFpQSTTISIA 1413
Cdd:COG1135 137 YPSQ----LSGGQKQ------------RVgiaralannpkVLLcDEATSALDpeT-TRSILDllKDINREL-GLTIVLIT 198
|
250 260 270
....*....|....*....|....*....|....*.
gi 392896924 1414 HRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNPDS 1448
Cdd:COG1135 199 HEMDVVRRiCDRVAVLENGRIVEQGPVLDVFANPQS 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
585-775 |
3.29e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 58.53 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------SIAYVPQHSWIFNK-TIKENI 651
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 LFGNELSNYFYDQVVGscQLKTDFRHFQQGE--NTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGR 729
Cdd:cd03266 100 EYFAGLYGLKGDELTA--RLEELADRLGMEEllDRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 392896924 730 ALFDKVigpdGLLRS--KTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHG 775
Cdd:cd03266 174 ALREFI----RQLRAlgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1221-1294 |
3.44e-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: 56.69 E-value: 3.44e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEidTIG-LHQL 1294
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--KIGyFEQL 71
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
584-772 |
3.45e-09 |
|
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: 57.44 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSL---LSAVL--DEmvlldGRVKVGGSIAYV--PQHSWifnktikenilfgne 656
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLmkiLSGLYkpDS-----GEILVDGKEVSFasPRDAR--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 657 lsnyfydqvvgscqlktdfrhfqqgentmvgENGIT----LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALF 732
Cdd:cd03216 74 -------------------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 392896924 733 dKVIgpdGLLRS--KTRVLVTHNLQYTKYV-DTIYVIEDGQIV 772
Cdd:cd03216 123 -KVI---RRLRAqgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
568-783 |
3.46e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.79 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNW-KG-PQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG-------------- 631
Cdd:PRK13646 3 IRFDNVSYTYqKGtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 ---SIAYVPQ--HSWIFNKTIKENILFGNELSNYFYDQVVGSC-QLKTDFRHfqqgENTMVGENGITLSGGQKARISLAR 705
Cdd:PRK13646 83 vrkRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAhRLLMDLGF----SRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 706 AVYQDKDIYLLDDPLSAVDAHVGRALFdKVIGPDGLLRSKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGS----FEDI 780
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVM-RLLKSLQTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSpkelFKDK 237
|
...
gi 392896924 781 AYV 783
Cdd:PRK13646 238 KKL 240
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
271-546 |
3.62e-09 |
|
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: 59.72 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 271 LNPILLKQLIDYVSLHDQP--------LSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYqtvLSNAILHKILRLSP 342
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGgggvdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYD---LRKDLFEKLQRLPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 343 SARSNRTAGEILNHAAVDIEIIVHSvpyLQNmwSVPfQVTLAMTMLAITLgwAAMAGV-----CIMILFIPLNLCTSRFI 417
Cdd:cd18547 94 SYFDTHSHGDIMSRVTNDVDNISQA---LSQ--SLT-QLISSILTIVGTL--IMMLYIsplltLIVLVTVPLSLLVTKFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 418 -KLSQ---QKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFEDQINRLRAKevkmLRNVCILSRIvdVANAASPFLVAIG 493
Cdd:cd18547 166 aKRSQkyfRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEE----LYKASFKAQF--YSGLLMPIMNFIN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 494 SFTcYVLwspdengltpsVAFV--------ALTI-----F----NQLRQPMRMVANLINTLVQARVSNKR 546
Cdd:cd18547 240 NLG-YVL-----------VAVVggllvingALTVgviqaFlqysRQFSQPINQISQQINSLQSALAGAER 297
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1237-1445 |
3.65e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLH-QLRSKLIIIPQEPVVFSGTLRFN 1315
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1316 ldpfNQYSDDQIWNCLEICQLKQFAQE--DDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTD 1393
Cdd:PRK10895 98 ----NLMAVLQIRDDLSAEQREDRANElmEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1394 GIVQRAIrQHFPQS---TTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSNLLLN 1445
Cdd:PRK10895 174 IDIKRII-EHLRDSglgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1221-1442 |
3.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKN----LPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEI-DTIGLHQLR 1295
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1296 SKLIIIPQEP------------VVFsGTLRFNLDPfnqysdDQIWNCLEICqLKQFAQEDDKTLDRYIAEGgknmsvGER 1363
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAF-GPENLGIPP------EEIRERVDES-LKKVGMYEYRRHAPHLLSG------GQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1364 QLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQS--TTISIAHRLDTIVDSDRIVVLDAGRVAEFDTPSN 1441
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 392896924 1442 L 1442
Cdd:PRK13633 231 I 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1237-1427 |
4.46e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVV---FSG--- 1310
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVrqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1311 --------TLRFnlDPFNQYSDDQIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLCLCRALLRGARIVILD 1382
Cdd:PRK09536 98 vemgrtphRSRF--DTWTETDRAAVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392896924 1383 EATASVDtvtdgiVQRAIRqhfpqstTISIAHRLdtiVDSDRIVV 1427
Cdd:PRK09536 165 EPTASLD------INHQVR-------TLELVRRL---VDDGKTAV 193
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
567-780 |
4.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.46 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWkGPQNP---PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------ 631
Cdd:PRK13641 2 SIKFENVDYIY-SPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 -------SIAYVPQHSWIFNKTIKENILFGNElsNY-FYDQVVGSCQLKTdFRHFQQGENtMVGENGITLSGGQKARISL 703
Cdd:PRK13641 81 kklrkkvSLVFQFPEAQLFENTVLKDVEFGPK--NFgFSEDEAKEKALKW-LKKVGLSED-LISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 704 ARAVYQDKDIYLLDDPLSAVDAHVGRALFDkvIGPDGLLRSKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1447 |
5.37e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.98 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEP--VVFSGTL--RFNLDPFNQ-YSDDQIWN----CLEICQLKQFAQEDDKTLdryiaeggknmSVGERQLLCLCRA 1371
Cdd:PRK13647 84 VFQDPddQVFSSTVwdDVAFGPVNMgLDKDEVERrveeALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1372 LLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIA-HRLDTIVD-SDRIVVLDAGRVAEFDTPSnLLLNPD 1447
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTDED 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
569-780 |
5.42e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.36 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 569 VFKNASLNWKGPQNPP----VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVG-------------- 630
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 631 ------GSIAYVPQhSWIFNKTIKENILFGNElsNYFYDqvvgscqlKTDFRHFQQGENTMVG-------ENGITLSGGQ 697
Cdd:PRK13643 81 pvrkkvGVVFQFPE-SQLFEETVLKDVAFGPQ--NFGIP--------KEKAEKIAAEKLEMVGladefweKSPFELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 698 KARISLARAVYQDKDIYLLDDPLSAVD--AHVGRALFDKVIGPDGllrsKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQH 774
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDpkARIEMMQLFESIHQSG----QTVVLVTHLMdDVADYADYVYLLEKGHIISC 225
|
....*.
gi 392896924 775 GSFEDI 780
Cdd:PRK13643 226 GTPSDV 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
546-725 |
5.90e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 546 RLRQFLN-------DEEMERKTEVALGNAIVFKNASLnwKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLD 618
Cdd:COG4178 334 RLAGFEEaleaadaLPEAASRIETSEDGALALEDLTL--RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 619 emvlL----DGRVKV--GGSIAYVPQHSWIFNKTIKENILFGN---ELSNYFYDQVVGSCQLkTDFR-HFQQGENTmvge 688
Cdd:COG4178 412 ----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYPAtaeAFSDAELREALEAVGL-GHLAeRLDEEADW---- 482
|
170 180 190
....*....|....*....|....*....|....*..
gi 392896924 689 nGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:COG4178 483 -DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
585-776 |
6.44e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS------------IAYVPQhswiFNK-----TI 647
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQ----FDNldpdfTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 648 KENIL-FGNelsnYF---YDQVVGSCQLKTDFRHFQQGENTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:PRK13537 98 RENLLvFGR----YFglsAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 392896924 724 DAHVGRALFDKVigPDGLLRSKTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHGS 776
Cdd:PRK13537 170 DPQARHLMWERL--RSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGA 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
575-790 |
6.71e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.55 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 575 LNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSL---LSAVL---DEMVLLDG-------------RVKVGgsIAY 635
Cdd:PRK13639 7 LKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILkptSGEVLIKGepikydkksllevRKTVG--IVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 636 VPQHSWIFNKTIKENILFG--------NELSNYFYDQvvgscqLKTdfrhfqqgentmVGENGIT------LSGGQKARI 701
Cdd:PRK13639 85 QNPDDQLFAPTVEEDVAFGplnlglskEEVEKRVKEA------LKA------------VGMEGFEnkpphhLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 702 SLARAVYQDKDIYLLDDPLSAVD----AHVGRALFDkvIGPDGLlrskTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHGS 776
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYD--LNKEGI----TIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
250
....*....|....*...
gi 392896924 777 ----FEDIAYVDGPFGRL 790
Cdd:PRK13639 221 pkevFSDIETIRKANLRL 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1220-1442 |
7.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.64 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1220 KIELDGFSMRYRKNLPL---VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIdtigLHQLRS 1296
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI----THKTKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1297 KLI--IIPQEPVVFsgtlRFnldPFNQYSDDQIWNCLEICQlKQFAQEDDKTLDR-------------YIAEGGKNMSVG 1361
Cdd:PRK13646 78 KYIrpVRKRIGMVF----QF---PESQLFEDTVEREIIFGP-KNFKMNLDEVKNYahrllmdlgfsrdVMSQSPFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1362 ERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDT 1438
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTS 229
|
....
gi 392896924 1439 PSNL 1442
Cdd:PRK13646 230 PKEL 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
585-863 |
9.33e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKV--GGSIAYVPQHSWIFNKTIKENILFGNELSNYFY 662
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakGIKLGYFAQHQLEFLRADESPLQHLARLAPQEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 663 DQvvgscQLKTDFRHFQ-QGENtmVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIGPDGL 741
Cdd:PRK10636 407 EQ-----KLRDYLGGFGfQGDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 742 LrsktrVLVTHN---LQYTkyVDTIYVIEDGQIvqhgsfediayvdGPF-GRLwsecENSDEDVADEEAESSEASVTPPv 817
Cdd:PRK10636 480 L-----VVVSHDrhlLRST--TDDLYLVHDGKV-------------EPFdGDL----EDYQQWLSDVQKQENQTDEAPK- 534
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 392896924 818 pvlENGDNGAIEKSSQiDRTNSHFSEKSRKSEEKPQKVEKNVENVQ 863
Cdd:PRK10636 535 ---ENNANSAQARKDQ-KRREAELRTQTQPLRKEIARLEKEMEKLN 576
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1230-1428 |
1.04e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1230 YRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFS 1309
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1310 GTLRFNLD-PF---NQYSDDQIWncleICQLKQFAQeDDKTLDRYIAEggknMSVGERQLLCLCRALLRGARIVILDEAT 1385
Cdd:PRK10247 95 DTVYDNLIfPWqirNQQPDPAIF----LDDLERFAL-PDTILTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392896924 1386 ASVD----TVTDGIVQRAIRQHfpQSTTISIAHRLDTIVDSDRIVVL 1428
Cdd:PRK10247 166 SALDesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1238-1446 |
1.08e-08 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.04 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIG---LHQLRSKLIiipqePVVFSgtlRF 1314
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKKI-----SMVFQ---SF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLDPfNQYSDDQIWNCLEIC-------------QLKQFAQEDDKtlDRYIAEggknMSVGERQLLCLCRALLRGARIVIL 1381
Cdd:cd03294 112 ALLP-HRTVLENVAFGLEVQgvpraereeraaeALELVGLEGWE--HKYPDE----LSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1382 DEATASVDTVTDGIVQ----RAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNP 1446
Cdd:cd03294 185 DEAFSALDPLIRREMQdellRLQAEL--QKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1237-1447 |
1.37e-08 |
|
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: 57.30 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQL-RSKLIIIPQEPVVFSG-TLRF 1314
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLdpfnqysddqiwncleicQLKQFAQEDDKTLDRYIAE---------------GGkNMSVGERQLLclcrallrgA--- 1376
Cdd:COG0410 98 NL------------------LLGAYARRDRAEVRADLERvyelfprlkerrrqrAG-TLSGGEQQML---------Aigr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1377 ------RIVILDEATAS-----VDTVTDGIvqRAIRQhfpQSTTI-------SIAHRLdtivdSDRIVVLDAGRVAEFDT 1438
Cdd:COG0410 150 almsrpKLLLLDEPSLGlapliVEEIFEII--RRLNR---EGVTIllveqnaRFALEI-----ADRAYVLERGRIVLEGT 219
|
....*....
gi 392896924 1439 PSNLLLNPD 1447
Cdd:COG0410 220 AAELLADPE 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
578-775 |
1.56e-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: 56.50 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 578 KGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVldeMVLLDGRVKVGGSIAYVPQHSWIFNKTIKENILFGNEL 657
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL---ANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 658 SNYFYDQVVGscqlKT-DFRHFQQGeNTMVgeNGItlSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVgrAL-FDKV 735
Cdd:cd03233 92 DVHFPTLTVR----ETlDFALRCKG-NEFV--RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSST--ALeILKC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 392896924 736 IgpdgllRSKTRVLVTHNL--------QYTKYVDTIYVIEDGQIVQHG 775
Cdd:cd03233 161 I------RTMADVLKTTTFvslyqasdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1237-1443 |
1.68e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.33 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSG-TLR-- 1313
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1314 --FNLDPFNQY-----SDDQ--IWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLCLCRALLRGARIVILDEA 1384
Cdd:PRK11231 97 vaYGRSPWLSLwgrlsAEDNarVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1385 TASVDTVTDGIVQRAIRQHFPQ-STTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLL 1443
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
545-719 |
1.89e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 545 KRLRQflndEEMERKtEVaLGNA------------IVF--KNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKS 610
Cdd:PRK11147 289 KALRR----ERSERR-EV-MGTAkmqveeasrsgkIVFemENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKT 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 611 SLLSAVLDEMVLLDGRVKVGG--SIAYVPQHSWIFN--KTIKENILFGNE--LSNYFYDQVVGSCQlktDFRHFQQGENT 684
Cdd:PRK11147 360 TLLKLMLGQLQADSGRIHCGTklEVAYFDQHRAELDpeKTVMDNLAEGKQevMVNGRPRHVLGYLQ---DFLFHPKRAMT 436
|
170 180 190
....*....|....*....|....*....|....*
gi 392896924 685 MVGengiTLSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:PRK11147 437 PVK----ALSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1221-1454 |
2.00e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLV---LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIG----LHQ 1293
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1294 LRSKLIIIPQEP--VVFSGT----LRFNLDPFNQYSDDQIWNCLEICQLKQFAQEddktldrYIAEGGKNMSVGERQLLC 1367
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETvlkdVAFGPQNFGIPKEKAEKIAAEKLEMVGLADE-------FWEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1368 LCRALLRGARIVILDEATASVDTVTDGIVQRAIRQ-HFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLN 1445
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
....*....
gi 392896924 1446 PDSLYSQLL 1454
Cdd:PRK13643 235 VDFLKAHEL 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1189-1443 |
2.04e-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: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1189 ERVNEYQKLEPEapwrIEKSLENEEKWPVkgkIELDGFSMRY---RKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLT 1265
Cdd:TIGR03269 255 EVVAVFMEGVSE----VEKECEVEVGEPI---IKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1266 MALYRMIEGESGT--IKIDDVEIDT--------------IG-LHQLRSkliIIPQEPVVFSGTLRFNLD-PfnqysdDQI 1327
Cdd:TIGR03269 328 KIIAGVLEPTSGEvnVRVGDEWVDMtkpgpdgrgrakryIGiLHQEYD---LYPHRTVLDNLTEAIGLElP------DEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1328 WNCLEICQLKQFAQEDDKT---LDRYIAEggknMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAI---R 1401
Cdd:TIGR03269 399 ARMKAVITLKMVGFDEEKAeeiLDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaR 474
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 392896924 1402 QHFPQsTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLL 1443
Cdd:TIGR03269 475 EEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
539-731 |
2.24e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.41 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 539 QARvSNKRLRQF--LNDEEMERKTEVA---------LGNAIV-FKNASlnwKGPQNPPVLKDLSATIKPGQLIAIVGSVG 606
Cdd:TIGR03719 283 QAK-SKARLARYeeLLSQEFQKRNETAeiyippgprLGDKVIeAENLT---KAFGDKLLIDDLSFKLPPGGIVGVIGPNG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 607 GGKSSLLSAVLDEMVLLDGRVKVGGS--IAYVPQ--HSWIFNKTIKENILFGNELsnyfydQVVGSCQLKT-------DF 675
Cdd:TIGR03719 359 AGKSTLFRMITGQEQPDSGTIEIGETvkLAYVDQsrDALDPNKTVWEEISGGLDI------IKLGKREIPSrayvgrfNF 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 676 RHFQQGEntMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRAL 731
Cdd:TIGR03719 433 KGSDQQK--KVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
322-547 |
2.32e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 57.52 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 322 AVYYQTVLSNAILHKIL------------RLSPSARSNRTAGEILNHAAVDIEIIvhsvpylQNmwsvpFQVTLAMTMLA 389
Cdd:cd18564 70 ASYAGTYLTALVGQRVVldlrrdlfahlqRLSLSFHDRRRTGDLLSRLTGDVGAI-------QD-----LLVSGVLPLLT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 390 ITLGWAAMAGVC---------IMILFIP-LNLCTSRF---IKLSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFED 456
Cdd:cd18564 138 NLLTLVGMLGVMfwldwqlalIALAVAPlLLLAARRFsrrIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEER 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 457 QINR---------LRAKEVKMLrnvciLSRIVDVanaaspfLVAIGsfTCYVLW----SPDENGLTPSVAFVALTIFNQL 523
Cdd:cd18564 218 RFARenrkslragLRAARLQAL-----LSPVVDV-------LVAVG--TALVLWfgawLVLAGRLTPGDLLVFLAYLKNL 283
|
250 260
....*....|....*....|....
gi 392896924 524 RQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18564 284 YKPVRDLAKLTGRIAKASASAERV 307
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
585-780 |
2.83e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.42 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVL------DEMVLLDGRVKVGGS-----IAYVPQHSWIF-NKTIKENIL 652
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAglekptEGQIFIDGEDVTHRSiqqrdICMVFQSYALFpHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 653 FGNELsnyfydQVVGSCQLKT---------DFRHFqqgENTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:PRK11432 101 YGLKM------LGVPKEERKQrvkealelvDLAGF---EDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 724 DAHVGRALFDKVigpdgllR------SKTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK11432 168 DANLRRSMREKI-------RelqqqfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
584-780 |
2.96e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.65 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV-----LDE-MVLLDGRVkvggsIAYVP----------QHSWIF-NKT 646
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIagfetPDSgRIMLDGQD-----ITHVPaenrhvntvfQSYALFpHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELsnyfydQVVGSCQLKTdfRHFQ-----QGENtMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLS 721
Cdd:PRK09452 103 VFENVAFGLRM------QKTPAAEITP--RVMEalrmvQLEE-FAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 722 AVDA-----------HVGRALfdkvigpdGLlrskTRVLVTHN----LQYTkyvDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK09452 174 ALDYklrkqmqnelkALQRKL--------GI----TFVFVTHDqeeaLTMS---DRIVVMRDGRIEQDGTPREI 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
584-726 |
3.01e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLL---SAVLDE---MVLLDG-----------RVKVggsiAYVPQHSWIFNKT 646
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLkivASLISPtsgTLLFEGedistlkpeiyRQQV----SYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 647 IKENILFGNELSNyfydQVVGSCQLKTDFRHFQQGENTMvgENGIT-LSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:PRK10247 97 VYDNLIFPWQIRN----QQPDPAIFLDDLERFALPDTIL--TKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
.
gi 392896924 726 H 726
Cdd:PRK10247 171 S 171
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
586-776 |
3.02e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLSA---------VLDEMVLLDGRvKVGGSI-----AYVPQHSwIFNK--TIKE 649
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAlafrspkgvKGSGSVLLNGM-PIDAKEmraisAYVQQDD-LFIPtlTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGNEL---SNYFYDQVVGSC-QLKTDFRhFQQGENTMVGENGIT--LSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTKKEKRERVdEVLQALG-LRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 724 DA----HVGRALFDKVigpdglLRSKTRVLVTHNLQYTKY--VDTIYVIEDGQIVQHGS 776
Cdd:TIGR00955 198 DSfmaySVVQVLKGLA------QKGKTIICTIHQPSSELFelFDKIILMAEGRVAYLGS 250
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1221-1433 |
3.25e-08 |
|
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: 55.75 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGlhqlRSKLII 1300
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEpvvfSGTlrfnldpfnqYSDDQIwncleICQLKQFAQ-------EDDKTLDRYIAEGG---------KNMSVGERQ 1364
Cdd:cd03269 75 LPEE----RGL----------YPKMKV-----IDQLVYLAQlkglkkeEARRRIDEWLERLElseyankrvEELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1365 LLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISI-AHRLDTIVD-SDRIVVLDAGRV 1433
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1237-1435 |
3.27e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.23 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMAL-----YRMIEGEsgtIKIDDVEIDTIGLHQlRSKLIII--PQEPVVFS 1309
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkYEVTEGE---ILFKGEDITDLPPEE-RARLGIFlaFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1310 GTlrfnldpfnqysddqiwncleicqlkqfaqeddKTLD--RYIAEGgknMSVGERQLLCLCRALLRGARIVILDEATAS 1387
Cdd:cd03217 91 GV---------------------------------KNADflRYVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1388 VDTVTDGIVQRAIRQ-HFPQSTTISIAH--RLDTIVDSDRIVVLDAGRVAE 1435
Cdd:cd03217 135 LDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1216-1435 |
4.63e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 55.87 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1216 PVKGKIELDGFSMRY--RKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLtmaLyRMIEG----ESGTIKIDDVEIdti 1289
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL---L-RLIAGlekpTSGEVLVDGKPV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1290 glHQLRSKLIIIPQEP-----------VVFSgtLRFNLDPFNQYsDDQIWNCLEICQLKQFAqeddktlDRYIAEggknM 1358
Cdd:COG1116 76 --TGPGPDRGVVFQEPallpwltvldnVALG--LELRGVPKAER-RERARELLELVGLAGFE-------DAYPHQ----L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1359 SVGERQllclcrallRGARIVILDEATASVDTVTDGIVQ---RAIRQHFPQsTTISIAHrlDtiVD-----SDRIVVLDA 1430
Cdd:COG1116 140 SGGMRQrvaiaralaNDPEVLLMDEPFGALDALTRERLQdelLRLWQETGK-TVLFVTH--D--VDeavflADRVVVLSA 214
|
....*..
gi 392896924 1431 --GRVAE 1435
Cdd:COG1116 215 rpGRIVE 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1221-1438 |
4.73e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYrknlPLV--LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDD--VEIDT-------- 1288
Cdd:COG3845 6 LELRGITKRF----GGVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1289 IG-LHQ---LRSKL-----IIIPQEPvvfSGTLRFNLDPFNQysddqiwncleicQLKQFAQE-----DdktLDRYIAEg 1354
Cdd:COG3845 82 IGmVHQhfmLVPNLtvaenIVLGLEP---TKGGRLDRKAARA-------------RIRELSERygldvD---PDAKVED- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1355 gknMSVGERQLLCLCRALLRGARIVILDEATAsvdtV-----TD---GIVQRAIRQhfpQSTTISIAHRLDTIVD-SDRI 1425
Cdd:COG3845 142 ---LSVGEQQRVEILKALYRGARILILDEPTA----VltpqeADelfEILRRLAAE---GKSIIFITHKLREVMAiADRV 211
|
250
....*....|....
gi 392896924 1426 VVLDAGR-VAEFDT 1438
Cdd:COG3845 212 TVLRRGKvVGTVDT 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
585-781 |
4.84e-08 |
|
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: 55.52 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEM------VLLDG----------RVKVGgsIAYVPQHSWIFNK-TI 647
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptsgsVLFDGeditglppheIARLG--IGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 648 KENILFGNEL-SNYFYDQVVGSCQLKT---------DFRHFQQGENTMVGEngitLSGGQKARISLARAVYQDKDIYLLD 717
Cdd:cd03219 93 LENVMVAAQArTGSGLLLARARREEREareraeellERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 718 DP---LSAVDAHVGRALFDKVIGpdgllRSKTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDIA 781
Cdd:cd03219 169 EPaagLNPEETEELAELIRELRE-----RGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
584-780 |
4.87e-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: 55.86 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLS--------AVLDEMVLLdGRVKVGGSIAyvpqhswifnkTIKENI-LFG 654
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSlitgdlppTYGNDVRLF-GERRGGEDVW-----------ELRKRIgLVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 655 NELSNYFYD-----QVVGSCqlKTD----FRHFQQGE----NTMVGENGI---------TLSGGQKARISLARAVYQDKD 712
Cdd:COG1119 85 PALQLRFPRdetvlDVVLSG--FFDsiglYREPTDEQreraRELLELLGLahladrpfgTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 713 IYLLDDPLSAVDAHvGRALFDKVIgpDGLLRS--KTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG1119 163 LLILDEPTAGLDLG-ARELLLALL--DKLAAEgaPTLVLVTHHVEEiPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
585-780 |
4.87e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGSIAYVPQHSWIFNK-TIKENILFGNELSNYF-- 661
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVGMVFQQPNPFph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 662 ---YDQVvgSCQLKT----DFRHFQQGENTMVGENGI-------------TLSGGQKARISLARAVYQDKDIYLLDDPLS 721
Cdd:PRK14246 105 lsiYDNI--AYPLKShgikEKREIKKIVEECLRKVGLwkevydrlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 722 AVDAhVGRALFDKVIGPdgLLRSKTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK14246 183 MIDI-VNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1237-1447 |
5.21e-08 |
|
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: 55.52 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQlRSKLIIIP--QEPVVFSG-TLR 1313
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1314 FNLD---------------PFNQYSD--DQIWNCLEICQLKQFAQEddktldryIAEggkNMSVGERQLLCLCRALLRGA 1376
Cdd:cd03219 94 ENVMvaaqartgsglllarARREEREarERAEELLERVGLADLADR--------PAG---ELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896924 1377 RIVILDEATASVDTV-TDGIVQ--RAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRV-AEfDTPSNLLLNPD 1447
Cdd:cd03219 163 KLLLLDEPAAGLNPEeTEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRViAE-GTPDEVRNNPR 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1221-1450 |
5.25e-08 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 55.32 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLtmalYRMIEG----ESGTIKIDDVEIDTIGLHQLRS 1296
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGfetpTSGEILLDGKDITNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1297 KLI-----IIPQ----EPVVFSGTLRfNLDPfnQYSDDQIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLC 1367
Cdd:cd03300 75 NTVfqnyaLFPHltvfENIAFGLRLK-KLPK--AEIKERVAEALDLVQLEGYA-------NRKPSQ----LSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1368 LCRALLRGARIVILDEATASVDTVTDGIVQRAIR--QHFPQSTTISIAH-RLDTIVDSDRIVVLDAGRVAEFDTPSNLLL 1444
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKrlQKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
....*.
gi 392896924 1445 NPDSLY 1450
Cdd:cd03300 221 EPANRF 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1221-1282 |
5.33e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.47 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYR---------KNLPL-----------VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIK 1280
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslKELLLrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
..
gi 392896924 1281 ID 1282
Cdd:COG1134 85 VN 86
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
586-780 |
5.34e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSS---LLSAVLDE---MVLLDG-----------RVKVGGSIAYVPQH-SWIFNKTI 647
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPtrgQVLIDGvdiakisdaelREVRRKKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 648 KENILFGNELSNYFYDQVvgscQLKTDFRHFQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHV 727
Cdd:PRK10070 124 LDNTAFGMELAGINAEER----REKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 392896924 728 GRALFDKVIGPDGlLRSKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK10070 200 RTEMQDELVKLQA-KHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1237-1441 |
6.42e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGEsGTIKIDDVEIDTIGLHQL---RSKLIIIPQEP-------- 1305
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1306 ----VVFSGtLRFNLDPFNQYSDDQiwncleicQLKQFAQE---DDKTLDRYIAEggknMSVGERQLLCLCRALLRGARI 1378
Cdd:PRK15134 380 nvlqIIEEG-LRVHQPTLSAAQREQ--------QVIAVMEEvglDPETRHRYPAE----FSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1379 VILDEATASVD-TVTDGIVQ--RAIRQHFpQSTTISIAHRLDtIVDS--DRIVVLDAGRVAE-------FDTPSN 1441
Cdd:PRK15134 447 IILDEPTSSLDkTVQAQILAllKSLQQKH-QLAYLFISHDLH-VVRAlcHQVIVLRQGEVVEqgdcervFAAPQQ 519
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
584-780 |
6.57e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSaVLDEMVLLD-GRVKVGGS--------------IAYVPQHSWIF-NKTI 647
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMK-IIAGIVPPDsGTLEIGGNpcarltpakahqlgIYLVPQEPLLFpNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 648 KENILFGNELSNYFYDQVVG-----SCQLKTDfrhFQQGentmvgengiTLSGGQKARISLARAVYQDKDIYLLDDPLSA 722
Cdd:PRK15439 104 KENILFGLPKRQASMQKMKQllaalGCQLDLD---SSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 723 VDAHVGRALFDKVigpdGLLRSKTR--VLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK15439 171 LTPAETERLFSRI----RELLAQGVgiVFISHKLpEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1221-1434 |
7.13e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 54.68 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPLV--LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLhQLRSKL 1298
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSG-TLRFNLDPFNQYSDdqiwncLEICQLKQFAQEDDKTLD--RYIAEGGKNMSVGERQLLCLCRALLRG 1375
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLYG------LKGDELTARLEELADRLGmeELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1376 ARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIA-HRLDTIVD-SDRIVVLDAGRVA 1434
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1221-1449 |
7.16e-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: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEGE-----SGTIKIDDVEIDTIGLHQLR 1295
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLL----SLITGDlpptyGNDVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1296 SKL---------IIIPQEP---VVFSGtlRFN-LDPFNQYSDDQI---WNCLEICQLKQFAqeddktlDRYIAEggknMS 1359
Cdd:COG1119 78 KRIglvspalqlRFPRDETvldVVLSG--FFDsIGLYREPTDEQReraRELLELLGLAHLA-------DRPFGT----LS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1360 VGERQLLCLcrallrgAR-------IVILDEATASVDTVTDGIVQRAIRQ--HFPQSTTISIAHRLDTIVDS-DRIVVLD 1429
Cdd:COG1119 145 QGEQRRVLI-------ARalvkdpeLLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLK 217
|
250 260
....*....|....*....|
gi 392896924 1430 AGRVAEfDTPSNLLLNPDSL 1449
Cdd:COG1119 218 DGRVVA-AGPKEEVLTSENL 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1238-1456 |
7.31e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEID----TIGLHQLRSKLIIIPQ--EPVVFSGT 1311
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1312 LRFNLD--PFNQYSDDQIWNCLEICQLKQFAQEDDktldrYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVD 1389
Cdd:PRK13641 103 VLKDVEfgPKNFGFSEDEAKEKALKWLKKVGLSED-----LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1390 TVTdgivQRAIRQHFPQ-----STTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNPDSLYSQLLNE 1456
Cdd:PRK13641 178 PEG----RKEMMQLFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLDE 246
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
579-772 |
8.16e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.04 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 579 GPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEMVllDGRVKVGGS----------IAYVPQH-SWIFNK 645
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcLDKPT--SGTYRVAGQdvatldadalAQLRREHfGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 -------TIKENIlfgnelsnyfydqVVGSCQLKTDFRHFQQGENTMVGENGI---------TLSGGQKARISLARAVYQ 709
Cdd:PRK10535 95 yhllshlTAAQNV-------------EVPAVYAGLERKQRLLRAQELLQRLGLedrveyqpsQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 710 DKDIYLLDDPLSAVDAHVGralfDKVIGPDGLLRSK--TRVLVTHNLQYTKYVDTIYVIEDGQIV 772
Cdd:PRK10535 162 GGQVILADEPTGALDSHSG----EEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
948-1137 |
8.27e-08 |
|
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: 55.53 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 948 FGGLEMLLLALAFTVLTIG----SLRASYGLHSPLI----HALLVAPISFFDTTPTGRIINRLSrDldvIDKLQDNI-RM 1018
Cdd:cd18570 43 IISIGLILLYLFQSLLSYIrsylLLKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRFN-D---ANKIREAIsST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1019 CTQTLLNACMILV----LISISTPIFLVCAAPlILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFD 1094
Cdd:cd18570 119 TISLFLDLLMVIIsgiiLFFYNWKLFLITLLI-IPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLN 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 392896924 1095 KTERTTTALSTNVDKFAQCRY-LSHMSNR--WLATRLELLGNTCVL 1137
Cdd:cd18570 198 AEEQFLKKIEKKFSKLLKKSFkLGKLSNLqsSIKGLISLIGSLLIL 243
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
271-547 |
8.57e-08 |
|
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: 55.53 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 271 LNPILLKQLIDYVsLHDQPLSFGIAIACIMFSCSTTRSLL---QNYQIAgmcRQAVYYQTVLSNAILHKILRLSPSARSN 347
Cdd:cd18570 20 AGSFFFQILIDDI-IPSGDINLLNIISIGLILLYLFQSLLsyiRSYLLL---KLSQKLDIRLILGYFKHLLKLPLSFFET 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 348 RTAGEIL---NHAAVDIEIIVHSVPylqnmwSVPFQVTLAMTMLAI------TLGWAAMAGVCIMILFIplnLCTSRFIK 418
Cdd:cd18570 96 RKTGEIIsrfNDANKIREAISSTTI------SLFLDLLMVIISGIIlffynwKLFLITLLIIPLYILII---LLFNKPFK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 419 LSQQKQMKIKDERTKLSNEMLNGIKVVKLYAWEESFedqINRLRAKEVKMLRNVCILSRIVDVANAASPFLVAIGSFTcy 498
Cdd:cd18570 167 KKNREVMESNAELNSYLIESLKGIETIKSLNAEEQF---LKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLL-- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 499 VLWSPD----ENGLTPS--VAFVALTIFnqLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18570 242 ILWIGSylviKGQLSLGqlIAFNALLGY--FLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
580-725 |
8.91e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 580 PQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLS--AVLDEMVLLDGRVKVGGSIAYVPQHSWI-FNKTIKENILFG-- 654
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRimAGVDKDFNGEARPQPGIKVGYLPQEPQLdPTKTVRENVEEGva 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 655 ---------NELSNYF------YDQVV---GSCQLKTDFRHFQQGENTM----------VGENGIT-LSGGQKARISLAR 705
Cdd:TIGR03719 95 eikdaldrfNEISAKYaepdadFDKLAaeqAELQEIIDAADAWDLDSQLeiamdalrcpPWDADVTkLSGGERRRVALCR 174
|
170 180
....*....|....*....|
gi 392896924 706 AVYQDKDIYLLDDPLSAVDA 725
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDA 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
568-779 |
9.36e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWkgPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRV----KVggSIAYVPQHSwif 643
Cdd:PLN03073 509 ISFSDASFGY--PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKV--RMAVFSQHH--- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 nktikeniLFGNELSnyfydqvvgSCQLKTDFRHF----QQGENTMVGENGI----------TLSGGQKARISLARAVYQ 709
Cdd:PLN03073 582 --------VDGLDLS---------SNPLLYMMRCFpgvpEQKLRAHLGSFGVtgnlalqpmyTLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 710 DKDIYLLDDP-----LSAVDAHV-GRALFDkvigpDGLLrsktrvLVTHNLQY-TKYVDTIYVIEDGQIVQ-HGSFED 779
Cdd:PLN03073 645 KPHILLLDEPsnhldLDAVEALIqGLVLFQ-----GGVL------MVSHDEHLiSGSVDELWVVSEGKVTPfHGTFHD 711
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
566-775 |
1.00e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 566 NAIVFKNasLNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGSIAYVPQHSWI--- 642
Cdd:PRK13647 3 NIIEVED--LHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrsk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 643 ------------FNKTIKENILFG---NELSNYFYDQVVGSCqLKT----DFRHfqqgentmvgENGITLSGGQKARISL 703
Cdd:PRK13647 81 vglvfqdpddqvFSSTVWDDVAFGpvnMGLDKDEVERRVEEA-LKAvrmwDFRD----------KPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 704 ARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVigpDGL-LRSKTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHG 775
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL---DRLhNQGKTVIVATHDVDLAaEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1219-1459 |
1.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1219 GKIELDGFSMRYRKNLPL---VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTiGLHQ-- 1293
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPA-NLKKik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1294 ----LRSKLIIIPQEP--VVFSGTLRFNL--DPFNQYSDDQ--IWNCLEICQLKQFAQEddktldrYIAEGGKNMSVGER 1363
Cdd:PRK13645 84 evkrLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQeaYKKVPELLKLVQLPED-------YVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1364 QLLCLCRALLRGARIVILDEATASVDTVTD----GIVQRAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDT 1438
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERLNKEY--KKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
250 260 270
....*....|....*....|....*....|.
gi 392896924 1439 P----------SNLLLNPDSLYSQLLNEKNR 1459
Cdd:PRK13645 235 PfeifsnqellTKIEIDPPKLYQLMYKLKNK 265
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
592-776 |
1.12e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.20 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 592 TIKPGQLIAIVGSVGGGKSSLLS------AVLDEMVLLDGRVKVGGSIAYVP-----QHSWIFNK-TIKENILFGnelsn 659
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNliagflTPASGSLTLNGQDHTTTPPSRRPvsmlfQENNLFSHlTVAQNIGLG----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 660 yfydqVVGSCQLKTDFRHFQQgenTMVGENGIT---------LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAhvgrA 730
Cdd:PRK10771 96 -----LNPGLKLNAAQREKLH---AIARQMGIEdllarlpgqLSGGQRQRVALARCLVREQPILLLDEPFSALDP----A 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392896924 731 LFDKVIgpdGLL------RSKTRVLVTHNLQ-YTKYVDTIYVIEDGQIVQHGS 776
Cdd:PRK10771 164 LRQEML---TLVsqvcqeRQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGP 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
586-770 |
1.14e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSL---LSAV-----LDEMVLLDGRVKVGGSI---------------AYVPQhswi 642
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVyphgtYEGEIIFEGEELQASNIrdteragiaiihqelALVKE---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 643 fnKTIKENILFGNELSNYF---YDQVVGSC-----QLKTDFrhfqqGENTMVGEngitLSGGQKARISLARAVYQDKDIY 714
Cdd:PRK13549 97 --LSVLENIFLGNEITPGGimdYDAMYLRAqkllaQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 715 LLDDPLSAVDAHVGRALFDKVIGpdglLRSK--TRVLVTHNLQYTKYV-DTIYVIEDGQ 770
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRD----LKAHgiACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
584-732 |
1.16e-07 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 53.52 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------SIAYVPQHSWIFNK-TIKEN 650
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 651 ILFGNELSNYfYDQVVGSCQLKTDFRHFqqgENTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHvGRA 730
Cdd:TIGR01189 94 LHFWAAIHGG-AQRTIEDALAAVGLTGF---EDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVA 164
|
..
gi 392896924 731 LF 732
Cdd:TIGR01189 165 LL 166
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
584-752 |
1.31e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMvlldgRVKVGGSIAYVPQHSWIFNKTIKENILFGNELSNYFYd 663
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-----KGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 664 qVVGSCQL------KTDFRHfqqgentmvgengitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVig 737
Cdd:COG2401 118 -LLNAVGLsdavlwLRRFKE---------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL-- 179
|
170
....*....|....*...
gi 392896924 738 pdGLL---RSKTRVLVTH 752
Cdd:COG2401 180 --QKLarrAGITLVVATH 195
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
566-780 |
1.36e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 566 NAIVFKNASLNWKGPQnPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRV-------------KVGGS 632
Cdd:PRK13648 6 SIIVFKNVSFQYQSDA-SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 633 IAYV---PQHSWIfNKTIKENILFGNELSNYFYDQVVGSC-QLKTDFRHFQQGENtmvgeNGITLSGGQKARISLARAVY 708
Cdd:PRK13648 85 IGIVfqnPDNQFV-GSIVKYDVAFGLENHAVPYDEMHRRVsEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 709 QDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSK--TRVLVTHNLQYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLV---RKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
584-736 |
1.64e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.34 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVK----------VGGSIAYV-PQHSWIFNKTIKENIL 652
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddpdVAEACHYLgHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 653 FgnelsnyfydqvvgscqlktdFRHFQQGENTM-------VGENGIT------LSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:PRK13539 96 F---------------------WAAFLGGEELDiaaaleaVGLAPLAhlpfgyLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|....*..
gi 392896924 720 LSAVDAHvGRALFDKVI 736
Cdd:PRK13539 155 TAALDAA-AVALFAELI 170
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
585-774 |
1.67e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSavldemvLLDG-RVKVGGSIAYVPQHSWIFNKTIK---ENILFG------ 654
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLH-------LLGGlDTPTSGDVIFNGQPMSKLSSAAKaelRNQKLGfiyqfh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 655 ------NELSNYFYDQVVGscqlKTDFRHFQQGENTMVGENGIT---------LSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:PRK11629 97 hllpdfTALENVAMPLLIG----KKKPAEINSRALEMLAAVGLEhranhrpseLSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 720 LSAVDAHVGRALFDkVIGPDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQH 774
Cdd:PRK11629 173 TGNLDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1449 |
1.81e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLP---LVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIdTIG-----LH 1292
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI-TAGkknkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1293 QLRSKLIIIPQ--EPVVFSGTLR----FNLDPFNQYSDDQiwncleicqlKQFAQE-------DDKTLDRYIAEggknMS 1359
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEkdicFGPMNFGVSEEDA----------KQKAREmielvglPEELLARSPFE----LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1360 VGERQLLCLCRALLRGARIVILDEATASVDTVTdgivQRAIRQHF------PQSTTISIAHRLDTIVD-SDRIVVLDAGR 1432
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGT 223
|
250
....*....|....*..
gi 392896924 1433 VAEFDTPSNLLLNPDSL 1449
Cdd:PRK13634 224 VFLQGTPREIFADPDEL 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1237-1446 |
2.16e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKID--------DV-EIDTIglhQLRSKLIIIPQEPVV 1307
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfgkDIfQIDAI---KLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1308 FS-----GTLRFNLDPFNQYSDDQIWNCLEICQLKQFAQEDdkTLDRyIAEGGKNMSVGERQLLCLCRALLRGARIVILD 1382
Cdd:PRK14246 102 FPhlsiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKE--VYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1383 EATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNP 1446
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
568-780 |
2.23e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.32 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNAS--LNWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLL------------------------------SA 615
Cdd:PRK13651 3 IKVKNIVkiFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtgtiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 616 VLDEMVLLDGRVK-------VGGSIAYVPQHS--WIFNKTIKENILFG-----------NELSNYfYDQVVGscqLKTDF 675
Cdd:PRK13651 83 VLEKLVIQKTRFKkikkikeIRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvskeeaKKRAAK-YIELVG---LDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 676 rhfqqgentmVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAH-VGRAL--FDKVigpdgLLRSKTRVLVTH 752
Cdd:PRK13651 159 ----------LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILeiFDNL-----NKQGKTIILVTH 223
|
250 260 270
....*....|....*....|....*....|..
gi 392896924 753 N----LQYTKYVdtiYVIEDGQIVQHGSFEDI 780
Cdd:PRK13651 224 DldnvLEWTKRT---IFFKDGKIIKDGDTYDI 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1221-1295 |
2.54e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.42 E-value: 2.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1221 IELDGFSMRYRKNLPLV--LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLR 1295
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELR 78
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1237-1282 |
2.78e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.07 E-value: 2.78e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEGE----SGTIKID 1282
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLL----KILAGElepdSGEVSIP 58
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
592-775 |
5.06e-07 |
|
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: 52.80 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 592 TIKPGQLIAIVGSVGGGKSSLLSavldemvLLDGRVK--------VGGSIAYVPQHSWIFNKTIKENILFgnELSNYFYD 663
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIK-------MLAGVLKpdegdieiELDTVSYKPQYIKADYEGTVRDLLS--SITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 664 QvvgsCQLKTDFRHFQQGENTMvgENGI-TLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHvGRALFDKVIGPDGLL 742
Cdd:cd03237 92 H----PYFKTEIAKPLQIEQIL--DREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAEN 164
|
170 180 190
....*....|....*....|....*....|...
gi 392896924 743 RSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHG 775
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNG 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1221-1433 |
5.38e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.78 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPL---VLKNIDLKIEGGERIGVIGRTGSGKSSltmaLYRMIEGE----SGTIKIDDVEIDTIGLHQ 1293
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIAGSlppdSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1294 lRSKLII-IPQEPVvfSGT---------------------LRFNLDPfnqysddqiwncleicQLKQFAQEDDKTL---- 1347
Cdd:COG1101 78 -RAKYIGrVFQDPM--MGTapsmtieenlalayrrgkrrgLRRGLTK----------------KRRELFRELLATLglgl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1348 -DRYIAEGGkNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIV----QRAIRQHfpQSTTISIAHRL-DTIVD 1421
Cdd:COG1101 139 eNRLDTKVG-LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTHNMeQALDY 215
|
250
....*....|..
gi 392896924 1422 SDRIVVLDAGRV 1433
Cdd:COG1101 216 GNRLIMMHEGRI 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
566-780 |
6.57e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 566 NAIVFKNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSaVLDEMVLLDGRVKVGGSIAYVPQHSW---- 641
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 642 ----------------IFNKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTM--VGENGITLSGGQKARISL 703
Cdd:PRK14247 78 ielrrrvqmvfqipnpIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKdrLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 704 ARAVYQDKDIYLLDDPLSAVD----AHVgRALFDKvigpdgLLRSKTRVLVTH-NLQYTKYVDTIYVIEDGQIVQHGSFE 778
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDpentAKI-ESLFLE------LKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTR 230
|
..
gi 392896924 779 DI 780
Cdd:PRK14247 231 EV 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1220-1435 |
6.75e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1220 KIELDGFSMRYRKNlPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRsKLI 1299
Cdd:PRK10522 322 TLELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYR-KLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1300 iipqePVVFSGTLRFN--LDPFNQYSDDQI---WncLEICQLKQFAQEDDKTLDRYiaeggkNMSVGERQLLCLCRALLR 1374
Cdd:PRK10522 400 -----SAVFTDFHLFDqlLGPEGKPANPALvekW--LERLKMAHKLELEDGRISNL------KLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896924 1375 GARIVILDEATASVDTVtdgivqraIRQHFPQ----------STTISIAHRLDTIVDSDRIVVLDAGRVAE 1435
Cdd:PRK10522 467 ERDILLLDEWAADQDPH--------FRREFYQvllpllqemgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1237-1448 |
8.57e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEI----DTIG---------LHQLRSKLIIIPQ 1303
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrDKDGqlkvadknqLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1304 EpvvfsgtlrFNLDPFNQYSDDQIWNCLEICQL-KQFAQE-----------DDKTLDRYIAeggkNMSVGERQLLCLCRA 1371
Cdd:PRK10619 100 H---------FNLWSHMTVLENVMEAPIQVLGLsKQEAREravkylakvgiDERAQGKYPV----HLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 1372 LLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQ-STTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNPDS 1448
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1449 |
8.69e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.11 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLII 1300
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEP--VVFSGTLRFNL--DPFNQYSDDQiwncleicQLKQFAQEDDKTL--DRYIAEGGKNMSVGERQLLCLCRALLR 1374
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEE--------TVAHRVSSALHMLglEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 1375 GARIVILDEATASVDTVTDGIVQRAIRQhFPQS---TTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNPDSL 1449
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLND-LPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1237-1440 |
8.70e-07 |
|
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: 53.27 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMAL-----YRMIEG----------ESGTI---------------KIDDVEI 1286
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqYEPTSGriiyhvalceKCGYVerpskvgepcpvcggTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1287 DTIGL-----HQLRSKLIIIPQEpvvfsgtlrfnldPFNQYSDDQ-IWNCLEicQLKQFAQEDDKTLDR----------- 1349
Cdd:TIGR03269 95 DFWNLsdklrRRIRKRIAIMLQR-------------TFALYGDDTvLDNVLE--ALEEIGYEGKEAVGRavdliemvqls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1350 -YIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQS--TTISIAHRLDTIVD-SDRI 1425
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKA 239
|
250
....*....|....*
gi 392896924 1426 VVLDAGRVAEFDTPS 1440
Cdd:TIGR03269 240 IWLENGEIKEEGTPD 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1240-1455 |
1.01e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1240 NIDLKieGGERIGVIGRTGSGKSSLTMALYRMIEGE---SGTIKIDDVEIDTI---GLHQLRSKLI-IIPQEPVVfsgtl 1312
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLpekELNKLRAEQIsMIFQDPMT----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1313 rfNLDPFNQYSdDQIwncLEICQL-----KQFA-QEDDKTLDRY-IAEGGKNM-------SVGERQLLCLCRALLRGARI 1378
Cdd:PRK09473 109 --SLNPYMRVG-EQL---MEVLMLhkgmsKAEAfEESVRMLDAVkMPEARKRMkmyphefSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1379 VILDEATASVDtVTdgiVQRAI-------RQHFpQSTTISIAHRLDTIVDS-DRIVVLDAGRVAEFDTPSNLLLNPDSLY 1450
Cdd:PRK09473 183 LIADEPTTALD-VT---VQAQImtllnelKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
....*.
gi 392896924 1451 SQ-LLN 1455
Cdd:PRK09473 258 SIgLLN 263
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
986-1099 |
1.19e-06 |
|
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: 52.00 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 986 PISFFDTTPTGRIINRLSRDldvIDKLQDnirMCTQTLLN--------ACMILVLISISTPIFLVCAAPLILIyYFVMIY 1057
Cdd:cd18544 88 PLSFFDRTPVGRLVTRVTND---TEALNE---LFTSGLVTligdllllIGILIAMFLLNWRLALISLLVLPLL-LLATYL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 392896924 1058 YIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERT 1099
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKRE 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
586-780 |
1.41e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIK---PGQLI-AIVGSVGGGKSSLLSA------------VLDEMVLLDGRVKVG-----GSIAYVPQHSWIF- 643
Cdd:PRK11144 10 LGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAisgltrpqkgriVLNGRVLFDAEKGIClppekRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENILFG--NELSNYFyDQVVGSCQLKTDFRHFQqgentmvgengITLSGGQKARISLARAVYQDKDIYLLDDPLS 721
Cdd:PRK11144 90 HYKVRGNLRYGmaKSMVAQF-DKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 722 AVDAHVGRALFD------KVIgpdgllrsKTRVL-VTHNLQ-YTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK11144 158 SLDLPRKRELLPylerlaREI--------NIPILyVSHSLDeILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
943-1093 |
1.63e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 51.39 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 943 IVYAGFGGLEMLLLALAFTvltigslRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLD-VIDKLQDNIRMCTQ 1021
Cdd:cd18572 47 VLSGLFSGLRGGCFSYAGT-------RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQkVSDPLSTNLNVFLR 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1022 TLLNACMILV-LISISTPIFLVCAA---PLILIYYFVMIYYIPTSRQL-KRLESANrspilSTIAESIHGASSIRAF 1093
Cdd:cd18572 120 NLVQLVGGLAfMFSLSWRLTLLAFItvpVIALITKVYGRYYRKLSKEIqDALAEAN-----QVAEEALSNIRTVRSF 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1238-1450 |
1.65e-06 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 50.80 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLtmalYRMIEG----ESGTIKIDDVeiDTIGLHQLRSKLIIIPQEPVVFSG-TL 1312
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGlerpDSGTILFGGE--DATDVPVQERNVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1313 RFNL-----------DPFNQYSDDQIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLCLCRALLRGARIVIL 1381
Cdd:cd03296 92 FDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLA-------DRYPAQ----LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1382 DEATASVDTVTDGIVQRAIRQ--HFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNPDSLY 1450
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1238-1431 |
1.73e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGlHQLRSKL--IIIPQE-PVVFSGTLRF 1314
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLdPFNQYSDDQIW--NCLEICQLKQFAQE--DDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASvdt 1390
Cdd:PRK09700 100 NL-YIGRHLTKKVCgvNIIDWREMRVRAAMmlLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS--- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 392896924 1391 VTDGIVQR---AIRQHFPQSTTI-SIAHRLDTIVD-SDRIVVLDAG 1431
Cdd:PRK09700 176 LTNKEVDYlflIMNQLRKEGTAIvYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1237-1434 |
1.81e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDD---VEIDTIGLHQLrsKLIIIPQEPVVFSG-TL 1312
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTPAKAHQL--GIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1313 RFNLD---PFNQYSDDQIWNCLEI--CQLKQFAQEddKTLDryiaeggknmsVGERQLLCLCRALLRGARIVILDEATAS 1387
Cdd:PRK15439 104 KENILfglPKRQASMQKMKQLLAAlgCQLDLDSSA--GSLE-----------VADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392896924 1388 VDTV-TDGIVQRaIRQHFPQSTTIS-IAHRLDTIVD-SDRIVVLDAGRVA 1434
Cdd:PRK15439 171 LTPAeTERLFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIA 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
585-784 |
2.19e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS-------------IAYVPQHSWI-FNKTIKEN 650
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 651 ILFGNELSNYFY--------DQVVGSCQlktdfrhfQQGENTMVGENGITLSGGQKARISLARAVYQDKDIYLLDDPLSA 722
Cdd:PRK10253 102 VARGRYPHQPLFtrwrkedeEAVTKAMQ--------ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 723 VDAHVGRALFDKVigpDGLLRSK--TRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDIAYVD 784
Cdd:PRK10253 174 LDISHQIDLLELL---SELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
581-782 |
2.37e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 581 QNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEM--------VLLDGRV---KVGGSIAYVPQHSWIF-NKTIK 648
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgtILANNRKptkQILKRTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENILF------GNELSN----YFYDQVVGSCQLKtdfrhfqQGENTMVGENGIT-LSGGQKARISLARAVYQDKDIYLLD 717
Cdd:PLN03211 159 ETLVFcsllrlPKSLTKqekiLVAESVISELGLT-------KCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 718 DPLSAVDAHVGRALFDKVIGpdglLRSKTRVLVTHNLQYTKYV----DTIYVIEDGQIVQHGSFED-IAY 782
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGS----LAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSDaMAY 297
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
585-780 |
2.62e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.61 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV-----LDEMVLLDGRVKVGGSIAYVP---------QHSWIF------- 643
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPdvdpievrrEVGMVFqypnpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENILFGNELSNYF-----YDQVVGSCQLKTDFrhFQQGENTMVGENGiTLSGGQKARISLARAVYQDKDIYLLDD 718
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVkskkeLDERVEWALKKAAL--WDEVKDRLNDYPS-NLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 719 PLSAVDAhVGRALFDKVIGPdgLLRSKTRVLVTHN-LQYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK14267 176 PTANIDP-VGTAKIEELLFE--LKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
586-772 |
2.99e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSL---LSAV-----LDEMVLLDGRVKVGGS--------IAYVPQH-SWIFNKTIK 648
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVyphgtWDGEIYWSGSPLKASNirdteragIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENILFGNELSN----YFYDQVVGSCQ-LKTDFRHFQQGENTMVGENGitlsGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:TIGR02633 97 ENIFLGNEITLpggrMAYNAMYLRAKnLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392896924 724 DAHVGRALFDkvIGPDGLLRSKTRVLVTHNLQYTKYV-DTIYVIEDGQIV 772
Cdd:TIGR02633 173 TEKETEILLD--IIRDLKAHGVACVYISHKLNEVKAVcDTICVIRDGQHV 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
586-776 |
4.58e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.09 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSS---LLSAVLDE---MVLLDG-----------RVKVGgSIAYVPQHSWIfNKTIK 648
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFEEfegKVKIDGelltaenvwnlRRKIG-MVFQNPDNQFV-GATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 649 ENILFGNELSNYFYDQV---VGSCQLKTDFRHFQQGENTmvgengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:PRK13642 101 DDVAFGMENQGIPREEMikrVDEALLAVNMLDFKTREPA-------RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392896924 726 hVGRALFDKVIGPDGLLRSKTRVLVTHNLQYTKYVDTIYVIEDGQIVQHGS 776
Cdd:PRK13642 174 -TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1237-1449 |
4.95e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQE-PVVFSGTLRfN 1315
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVR-E 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1316 LDPFNQYSddqiWNCleicQLKQFAQEDDKTLDRYIAEGG---------KNMSVGERQLLCLCRALLRGARIVILDEATA 1386
Cdd:PRK10575 105 LVAIGRYP----WHG----ALGRFGAADREKVEEAISLVGlkplahrlvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1387 SVDTVTD----GIVQRAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNlLLNPDSL 1449
Cdd:PRK10575 177 ALDIAHQvdvlALVHRLSQER--GLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAE-LMRGETL 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
585-780 |
5.62e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLL------------SAVLDEMVLLDGRVKV-GGSIAYVPQH-SWIFNKTIKEN 650
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLkmlgrhqppsegEILLDAQPLESWSSKAfARKVAYLPQQlPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 651 ILFGNelsnYFYDQVVGSCQlKTDFRHFQQGEnTMVGENGI------TLSGGQKARISLARAVYQDKDIYLLDDPLSAVD 724
Cdd:PRK10575 106 VAIGR----YPWHGALGRFG-AADREKVEEAI-SLVGLKPLahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 725 -AHVGRALfdKVIGPDGLLRSKTRVLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK10575 180 iAHQVDVL--ALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1237-1455 |
5.95e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRM-----IEGESGTIKI---DDVEIDTIGLHQLR-SKLIIIPQEPVV 1307
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFhgeSLLHASEQTLRGVRgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1308 fsgtlrfNLDPFN------------------QYSDDQIWNCLEICQLKQFAQEddktldryIAEGGKNMSVGERQLLCLC 1369
Cdd:PRK15134 104 -------SLNPLHtlekqlyevlslhrgmrrEAARGEILNCLDRVGIRQAAKR--------LTDYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1370 RALLRGARIVILDEATASVD-TVTDGIVQ--RAIRQHFPQStTISIAHRLDtIVD--SDRIVVLDAGRVAEFDTPSNLLL 1444
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDvSVQAQILQllRELQQELNMG-LLFITHNLS-IVRklADRVAVMQNGRCVEQNRAATLFS 246
|
250
....*....|..
gi 392896924 1445 NPDSLYS-QLLN 1455
Cdd:PRK15134 247 APTHPYTqKLLN 258
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
693-775 |
6.57e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.24 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 693 LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFD--KVIGPDGLlrskTRVLVTHNLQYTKYVDT--IYvIED 768
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSiiRELAETGI----TQVIVTHEVEVARKTASrvVY-MEN 216
|
....*..
gi 392896924 769 GQIVQHG 775
Cdd:PRK11124 217 GHIVEQG 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1222-1434 |
6.58e-06 |
|
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: 48.83 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSMryrknlplvlkNIDLKIEGgERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDD-VEIDT---IGLHQLRSK 1297
Cdd:cd03297 9 RLPDFTL-----------KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtVLFDSrkkINLPPQQRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1298 LIIIPQEPVVFSG-TLRFNLD---PFNQYSDDQIwNCLEICQLKQFaqedDKTLDRYIAEggknMSVGERQLLCLCRALL 1373
Cdd:cd03297 77 IGLVFQQYALFPHlNVRENLAfglKRKRNREDRI-SVDELLDLLGL----DHLLNRYPAQ----LSGGEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1374 RGARIVILDEATASVDTVTDGIVQ---RAIRQHFpQSTTISIAHRLDTIVD-SDRIVVLDAGRVA 1434
Cdd:cd03297 148 AQPELLLLDEPFSALDRALRLQLLpelKQIKKNL-NIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1237-1448 |
6.93e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 48.94 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDdveidtiGLHQLRSKLII--IPQEP-VVFSgtlR 1313
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-------GLKVNDPKVDErlIRQEAgMVFQ---Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1314 FNLDPFNQYSDDQIWNCLEICQL-KQFAQEDDKTL----------DRYIAEggknMSVGERQLLCLCRALLRGARIVILD 1382
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVRGAsKEEAEKQARELlakvglaeraHHYPSE----LSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1383 EATASVDTVTDGIVQRAIRQHFPQSTT-------ISIAHRLDTivdsdRIVVLDAGRVAEFDTPSNLLLNPDS 1448
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTmvivtheIGFAEKVAS-----RLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
563-780 |
7.12e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.32 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 563 ALGNAIVFKNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEMV---LLDGRVKVGGSIAYVP 637
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKT---VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVsgyRYSGDVLLGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 638 QHSWIFNKTIKENILFGNELSNYFYDQVVGSCQL-----KTDFRHFQQGENTMVG----------ENGITLSGGQKARIS 702
Cdd:PRK14271 94 RDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAhklvpRKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 703 LARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVigpDGLLRSKTRVLVTHNL-QYTKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1220-1279 |
9.93e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.31 E-value: 9.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1220 KIELDGFSMRYRKNLPLVLK---NIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTI 1279
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1204-1435 |
1.06e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1204 RIEKSLENEEKWPVKGKIELDGFSMRYRKNLPLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEG--ESGTIKI 1281
Cdd:COG2401 12 RVTKVYSSVLDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1282 DDVEIDtiglhqlrSKLIIIPQEPVvfsgtlrfnLDPFNQ---------YSDDQIWncleicqlkqfaqeddktLDRYia 1352
Cdd:COG2401 92 PDNQFG--------REASLIDAIGR---------KGDFKDavellnavgLSDAVLW------------------LRRF-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1353 eggKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIV----QRAIRQHfpQSTTISIAHRLDTIVD--SDRIV 1426
Cdd:COG2401 135 ---KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVarnlQKLARRA--GITLVVATHHYDVIDDlqPDLLI 209
|
....*....
gi 392896924 1427 VLDAGRVAE 1435
Cdd:COG2401 210 FVGYGGVPE 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1254-1439 |
1.12e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1254 IGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTiGLHQLRSKLIIIPQEPVVFSGTLRFNLDPFNQYSDDQIWnclEI 1333
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW---EE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1334 CQLKQFAQEDDKTLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISIA 1413
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST 1117
|
170 180
....*....|....*....|....*..
gi 392896924 1414 HRLDTI-VDSDRIVVLDAGRVAEFDTP 1439
Cdd:TIGR01257 1118 HHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1222-1447 |
1.17e-05 |
|
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: 48.50 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSMRYRKnlpLV-LKNIDLKIEGGERIGVIGRTGSGKSSLtmalYRMIEGE----SGTIKIDDVEIDTIGLHQlRS 1296
Cdd:COG0411 6 EVRGLTKRFGG---LVaVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLITGFyrptSGRILFDGRDITGLPPHR-IA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1297 KL--------------------IIIPQEPVVFSGTLRFNLDPFNQYSD-----DQIWNCLEICQLKQFAqeddktlDRYI 1351
Cdd:COG0411 78 RLgiartfqnprlfpeltvlenVLVAAHARLGRGLLAALLRLPRARREerearERAEELLERVGLADRA-------DEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1352 AeggkNMSVGERQLLCLCRALLRGARIVILDEATASVDTV-TDGIVQ--RAIRQHFpqSTTIS-IAHRLDTIVD-SDRIV 1426
Cdd:COG0411 151 G----NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAEliRRLRDER--GITILlIEHDMDLVMGlADRIV 224
|
250 260
....*....|....*....|..
gi 392896924 1427 VLDAGRV-AEfDTPSNLLLNPD 1447
Cdd:COG0411 225 VLDFGRViAE-GTPAEVRADPR 245
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
951-1098 |
1.19e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 49.05 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 951 LEMLLLALAFTVLTIG--------SLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVI-----DKLQDnir 1017
Cdd:cd18563 47 LGLAGAYVLSALLGILrgrllarlGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLqdflsDGLPD--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1018 MCTQTLLNACMILVLISISTPIFLVCAAPLILIYYFVMIYYiPTSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTE 1097
Cdd:cd18563 124 FLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFW-KKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEK 202
|
.
gi 392896924 1098 R 1098
Cdd:cd18563 203 R 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
578-771 |
1.26e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.24 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 578 KGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLS--AVLD-----EMVLL---------DGRVKV-GGSIAYVPQhS 640
Cdd:PRK10584 18 QGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAilAGLDdgssgEVSLVgqplhqmdeEARAKLrAKHVGFVFQ-S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 641 WIFNKTIK--ENI----LFGNELSNYFYDQVVGSCQlktdfrhfQQGENTMVGENGITLSGGQKARISLARAVYQDKDIY 714
Cdd:PRK10584 97 FMLIPTLNalENVelpaLLRGESSRQSRNGAKALLE--------QLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 715 LLDDPLSAVDAHVGRALFDkvigpdgLLRSKTR------VLVTHNLQYTKYVDTIYVIEDGQI 771
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIAD-------LLFSLNRehgttlILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
539-731 |
1.27e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 539 QARvSNKRLRQF--LNDEEMERKTEVA---------LGNAIV-FKNASlnwKGPQNPPVLKDLSATIKPGQLIAIVGSVG 606
Cdd:PRK11819 285 QAK-SKARLARYeeLLSEEYQKRNETNeifippgprLGDKVIeAENLS---KSFGDRLLIDDLSFSLPPGGIVGIIGPNG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 607 GGKSSLLSAVLDEMVLLDGRVKVGGS--IAYVPQH--SWIFNKTIKENILFGNE---LSNYfydQV-----VGSCQLK-T 673
Cdd:PRK11819 361 AGKSTLFKMITGQEQPDSGTIKIGETvkLAYVDQSrdALDPNKTVWEEISGGLDiikVGNR---EIpsrayVGRFNFKgG 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 674 DfrhfQQgenTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRAL 731
Cdd:PRK11819 438 D----QQ---KKVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL 484
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1238-1446 |
1.39e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.23 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMieGE-------SGTIKIDDVEI-----DTIglhQLRSKLIIIPQEP 1305
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM--NDlnpevtiTGSIVYNGHNIysprtDTV---DLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1306 VVFSGTLRFNLD---PFNQYSDDQIWNCLEICQLKQfAQEDDKTLDRyIAEGGKNMSVGERQLLCLCRALLRGARIVILD 1382
Cdd:PRK14239 96 NPFPMSIYENVVyglRLKGIKDKQVLDEAVEKSLKG-ASIWDEVKDR-LHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1383 EATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNP 1446
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1221-1438 |
1.42e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLtMalyRMIEG----ESGTIKID--DVEIDTIgLHQL 1294
Cdd:COG1129 5 LEMRGISKSFGGVK--ALDGVSLELRPGEVHALLGENGAGKSTL-M---KILSGvyqpDSGEILLDgePVRFRSP-RDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1295 RSKLIIIPQEPVVF-----------------SGTLRFNldpfnqysddqiwncleicQLKQFAQEddkTLDRYiaegG-- 1355
Cdd:COG1129 78 AAGIAIIHQELNLVpnlsvaeniflgreprrGGLIDWR-------------------AMRRRARE---LLARL----Gld 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1356 -------KNMSVGERQLLCLCRALLRGARIVILDEATAS-----VDTVTDgIVQR------AIrqhfpqsttISIAHRLD 1417
Cdd:COG1129 132 idpdtpvGDLSVAQQQLVEIARALSRDARVLILDEPTASltereVERLFR-IIRRlkaqgvAI---------IYISHRLD 201
|
250 260
....*....|....*....|...
gi 392896924 1418 TIVD-SDRIVVL-DAGRVAEFDT 1438
Cdd:COG1129 202 EVFEiADRVTVLrDGRLVGTGPV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
693-780 |
1.57e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 49.30 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 693 LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVgRAlfdKVIgpdGLLRS--KTR----VLVTHNLQYTKYV-DTIYV 765
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-QA---QIL---DLLRDlqREHglayLFISHDLAVVRALaHRVMV 498
|
90
....*....|....*
gi 392896924 766 IEDGQIVQHGSFEDI 780
Cdd:COG4172 499 MKDGKVVEQGPTEQV 513
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
271-547 |
1.76e-05 |
|
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: 48.28 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 271 LNPILLKQLIDYVSL---HDQPLSFGIAIACIMFSCSTTrSLLQNYQIAGMcrqavyyQTVLSNAILH----KILRLSPS 343
Cdd:cd18555 20 LIPILTQYVIDNVIVpgnLNLLNVLGIGILILFLLYGLF-SFLRGYIIIKL-------QTKLDKSLMSdffeHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 344 ARSNRTAGEILNHAavdieiivHSVPYLQNMWS------------VPFqVTLAMTMLAITLGWAAMAGVCIMILFIplnL 411
Cdd:cd18555 92 FFENRSSGDLLFRA--------NSNVYIRQILSnqvisliidlllLVI-YLIYMLYYSPLLTLIVLLLGLLIVLLL---L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 412 CTSRFIKLSQQKQMKIKDERTKLSNEMLNGIKVVK--------LYAWEESFEDQINRLRAKEVKMLrnvcILSRIVDVAN 483
Cdd:cd18555 160 LTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKWENLFKKQLKAFKKKERLSN----ILNSISSSIQ 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 484 AASPFLV-AIGSFtcYVLwspdENGLT--PSVAFVALTIfnqlrQPMRMVANLINT---LVQARVSNKRL 547
Cdd:cd18555 236 FIAPLLIlWIGAY--LVI----NGELTlgELIAFSSLAG-----SFLTPIVSLINSynqFILLKSYLERL 294
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
576-776 |
1.89e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.31 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 576 NWKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------------------ 631
Cdd:PRK13631 32 DEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpyskkiknf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 632 -----SIAYV---PQHSwIFNKTIKENILFG-----------NELSNYFYDQVvgscQLKTDFrhfqqgentmVGENGIT 692
Cdd:PRK13631 112 kelrrRVSMVfqfPEYQ-LFKDTIEKDIMFGpvalgvkkseaKKLAKFYLNKM----GLDDSY----------LERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 693 LSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVGRALFDKVIgpDGLLRSKTRVLVTHNLQYTKYV-DTIYVIEDGQI 771
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIL--DAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKI 254
|
....*
gi 392896924 772 VQHGS 776
Cdd:PRK13631 255 LKTGT 259
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1237-1459 |
2.59e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.16 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLtmalYRMIEG----ESGTIKIDDVeiDTIGLHQLRSKLIIIPQEPVVF---- 1308
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGlehqTSGHIRFHGT--DVSRLHARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1309 -SGTLRFNLD-------PFNQYSDDQIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLCLCRALLRGARIVI 1380
Cdd:PRK10851 91 vFDNIAFGLTvlprrerPNAAAIKAKVTQLLEMVQLAHLA-------DRYPAQ----LSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1381 LDEATASVDTVTDGIVQRAIRQ-H----FpqsTTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLLNPDSLYS-QL 1453
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQlHeelkF---TSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPATRFVlEF 236
|
....*.
gi 392896924 1454 LNEKNR 1459
Cdd:PRK10851 237 MGEVNR 242
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1221-1435 |
2.60e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.29 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGlHQLRSKLII 1300
Cdd:PRK13536 42 IDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQ-EPVVFSGTLRFNLDPFNQY---SDDQIWNCleICQLKQFAQEDDKTlDRYIAEggknMSVGERQLLCLCRALLRGA 1376
Cdd:PRK13536 119 VPQfDNLDLEFTVRENLLVFGRYfgmSTREIEAV--IPSLLEFARLESKA-DARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1377 RIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISI-------AHRLdtivdSDRIVVLDAGR-VAE 1435
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRkIAE 253
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
953-1099 |
2.71e-05 |
|
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: 47.85 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 953 MLLLALAFTVLTIGSLRASYG---------------LHSPLIHALLVAPISFFDTTPTGRIINRLSRDldvIDKLQDnir 1017
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLriylmakvgqrilydLRQDLFSHLQKLSFSFFDSRPVGKILSRVIND---VNSLSD--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1018 MCTQTLLN--------ACMILVLISISTPIFLVCAA--PLILIyyfVMIYYIPTSRQLKRLESANRSPILSTIAESIHGA 1087
Cdd:cd18545 113 LLSNGLINlipdlltlVGIVIIMFSLNVRLALVTLAvlPLLVL---VVFLLRRRARKAWQRVRKKISNLNAYLHESISGI 189
|
170
....*....|..
gi 392896924 1088 SSIRAFDKTERT 1099
Cdd:cd18545 190 RVIQSFAREDEN 201
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
942-1108 |
3.05e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 47.63 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGfGGLEMLLLALAFTvltIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVI-DKLQDNIRMCT 1020
Cdd:cd18780 49 LGVVLI-GSIATFLRSWLFT---LAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLqNAVTVNLSMLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1021 QTLLNACM-ILVLISIS---TPIFLVCAAPLILIyyfVMIYyiptSRQLKRL------ESANRspilSTIAE-SIHGASS 1089
Cdd:cd18780 125 RYLVQIIGgLVFMFTTSwklTLVMLSVVPPLSIG---AVIY----GKYVRKLskkfqdALAAA----STVAEeSISNIRT 193
|
170
....*....|....*....
gi 392896924 1090 IRAFDKTERTTTALSTNVD 1108
Cdd:cd18780 194 VRSFAKETKEVSRYSEKIN 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1239-1442 |
3.10e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.10 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1239 KNIDLKIEGGERIGVIGRTGSGKSSLtmalYRMIEG----ESGTIKIDDVEIDTIglhqlrskliiipqEP------VVF 1308
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTL----LRMIAGlediTSGDLFIGEKRMNDV--------------PPaergvgMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1309 -SGTLRFNLDPFNQYS-------------DDQIWNCLEICQLkqfaqedDKTLDRYiaegGKNMSVGERQLLCLCRALLR 1374
Cdd:PRK11000 82 qSYALYPHLSVAENMSfglklagakkeeiNQRVNQVAEVLQL-------AHLLDRK----PKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1375 GARIVILDEATASVDTVTDgiVQRAI---RQHFP-QSTTISIAH-RLDTIVDSDRIVVLDAGRVAEFDTPSNL 1442
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALR--VQMRIeisRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1237-1454 |
3.18e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.37 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTI--------KID---------DVEI---DTIGLHQLRS 1296
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNraqrkafrrDIQMvfqDSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1297 KLIIIPQEPvvfsgtLR--FNLDPfnqysDDQIWNCLEICQLKQFAQEDdktLDRYIAEggknMSVGERQLLCLCRALLR 1374
Cdd:PRK10419 107 TVREIIREP------LRhlLSLDK-----AERLARASEMLRAVDLDDSV---LDKRPPQ----LSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1375 GARIVILDEATASVDTVTD-GIVQ--RAIRQHFpQSTTISIAHRLdTIVD--SDRIVVLDAGRVAEfDTPSNLLLNPDSL 1449
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQaGVIRllKKLQQQF-GTACLFITHDL-RLVErfCQRVMVMDNGQIVE-TQPVGDKLTFSSP 245
|
....*
gi 392896924 1450 YSQLL 1454
Cdd:PRK10419 246 AGRVL 250
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
585-780 |
3.40e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.49 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS-------------IAYVPQHS--WIFNKTIKE 649
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFGnelsnyfydqvvgSCQLKTDFRHFQQGENTMVGENGIT---------LSGGQKARISLARAVYQDKDIYLLDDPL 720
Cdd:PRK13652 99 DIAFG-------------PINLGLDEETVAHRVSSALHMLGLEelrdrvphhLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 721 SAVDAHVGRALFDKVigpDGLLRS--KTRVLVTHNLQYT-KYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK13652 166 AGLDPQGVKELIDFL---NDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1238-1454 |
4.23e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDD----------VEIDTIGLHQLR----SKLIIIPQ 1303
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1304 EPVVfsgtlrfNLDPFNQYSdDQIWNCLEICQ--------------LKQFAQEDDKT-LDRYIAEggknMSVGERQLLCL 1368
Cdd:PRK10261 112 EPMT-------SLNPVFTVG-EQIAESIRLHQgasreeamveakrmLDQVRIPEAQTiLSRYPHQ----LSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1369 CRALLRGARIVILDEATASVD-TVTDGIVQ--RAIRQHFPQStTISIAHRLDTIVD-SDRIVVLDAGRVAEFDTPSNLLL 1444
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDvTIQAQILQliKVLQKEMSMG-VIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFH 258
|
250
....*....|
gi 392896924 1445 NPDSLYSQLL 1454
Cdd:PRK10261 259 APQHPYTRAL 268
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
986-1099 |
4.46e-05 |
|
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: 47.01 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 986 PISFFDTTPTGRIINRLSRDldvIDKLQDNIRMCTQTLLNACMILVLI-----SISTPIFLVCAAPLILIyYFVMIYYIP 1060
Cdd:cd18547 92 PLSYFDTHSHGDIMSRVTND---VDNISQALSQSLTQLISSILTIVGTlimmlYISPLLTLIVLVTVPLS-LLVTKFIAK 167
|
90 100 110
....*....|....*....|....*....|....*....
gi 392896924 1061 TSRQLKRLESANRSPILSTIAESIHGASSIRAFDKTERT 1099
Cdd:cd18547 168 RSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEA 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
592-722 |
4.54e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 592 TIKPGQLIAIVGSVGGGKSS---LLSAVL--DEmvlldGRVKVGGSIAYVPQH-SWIFNKTIKENI--LFGNEL-SNYFY 662
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTfakILAGVLkpDE-----GEVDEDLKISYKPQYiSPDYDGTVEEFLrsANTDDFgSSYYK 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 663 DQVVGSCQLKtdfRHFQQgentMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPlSA 722
Cdd:COG1245 437 TEIIKPLGLE---KLLDK----NVKD----LSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1221-1442 |
5.08e-05 |
|
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: 46.21 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKID--DVEIDTIGLhqlRSKL 1298
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREPREV---RRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1299 IIIPQEPVVFSG-TLRFNLDPF-------NQYSDDQIWNCLEICQLKQFAqeddktlDRYIaeggKNMSVGERQLLCLCR 1370
Cdd:cd03265 76 GIVFQDLSVDDElTGWENLYIHarlygvpGAERRERIDELLDFVGLLEAA-------DRLV----KTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1371 ALLRGARIVILDEATASVDTVTDGIVQRAIRQ-HFPQSTTISIA-HRLDTIVD-SDRIVVLDAGRVAEFDTPSNL 1442
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKlKEEFGMTILLTtHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
271-543 |
5.87e-05 |
|
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: 46.61 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 271 LNPILLKQLID-YVSLHDQPLSFGIAIACIMFSCSTTRSLL---QNY--QIAGmcrQAVYYQtvLSNAILHKILRLSPSA 344
Cdd:cd18544 17 LGPLLIKRAIDdYIVPGQGDLQGLLLLALLYLGLLLLSFLLqylQTYllQKLG---QRIIYD--LRRDLFSHIQRLPLSF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 345 RSNRTAGEILNHAAVDIEIIvhsvpylQNMWSVpFQVTLA---MTMLAITlgwAAMAGV-----CIMILFIPLNLCTSRF 416
Cdd:cd18544 92 FDRTPVGRLVTRVTNDTEAL-------NELFTS-GLVTLIgdlLLLIGIL---IAMFLLnwrlaLISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 417 IklsqQKQMKI--KDERTKLS------NEMLNGIKVVKLYAWEESFE---DQINR-LRAKEVKMLRNVCILSRIVDVANA 484
Cdd:cd18544 161 F----RKKSRKayREVREKLSrlnaflQESISGMSVIQLFNREKREFeefDEINQeYRKANLKSIKLFALFRPLVELLSS 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 485 aspflVAIGSftcyVLW----SPDENGLTPSV--AFVALTifNQLRQPMRMVANLINTLVQARVS 543
Cdd:cd18544 237 -----LALAL----VLWygggQVLSGAVTLGVlyAFIQYI--QRFFRPIRDLAEKFNILQSAMAS 290
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
585-725 |
5.89e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEM---VLLDGRVKVGG---------SIAYVPQ---HswIFNKTIKE 649
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGrpldssfqrSIGYVQQqdlH--LPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 650 NILFG------NELSNY----FYDQVVgscqlktDFRHFQQGENTMVGENGITLSGGQKARISLA-RAVYQDKDIYLLDD 718
Cdd:TIGR00956 856 SLRFSaylrqpKSVSKSekmeYVEEVI-------KLLEMESYADAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDE 928
|
....*..
gi 392896924 719 PLSAVDA 725
Cdd:TIGR00956 929 PTSGLDS 935
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1238-1454 |
6.32e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIG---LHQLRSKLIIIPQEPVVfsgtlrf 1314
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLDPfNQYSDDQIWNCLEICQL---KQFAQEDDKTLD----------RYIAEggknMSVGERQLLCLCRALLRGARIVIL 1381
Cdd:PRK10261 413 SLDP-RQTVGDSIMEPLRVHGLlpgKAAAARVAWLLErvgllpehawRYPHE----FSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1382 DEATASVDTVTDGIV-------QRAIRQHFpqsttISIAHRLdTIVD--SDRIVVLDAGRVAEFDTPSNLLLNPDSLYSQ 1452
Cdd:PRK10261 488 DEAVSALDVSIRGQIinllldlQRDFGIAY-----LFISHDM-AVVEriSHRVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
|
..
gi 392896924 1453 LL 1454
Cdd:PRK10261 562 KL 563
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
253-546 |
6.58e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 46.76 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 253 ATIITLTLARLTAdivhylnPILLKQLIDYVSLHDQPLSF-----GIAIACIMFS--CSTTRSLLQNYQIAGMC---RQA 322
Cdd:cd18778 6 LCALLSTLLGLVP-------PWLIRELVDLVTIGSKSLGLllglaLLLLGAYLLRalLNFLRIYLNHVAEQKVVadlRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 323 VYyqtvlsnailHKILRLSPSARSNRTAGEILNHAAVDIE----IIVHSVPylQNMWSVpFQVtLAMTMLAITLGWAAMA 398
Cdd:cd18778 79 LY----------DKLQRLSLRYFDDRQTGDLMSRVINDVAnverLIADGIP--QGITNV-LTL-VGVAIILFSINPKLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 399 GVCIMILFipLNLCTSRFIKLSQQKQMKIKDERTKLS---NEMLNGIKVVKLYAWEES----FEDQINRLRAKEVKMLRn 471
Cdd:cd18778 145 LTLIPIPF--LALGAWLYSKKVRPRYRKVREALGELNallQDNLSGIREIQAFGREEEeakrFEALSRRYRKAQLRAMK- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 472 vcilsrivdVANAASPFLVAIGSF-TCYVLW------SPDENGLTPSVAFVALTIFnqLRQPMRMVANLINTLVQARVSN 544
Cdd:cd18778 222 ---------LWAIFHPLMEFLTSLgTVLVLGfggrlvLAGELTIGDLVAFLLYLGL--FYEPITSLHGLNEMLQRALAGA 290
|
..
gi 392896924 545 KR 546
Cdd:cd18778 291 ER 292
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
937-1091 |
6.68e-05 |
|
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: 46.70 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 937 SVETRLIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDldvIDKLQDNI 1016
Cdd:cd18577 45 DVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSD---TNLIQDGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1017 --RMCTqTLLNACMILVLISIStpiF---------LVCAAPLILIYYFVMIYYI--PTSRQLKRLESAnrspilSTIA-E 1082
Cdd:cd18577 122 geKLGL-LIQSLSTFIAGFIIA---FiyswkltlvLLATLPLIAIVGGIMGKLLskYTKKEQEAYAKA------GSIAeE 191
|
....*....
gi 392896924 1083 SIhgaSSIR 1091
Cdd:cd18577 192 AL---SSIR 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
586-784 |
7.24e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLSaVL------DE-MVLLDGRVKVGGS--------IA-------YVPqhswif 643
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLK-ILsgnyqpDAgSILIDGQEMRFASttaalaagVAiiyqelhLVP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENILFGnELSNYFydQVVGSCQLKTDFRHFQQ--GE----NTMVGEngitLSGGQKARISLARAVYQDKDIYLLD 717
Cdd:PRK11288 93 EMTVAENLYLG-QLPHKG--GIVNRRLLNYEAREQLEhlGVdidpDTPLKY----LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 718 DPLSAVDAHVGRALFdKVIGPdglLRSKTRVL--VTHNL-QYTKYVDTIYVIEDGQIVQHgsFEDIAYVD 784
Cdd:PRK11288 166 EPTSSLSAREIEQLF-RVIRE---LRAEGRVIlyVSHRMeEIFALCDAITVFKDGRYVAT--FDDMAQVD 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1243-1429 |
8.63e-05 |
|
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: 45.86 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1243 LKIEGG-----ERIGVIGRTGSGKSslTMAlyRMIEGEsgtIKIDDVEIDTiglhqLRSKLIIIPQEPVV-FSGTLR--- 1313
Cdd:cd03237 15 LEVEGGsisesEVIGILGPNGIGKT--TFI--KMLAGV---LKPDEGDIEI-----ELDTVSYKPQYIKAdYEGTVRdll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1314 FNLDPfNQYSDDQiWNClEICQLKQFaqedDKTLDRYIAEggknMSVGERQLLCLCRALLRGARIVILDEATASVDTVTD 1393
Cdd:cd03237 83 SSITK-DFYTHPY-FKT-EIAKPLQI----EQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392896924 1394 GIVQRAIRqHF---PQSTTISIAHrlDTIVD---SDRIVVLD 1429
Cdd:cd03237 152 LMASKVIR-RFaenNEKTAFVVEH--DIIMIdylADRLIVFE 190
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
255-546 |
9.96e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 45.96 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 255 IITLTLARLTADIVHYLNPILLKQLIDYV---SLHDQPLSFGIAIACIMFSCSTTRSLLQ---NY-------QIAGMCRQ 321
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVliqLGPGGNTSLLLLLVLGLAGAYVLSALLGilrGRllarlgeRITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 322 AVYyqtvlsnailHKILRLSPSARSNRTAGEILNHaavdieiIVHSVPYLQN--MWSVPFQVTLAMTMLAI-----TLGW 394
Cdd:cd18563 81 DLY----------EHLQRLSLSFFDKRQTGSLMSR-------VTSDTDRLQDflSDGLPDFLTNILMIIGIgvvlfSLNW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 395 AaMAgvCIMILFIPLNLCTSRFI--KLSQ--QKQMKIKDERTKLSNEMLNGIKVVKLYAWE----ESFEDQINRLRAKEV 466
Cdd:cd18563 144 K-LA--LLVLIPVPLVVWGSYFFwkKIRRlfHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEkreiKRFDEANQELLDANI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 467 KMLRnvcilsrivdVANAASPFLVAIGSFTCYVLW---SPD--ENGLTPS--VAFVALTIfnQLRQPMRMVANLINTLVQ 539
Cdd:cd18563 221 RAEK----------LWATFFPLLTFLTSLGTLIVWyfgGRQvlSGTMTLGtlVAFLSYLG--MFYGPLQWLSRLNNWITR 288
|
....*..
gi 392896924 540 ARVSNKR 546
Cdd:cd18563 289 ALTSAER 295
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
923-1068 |
1.00e-04 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 45.97 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 923 VDYLnSTSSVDGPVSVETRLIVYAGFGGLeMLLLALA----FTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRI 998
Cdd:cd18573 23 IDVA-SKESGDIEIFGLSLKTFALALLGV-FVVGAAAnfgrVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGEL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 999 INRLSRDLDVIDK-LQDNIRMCTQTLLNACM-ILVLISISTPIFLV--CAAPLILIyyFVMIYyiptSRQLKRL 1068
Cdd:cd18573 101 VSRLSSDTSVVGKsLTQNLSDGLRSLVSGVGgIGMMLYISPKLTLVmlLVVPPIAV--GAVFY----GRYVRKL 168
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
567-725 |
1.03e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.38 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 567 AIVFKNASLNWKGPQnpPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAV--LDEM----VLLDGRVkVGG------SIA 634
Cdd:PRK11650 3 GLKLQAVRKSYDGKT--QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagLERItsgeIWIGGRV-VNElepadrDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 635 YVPQ------HswifnKTIKENILFGnelsnyfydqvvgscqLKTdfRHFQQGE-NTMVGENGIT-------------LS 694
Cdd:PRK11650 80 MVFQnyalypH-----MSVRENMAYG----------------LKI--RGMPKAEiEERVAEAARIleleplldrkpreLS 136
|
170 180 190
....*....|....*....|....*....|.
gi 392896924 695 GGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:PRK11650 137 GGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
584-755 |
1.09e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.93 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG------------SIAYVPQHSWIfnktikENI 651
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltnisdvhqNMGYCPQFDAI------DDL 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 LFGNElSNYFYDQVVGscqlkTDFRHFQQGENTMVGENGITL---------SGGQKARISLARAVYQDKDIYLLDDPLSA 722
Cdd:TIGR01257 2027 LTGRE-HLYLYARLRG-----VPAEEIEKVANWSIQSLGLSLyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190
....*....|....*....|....*....|....
gi 392896924 723 VDAHVGRALFDKVIgpdGLLRS-KTRVLVTHNLQ 755
Cdd:TIGR01257 2101 MDPQARRMLWNTIV---SIIREgRAVVLTSHSME 2131
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1221-1454 |
1.36e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.51 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLPL---VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTiglhQLRSK 1297
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS----TSKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1298 LI--IIPQEPVVFsgtlrfnldpfnQYSDDQIWnclEICQLKQFA---------QEDDKTLDRY------IAEG--GKN- 1357
Cdd:PRK13649 79 DIkqIRKKVGLVF------------QFPESQLF---EETVLKDVAfgpqnfgvsQEEAEALAREklalvgISESlfEKNp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1358 --MSVGERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQ-HFPQSTTISIAHRLDTIVD-SDRIVVLDAGRV 1433
Cdd:PRK13649 144 feLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANyADFVYVLEKGKL 223
|
250 260
....*....|....*....|.
gi 392896924 1434 AEFDTPSNLLLNPDSLYSQLL 1454
Cdd:PRK13649 224 VLSGKPKDIFQDVDFLEEKQL 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
585-725 |
1.43e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLlsavldeMVLLDGRvKVGG------SIAYVPQHSWIFNK------------- 645
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTL-------MDVLAGR-KTGGyiegdiRISGFPKKQETFARisgyceqndihsp 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 --TIKENILFG------NELSNY----FYDQVVGSCQLktdfrhfQQGENTMVGENGIT-LSGGQKARISLARAVYQDKD 712
Cdd:PLN03140 967 qvTVRESLIYSaflrlpKEVSKEekmmFVDEVMELVEL-------DNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPS 1039
|
170
....*....|...
gi 392896924 713 IYLLDDPLSAVDA 725
Cdd:PLN03140 1040 IIFMDEPTSGLDA 1052
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
694-780 |
1.65e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 694 SGGQKARISLARAVYQDKDIYLLDDPLSAVDAHVgRA----LFDKVIGPDGLlrskTRVLVTHNLQYTKYV-DTIYVIED 768
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV-QAqvlnLMMDLQQELGL----SYVFISHDLSVVEHIaDEVMVMYL 230
|
90
....*....|..
gi 392896924 769 GQIVQHGSFEDI 780
Cdd:PRK11308 231 GRCVEKGTKEQI 242
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
932-1093 |
1.78e-04 |
|
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: 45.17 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 932 VDGPVSVETR--LIVYAGFggleMLLLALAFTVLTIG--------SLRASYGLHSPLIHALLVAPISFFDTTPTGRIINR 1001
Cdd:cd18543 26 IDGPIAHGDRsaLWPLVLL----LLALGVAEAVLSFLrrylagrlSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1002 LSRDLDVIdklQDNIRMCTQTLLNACMILV----LISISTPIFLVCAAPLILIYYFVMIY---YIPTSRqlkrlESANRS 1074
Cdd:cd18543 102 ATSDLSLV---QRFLAFGPFLLGNLLTLVVglvvMLVLSPPLALVALASLPPLVLVARRFrrrYFPASR-----RAQDQA 173
|
170 180
....*....|....*....|
gi 392896924 1075 PILSTIA-ESIHGASSIRAF 1093
Cdd:cd18543 174 GDLATVVeESVTGIRVVKAF 193
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
566-733 |
1.86e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.72 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 566 NAIVFKNASLNWKGPQnppVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS--IAYVPQHSWIf 643
Cdd:PRK09544 3 SLVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENILFGNELSNYFYDQVVGSCQLKTDFRHFQQGENTmvgengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAV 723
Cdd:PRK09544 79 DTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQ-------KLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170
....*....|
gi 392896924 724 DAHVGRALFD 733
Cdd:PRK09544 152 DVNGQVALYD 161
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1237-1445 |
2.15e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.48 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQ-LRSKLIIIPQEPVVFSG-TLRF 1314
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1315 NLDPFNQYSDDQiwncleicqlkQFAQEDDKTLD-------RYIAEGGkNMSVGERQLLCLCRALLRGARIVILDEATAS 1387
Cdd:PRK11614 100 NLAMGGFFAERD-----------QFQERIKWVYElfprlheRRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1388 VDTVTDGIVQRAIRQHFPQSTTISI-------AHRLdtivdSDRIVVLDAGRVAEFDTPSNLLLN 1445
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLveqnanqALKL-----ADRGYVLENGHVVLEDTGDALLAN 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1222-1442 |
2.38e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1222 ELDGFSmryrKNLPLV--LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEI------DTIG--- 1290
Cdd:PRK11288 6 SFDGIG----KTFPGVkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALAagv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1291 --LHQlrsKLIIIPQEPV---VFSGTL--RFNLdpfnqysddqiwncLEICQLKQFAQEDDKTLDRYI--AEGGKNMSVG 1361
Cdd:PRK11288 82 aiIYQ---ELHLVPEMTVaenLYLGQLphKGGI--------------VNRRLLNYEAREQLEHLGVDIdpDTPLKYLSIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1362 ERQLLCLCRALLRGARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTI-SIAHRLDTIVD-SDRIVVLDAGR-VAEFDT 1438
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVIlYVSHRMEEIFAlCDAITVFKDGRyVATFDD 224
|
....
gi 392896924 1439 PSNL 1442
Cdd:PRK11288 225 MAQV 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1221-1283 |
2.40e-04 |
|
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: 44.17 E-value: 2.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSltmaLYRMIEG----ESGTIKIDD 1283
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTT----TLRMIAGleepTSGRIYIGG 61
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
568-725 |
2.72e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 43.77 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 568 IVFKNASLNWKGP-QNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLL--------SAVLDEMVLLDGRVKVGG---SIAY 635
Cdd:cd03232 4 LTWKNLNYTVPVKgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagrktAGVITGEILINGRPLDKNfqrSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 636 VPQ---HSWifNKTIKENILFgnelsnyfydqvvgSCQLKtdfrhfqqgentmvgenGITLSggQKARISLARAVYQDKD 712
Cdd:cd03232 84 VEQqdvHSP--NLTVREALRF--------------SALLR-----------------GLSVE--QRKRLTIGVELAAKPS 128
|
170
....*....|...
gi 392896924 713 IYLLDDPLSAVDA 725
Cdd:cd03232 129 ILFLDEPTSGLDS 141
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1221-1280 |
2.95e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYrKNLPLvLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIK 1280
Cdd:PRK15064 320 LEVENLTKGF-DNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
942-1171 |
3.00e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 44.40 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGFGGLEMLLLALAFTVLTIGSLRAS----YGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKLQDN-- 1015
Cdd:cd18546 38 LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGerllYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTgl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1016 IRMCTQTLLNACMILVLISISTPIFLVCAAPLILIYYFVMIYyiptSRQLKRLESANR---SPILSTIAESIHGASSIRA 1092
Cdd:cd18546 118 VQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWF----RRRSSRAYRRAReriAAVNADLQETLAGIRVVQA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 1093 FDKTERtttalstNVDKFAQcrylshMSNRWLATRLEllgntcvlfaslSATLSTKYFgltPGMAGLSVsyaLTITEVL 1171
Cdd:cd18546 194 FRRERR-------NAERFAE------LSDDYRDARLR------------AQRLVAIYF---PGVELLGN---LATAAVL 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1221-1445 |
3.06e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRkNLPLvlkNIDLKIEGGERIGVIGRTGSGKSSltmaLYRMIEG----ESGTIKIDDVEidtiglHQL-- 1294
Cdd:PRK10771 2 LKLTDITWLYH-HLPM---RFDLTVERGERVAILGPSGAGKST----LLNLIAGfltpASGSLTLNGQD------HTTtp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1295 --RSKLIIIPQEPVVFSG-TLRFN----LDPFNQYSDDQiwncleICQLKQFAQED--DKTLDRYIAEggknMSVGERQL 1365
Cdd:PRK10771 68 psRRPVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQ------REKLHAIARQMgiEDLLARLPGQ----LSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1366 LCLcrallrgAR-------IVILDEATASVDTvtdgivqrAIRQ----------HFPQSTTISIAHRLDtivDSDRI--- 1425
Cdd:PRK10771 138 VAL-------ARclvreqpILLLDEPFSALDP--------ALRQemltlvsqvcQERQLTLLMVSHSLE---DAARIapr 199
|
250 260
....*....|....*....|.
gi 392896924 1426 -VVLDAGRVAeFDTPSNLLLN 1445
Cdd:PRK10771 200 sLVVADGRIA-WDGPTDELLS 219
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
982-1093 |
3.13e-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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 44.43 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 982 LLVAPISFFDTTPTGRIINRLSRdldvIDKLQDNI--RMCTqTLLNACMILVLISI----STPIFLVCAAPLILIYYFVM 1055
Cdd:cd18783 85 LLSLPIDFFERTPAGVLTKHMQQ----IERIRQFLtgQLFG-TLLDATSLLVFLPVlffySPTLALVVLAFSALIALIIL 159
|
90 100 110
....*....|....*....|....*....|....*...
gi 392896924 1056 IYYIPTSRQLKRLESANRSPiLSTIAESIHGASSIRAF 1093
Cdd:cd18783 160 AFLPPFRRRLQALYRAEGER-QAFLVETVHGIRTVKSL 196
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1221-1434 |
3.27e-04 |
|
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: 43.64 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYrKNLPLvlkNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVeiDTIGLHQLRSKLII 1300
Cdd:cd03298 1 VRLDKIRFSY-GEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV--DVTAAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQEPVVFSG-TLRFNLDpfnqysddqiwncLEICQLKQFAQEDDKTLDRYIAEGG---------KNMSVGERQLLCLCR 1370
Cdd:cd03298 75 LFQENNLFAHlTVEQNVG-------------LGLSPGLKLTAEDRQAIEVALARVGlaglekrlpGELSGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1371 ALLRGARIVILDEATASVD-TVTDGIVQRAIRQHFPQS-TTISIAHRLDTIVD-SDRIVVLDAGRVA 1434
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1237-1295 |
3.31e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKI---DDVEIDTIGLHQLR 1295
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqDVATLDADALAQLR 84
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
691-777 |
3.39e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 691 ITLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA----HVGRALfdKVIGPDGllrSKTRVLVTHNLQYTKYVDTIYVI 766
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAI--RRLSEEG---KKTALVVEHDLAVLDYLSDRIHV 144
|
90
....*....|.
gi 392896924 767 EDGQIVQHGSF 777
Cdd:cd03222 145 FEGEPGVYGIA 155
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
273-501 |
3.74e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.01 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 273 PILLKQLIDY------VSLHDQPLSFGIAIACIMFSCSTTRSLLQNY---QIAGMCRQAVYyqtvlsnailHKILRLSPS 343
Cdd:cd18575 16 GQGLRLLIDQgfaagnTALLNRAFLLLLAVALVLALASALRFYLVSWlgeRVVADLRKAVF----------AHLLRLSPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 344 A-RSNRTaGEILNHAAVDIEIIvhsvpylQNMWSVPFQVTL--------AMTMLAIT-LGWAAMAGVCIMILFIPLNLCT 413
Cdd:cd18575 86 FfETTRT-GEVLSRLTTDTTLI-------QTVVGSSLSIALrnlllligGLVMLFITsPKLTLLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 414 SRFIKLSQQKQMKIKDERTKlSNEMLNGIKVVKLYAWEE----SFEDQINRLRAKEVKMLRNVCILSRIVdvanaaspFL 489
Cdd:cd18575 158 RRVRRLSRASQDRLADLSAF-AEETLSAIKTVQAFTREDaerqRFATAVEAAFAAALRRIRARALLTALV--------IF 228
|
250
....*....|..
gi 392896924 490 VAIGSFTCyVLW 501
Cdd:cd18575 229 LVFGAIVF-VLW 239
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
585-778 |
4.25e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 585 VLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGG--SIAYVPQHSWIFNKTIKENILFGN------- 655
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALPQPALEYVIDGDreyrqle 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 656 ---ELSNYFYD-QVVGSCQLKTDFRH----------------FQQgenTMVGENGITLSGGQKARISLARAVYQDKDIYL 715
Cdd:PRK10636 96 aqlHDANERNDgHAIATIHGKLDAIDawtirsraasllhglgFSN---EQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 716 LDDPLSAVDahvgralFDKVIGPDGLLRS--KTRVLVTHNLQYTK-YVDTIYVIEDGQIVQ----HGSFE 778
Cdd:PRK10636 173 LDEPTNHLD-------LDAVIWLEKWLKSyqGTLILISHDRDFLDpIVDKIIHIEQQSLFEytgnYSSFE 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1221-1268 |
4.57e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 4.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLtMAL 1268
Cdd:NF033858 2 ARLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSL-LSL 46
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
594-724 |
4.76e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.51 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 594 KPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRvkvggsiaYVPQHSWifNKTIKEniLFGNELSNYFYD---------- 663
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDW--DEILDE--FRGSELQNYFTKllegdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 664 ----------QVVGSCQL---KTDFRHF-----QQGENTMVGENGIT-LSGGQKARISLARAVYQDKDIYLLDDPLSAVD 724
Cdd:cd03236 92 kpqyvdlipkAVKGKVGEllkKKDERGKldelvDQLELRHVLDRNIDqLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1238-1446 |
4.94e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIdTIGLHQLRSKLI-IIPQEPV---------- 1306
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQRIrMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1307 -VFSGTLRFNLDPFNQYSDDQIWNCLEICQLkqfaqeddktLDRYIAEGGKNMSVGERQLLCLCRALLRGARIVILDEAT 1385
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGL----------LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1386 ASVDTV--------------TDGIVQRAIRQHFPQSTTIsiahrldtivdSDRIVVLDAGRVAEFDTPSNLLLNP 1446
Cdd:PRK15112 178 ASLDMSmrsqlinlmlelqeKQGISYIYVTQHLGMMKHI-----------SDQVLVMHQGEVVERGSTADVLASP 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
584-780 |
5.24e-04 |
|
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: 44.29 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKS-SLLSAvldeMVLL-DGRVKVGGSIAYVPQHswIFNKTIKE-NILFGNELSNY 660
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvTALSI----LRLLpDPAAHPSGSILFDGQD--LLGLSERElRRIRGNRIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 661 F-------------YDQVVGSCQLKTDFRHFQQGENT--MVGENGIT------------LSGGQKARISLARAVYQDKDI 713
Cdd:COG4172 98 FqepmtslnplhtiGKQIAEVLRLHRGLSGAAARARAleLLERVGIPdperrldayphqLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 714 YLLDDPLSAVDAHVGRALFDkvigpdgLLRSKTR------VLVTHNLQY-TKYVDTIYVIEDGQIVQHGSFEDI 780
Cdd:COG4172 178 LIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHDLGVvRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1236-1287 |
5.43e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 42.94 E-value: 5.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1236 LVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEID 1287
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID 67
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
587-775 |
6.23e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.86 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 587 KDLSATIKPGQLIAIVGSVGGGKSSLLS--AVLDEMVllDGRVKVGG-----------SIAYVPQHSWIF-NKTIKENIL 652
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRmiAGLEDIT--SGDLFIGEkrmndvppaerGVGMVFQSYALYpHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 653 FGNELS-------NYFYDQVVGSCQLKtdfrHFQQGENTmvgengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVDA 725
Cdd:PRK11000 98 FGLKLAgakkeeiNQRVNQVAEVLQLA----HLLDRKPK-------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 726 ------HVGRALFDKVIGpdgllrsKTRVLVTHN-LQYTKYVDTIYVIEDGQIVQHG 775
Cdd:PRK11000 167 alrvqmRIEISRLHKRLG-------RTMIYVTHDqVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
566-638 |
6.27e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 6.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 566 NAIVFKNASlnwKGPQNPPVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVK--VGGSIAYVPQ 638
Cdd:PRK15064 318 NALEVENLT---KGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsENANIGYYAQ 389
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
986-1093 |
6.29e-04 |
|
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: 43.57 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 986 PISFFDTTPTGRIINRLSRDLDVIDK-LQDNIRMCTQTLLNACMILV-LISISTPIFLVCAAPLILIYYFVMIYYI---P 1060
Cdd:cd18542 86 SFSFHDKARTGDLMSRCTSDVDTIRRfLAFGLVELVRAVLLFIGALIiMFSINWKLTLISLAIIPFIALFSYVFFKkvrP 165
|
90 100 110
....*....|....*....|....*....|....
gi 392896924 1061 TSRQLKRLESAnrspiLSTIA-ESIHGASSIRAF 1093
Cdd:cd18542 166 AFEEIREQEGE-----LNTVLqENLTGVRVVKAF 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
691-764 |
6.54e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 6.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 691 ITLSGGQKARISLARAV----YQDKDIYLLDDPLSAVDAHVGRALFDKVIgpdGLLRSKTRVLV-THNLQYTKYVDTIY 764
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIL---EHLVKGAQVIViTHLPELAELADKLI 151
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
588-726 |
7.42e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 588 DLSATIKPGQLIAIVGSVGGGKSSLLS-----AVLDE-MVLLDG------RVKVGGSIAYVPQHSWIfnK---TIKENIL 652
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRilaglARPDAgEVLWQGepirrqRDEYHQDLLYLGHQPGI--KtelTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 653 FGNELSnyfydqvvgscQLKTDFRHFQ-------QG-ENTMVGengiTLSGGQKARISLARAVYQDKDIYLLDDPLSAVD 724
Cdd:PRK13538 97 FYQRLH-----------GPGDDEALWEalaqvglAGfEDVPVR----QLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
..
gi 392896924 725 AH 726
Cdd:PRK13538 162 KQ 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1221-1435 |
7.56e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1221 IELDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGlHQLRSKLII 1300
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1301 IPQ----EPvvfSGTLRFNLDPFNQYSDDQIWNCLEICQ-LKQFAQEDDKTlDRYIAEggknMSVGERQLLCLCRALLRG 1375
Cdd:PRK13537 85 VPQfdnlDP---DFTVRENLLVFGRYFGLSAAAARALVPpLLEFAKLENKA-DAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1376 ARIVILDEATASVDTVTDGIVQRAIRQHFPQSTTISI-------AHRLdtivdSDRIVVLDAGR-VAE 1435
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRkIAE 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
586-770 |
7.81e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLlsavldeMVLLDG-RVKVGGSIAYV--------PQHS-------------WIF 643
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTM-------MKVLTGiYTRDAGSILYLgkevtfngPKSSqeagigiihqelnLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 644 NKTIKENILFGNELSNYFydqvvGSCQLKTDFR---------HFQQGENTMVGEngitLSGGQKARISLARAVYQDKDIY 714
Cdd:PRK10762 93 QLTIAENIFLGREFVNRF-----GRIDWKKMYAeadkllarlNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896924 715 LLDDPLSAVDAHVGRALFdKVIGPdglLRSKTR--VLVTHNLQYT-KYVDTIYVIEDGQ 770
Cdd:PRK10762 164 IMDEPTDALTDTETESLF-RVIRE---LKSQGRgiVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
254-546 |
8.02e-04 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 43.16 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 254 TIITLTLARLTADIVhylNPILLKQLIDYVslhdqpLSFG---IAIACIMFSCSTTRSLLQNYQIAGMCRQavyyqtvLS 330
Cdd:cd18548 12 VLLELLLPTLMADII---DEGIANGDLSYI------LRTGllmLLLALLGLIAGILAGYFAAKASQGFGRD-------LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 331 NAILHKILRLSPSARSNRTAGEILNHAAVDIEIIvhsvpylQNMWS--------VPFQVTLAMTMLAIT---LGWAAMAG 399
Cdd:cd18548 76 KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQV-------QNFVMmllrmlvrAPIMLIGAIIMAFRInpkLALILLVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 400 VCIMILFIPLNLctSRFIKLSQQKQMKIkDERTKLSNEMLNGIKVVKLYAWE----ESFEDQINRLRAKEVKMLRNVCIL 475
Cdd:cd18548 149 IPILALVVFLIM--KKAIPLFKKVQKKL-DRLNRVVRENLTGIRVIRAFNREdyeeERFDKANDDLTDTSLKAGRLMALL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896924 476 SRIVD-VANAASPFLVAIGSFtcYVlwspDENGLTPS--VAFValTIFNQLRQPMRMVANLINTLVQARVSNKR 546
Cdd:cd18548 226 NPLMMlIMNLAIVAILWFGGH--LI----NAGSLQVGdlVAFI--NYLMQILMSLMMLSMVFVMLPRASASAKR 291
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
982-1093 |
9.25e-04 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 42.79 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 982 LLVAPISFFDTTPTGRIINRLSRDLDVI-DKLQDNIRMCTQTLLNA-CMILVLISISTPIFLVC--AAPLIliyyFVMIY 1057
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVqNALTSALTVLVRDPLTViGLLGVLFYLDWKLTLIAlvVLPLA----ALPIR 157
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 392896924 1058 YIptSRQLKRL------ESANrspILSTIAESIHGASSIRAF 1093
Cdd:cd18552 158 RI--GKRLRKIsrrsqeSMGD---LTSVLQETLSGIRVVKAF 194
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1238-1362 |
9.37e-04 |
|
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: 42.60 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTM-ALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVvfsG-TLRFN 1315
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI---GrTPRSN 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 392896924 1316 LDPFNQYSDD-QIWNClEICQLKQFAQEddkTLD-RYiaeGGKN------MSVGE 1362
Cdd:cd03271 88 PATYTGVFDEiRELFC-EVCKGKRYNRE---TLEvRY---KGKSiadvldMTVEE 135
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1223-1264 |
1.37e-03 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 42.36 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 392896924 1223 LDGFSMRYRKNLplVLKNIDLKIEGGERIGVIGRTGSGKSSL 1264
Cdd:PRK11247 15 LNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTL 54
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
584-751 |
1.46e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.76 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRVKVGGS----------IAYVpQHSWIFNKTIK--ENI 651
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYL-GHLPGLKADLStlENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 652 LFGNELSNYFYDQVVGSCQLKTDFRHFqqgENTMVGEngitLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAHvGRAL 731
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAIVGLAGY---EDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITL 175
|
170 180
....*....|....*....|
gi 392896924 732 FDKVIGPDglLRSKTRVLVT 751
Cdd:PRK13543 176 VNRMISAH--LRGGGAALVT 193
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1220-1283 |
2.26e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.14 E-value: 2.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1220 KIELDGFSMRYRKNLPlVLKNIDLKIEGGERIGVIGRTGSGKSSltmaLYRMIEG----ESGTIKIDD 1283
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGleriTSGEIWIGG 65
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
941-1093 |
2.28e-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: 41.63 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 941 RLIVYAGFggleMLLLALAFTVLTIG--------SLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLdvidkl 1012
Cdd:cd18541 38 QLLRYALL----ILLLALLIGIFRFLwrylifgaSRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1013 qDNIRMCT----QTLLNACMILVL-----ISISTPIFLVCAAPLILIyyFVMIYYIptSRQL-KRLESANRSpiLSTIA- 1081
Cdd:cd18541 108 -NAVRMALgpgiLYLVDALFLGVLvlvmmFTISPKLTLIALLPLPLL--ALLVYRL--GKKIhKRFRKVQEA--FSDLSd 180
|
170
....*....|....*
gi 392896924 1082 ---ESIHGASSIRAF 1093
Cdd:cd18541 181 rvqESFSGIRVIKAF 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1248-1310 |
2.46e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 2.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896924 1248 GERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQLRSKLIIIPQEPVVFSG 1310
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE 64
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
255-546 |
2.71e-03 |
|
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: 41.68 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 255 IITLTLARLTADIVHYLNPILLKQLID-YVSLHDQPLSFGIAIA-----CIMFSCSTTRSLLQNYqiAGmcrqavyyQTV 328
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDeYIPNGDLSGLLIIALLflalnLVNWVASRLRIYLMAK--VG--------QRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 329 LSN---AILHKILRLSPSARSNRTAGEILNHaavdieiIVHSVPYLQNMWS------VPFQVTLAMT---MLAI--TLGW 394
Cdd:cd18545 72 LYDlrqDLFSHLQKLSFSFFDSRPVGKILSR-------VINDVNSLSDLLSnglinlIPDLLTLVGIviiMFSLnvRLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 395 AAMAGVCIMILFIplnLCTSRFIKLSQQKQmkikdeRTKLSN------EMLNGIKVVKLYAWE----ESFEDQINRLRAK 464
Cdd:cd18545 145 VTLAVLPLLVLVV---FLLRRRARKAWQRV------RKKISNlnaylhESISGIRVIQSFAREdeneEIFDELNRENRKA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 465 EVKMLRNVCILSRIVDVANAASPFLV--------AIGSFTCYVLwspdengltpsVAFVALtiFNQLRQPMRMVANLINT 536
Cdd:cd18545 216 NMRAVRLNALFWPLVELISALGTALVywyggklvLGGAITVGVL-----------VAFIGY--VGRFWQPIRNLSNFYNQ 282
|
330
....*....|
gi 392896924 537 LVQARVSNKR 546
Cdd:cd18545 283 LQSAMASAER 292
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1235-1286 |
2.83e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1235 PLvLKNIDLKIEGGERIGVIGRTGSGKSSLTMALyrmiegeSGTIKIDDVEI 1286
Cdd:PRK11147 17 PL-LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRI 60
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
959-1093 |
2.88e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 41.38 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 959 AFTVLTIGSL-----RASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDldvidkLQD-----------NIRMCTQT 1022
Cdd:cd18574 57 LLTFAYISLLsvvgeRVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD------VQEfkssfkqcvsqGLRSVTQT 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896924 1023 LlnACMI-LVLISISTPIFLVCAAPLIliyYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAF 1093
Cdd:cd18574 131 V--GCVVsLYLISPKLTLLLLVIVPVV---VLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAF 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
692-726 |
2.99e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.99e-03
10 20 30
....*....|....*....|....*....|....*
gi 392896924 692 TLSGGQKARISLARAVYQDKDIYLLDDPLSAVDAH 726
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
584-780 |
3.21e-03 |
|
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: 41.58 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDemvLLDGRVKVGGSI-----------------------AYVPQ-- 638
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILG---LLPPPGITSGEIlfdgedllklsekelrkirgreiQMIFQdp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 639 -HSwiFN------KTIKENILFGNELS-NYFYDQVV---GSCQLKTDFRHFQQ--GEntmvgengitLSGGQKARISLAR 705
Cdd:COG0444 96 mTS--LNpvmtvgDQIAEPLRIHGGLSkAEARERAIellERVGLPDPERRLDRypHE----------LSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 706 AVYQDKDIYLLDDPLSAVDAHVgRA----LFDKvigpdglLRSKTR---VLVTHNLQYTKYV-DTIYVIEDGQIVQHGSF 777
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTI-QAqilnLLKD-------LQRELGlaiLFITHDLGVVAEIaDRVAVMYAGRIVEEGPV 235
|
...
gi 392896924 778 EDI 780
Cdd:COG0444 236 EEL 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1235-1305 |
3.56e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.23 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1235 PLVLKNID---LKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTI--------KIDDVEidtigLHQLRSKLIIIPQ 1303
Cdd:PRK15079 31 PKTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdllGMKDDE-----WRAVRSDIQMIFQ 105
|
..
gi 392896924 1304 EP 1305
Cdd:PRK15079 106 DP 107
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
687-781 |
3.64e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 687 GENGITLSGGQKARISLARAVyQDKD----IYLLDDPLSAVDAHVGRALFDkVIGPdglLRSK--TRVLVTHNLQYTKYV 760
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKEL-SKRStgrtLYILDEPTTGLHFDDIKKLLE-VLQR---LVDKgnTVVVIEHNLDVIKTA 898
|
90 100
....*....|....*....|....*....
gi 392896924 761 DtiYVIE--------DGQIVQHGSFEDIA 781
Cdd:TIGR00630 899 D--YIIDlgpeggdgGGTVVASGTPEEVA 925
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
953-1098 |
3.87e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 40.96 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 953 MLLLALAFTVLTIGSLRA--SYG---------------LHSPLIHALLVAPISFFDTTPTGRIINRLSRDldvIDKLQD- 1014
Cdd:cd18564 51 ALLLLAAAALVGIALLRGlaSYAgtyltalvgqrvvldLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGD---VGAIQDl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1015 ----NIRMCTQTLLNACMILVLISISTPIFLV--CAAPLILiyyFVMIYYIP----TSRQLKRLESAnrspILSTIAESI 1084
Cdd:cd18564 128 lvsgVLPLLTNLLTLVGMLGVMFWLDWQLALIalAVAPLLL---LAARRFSRrikeASREQRRREGA----LASVAQESL 200
|
170
....*....|....
gi 392896924 1085 HGASSIRAFDKTER 1098
Cdd:cd18564 201 SAIRVVQAFGREEH 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1240-1449 |
3.93e-03 |
|
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: 41.24 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1240 NIDLKIEGGERIGVIGRTGSGKSSLTmalyRMIEG----ESGTIKIDD-VEIDTiglhqlrSKLIIIP----------QE 1304
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLL----RAIAGlerpDSGRIRLGGeVLQDS-------ARGIFLPphrrrigyvfQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1305 PVVFS-----GTLRFNL----DPFNQYSDDQIWNCLEICQLkqfaqeddktLDRYIAeggkNMSVGERQLLclcrallrg 1375
Cdd:COG4148 86 ARLFPhlsvrGNLLYGRkrapRAERRISFDEVVELLGIGHL----------LDRRPA----TLSGGERQRV--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1376 A---------RIVILDEATASVDtvtdgiVQR---------AIRQHFpqstTISI---AHRLDTIVD-SDRIVVLDAGRV 1433
Cdd:COG4148 143 AigrallsspRLLLMDEPLAALD------LARkaeilpyleRLRDEL----DIPIlyvSHSLDEVARlADHVVLLEQGRV 212
|
250
....*....|....*.
gi 392896924 1434 AEFDTPSNLLLNPDSL 1449
Cdd:COG4148 213 VASGPLAEVLSRPDLL 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1238-1432 |
4.13e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1238 LKNIDLKIEGGERIGVIGRTGSGKSSLTMAL-----YRMIEGE---SGTIK----IDDVEIDTIGL-HQlrsKLIIIPQE 1304
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTYEGEiifEGEELqasnIRDTERAGIAIiHQ---ELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1305 PV---VFSGT--LRFNLDPFNQ-YSDDQIWncLEicQLKqfaqeddktLDRYIAEGGKNMSVGERQLLCLCRALLRGARI 1378
Cdd:PRK13549 98 SVlenIFLGNeiTPGGIMDYDAmYLRAQKL--LA--QLK---------LDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1379 VILDEATAS-----VDTVTDgIVqRAIRQHfpQSTTISIAHRLDTIVD-SDRIVVLDAGR 1432
Cdd:PRK13549 165 LILDEPTASlteseTAVLLD-II-RDLKAH--GIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1237-1431 |
4.46e-03 |
|
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: 40.17 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGtikidDVEIDTIGLHQLRSKLiiipQEPVVFSG------ 1310
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG-----RVLLNGGPLDFQRDSI----ARGLLYLGhapgik 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1311 -------TLRFnLDPFNqySDDQIWNCLEICQLKQFAqeddktlDRYIAEggknMSVGERQLLCLCRALLRGARIVILDE 1383
Cdd:cd03231 86 ttlsvleNLRF-WHADH--SDEQVEEALARVGLNGFE-------DRPVAQ----LSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 392896924 1384 ATASVDTVTDGIVQRAIRQHFPQSTTISIAHRLDTIVDSDRIVVLDAG 1431
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
586-627 |
4.68e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 4.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 392896924 586 LKDLSATIKPGQLIAIVGSVGGGKSSLLSAVLDEMVLLDGRV 627
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
273-468 |
4.73e-03 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 40.56 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 273 PILLKQLIDYVSLHDQPLSFGIAIACIMFscSTTRSLlqnYQIAGMCRQAVYY------QTVLSNAILHKILRLSPSARS 346
Cdd:cd18582 16 PFLLKYAVDALSAPASALLAVPLLLLLAY--GLARIL---SSLFNELRDALFArvsqraVRRLALRVFRHLHSLSLRFHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 347 NRTAGE---ILNHAAVDIEIIVHSVpyLQNMwsVP--FQVTLAMTMLAITLGW--AAMAGVCiMILFIPLNLCTSRFIkL 419
Cdd:cd18582 91 SRKTGAlsrAIERGTRGIEFLLRFL--LFNI--LPtiLELLLVCGILWYLYGWsyALITLVT-VALYVAFTIKVTEWR-T 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392896924 420 SQQKQMKIKDER--TKLSNEMLNgIKVVKLYAWEESFEDQINRLRAKEVKM 468
Cdd:cd18582 165 KFRREMNEADNEanAKAVDSLLN-YETVKYFNNEEYEAERYDKALAKYEKA 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1237-1305 |
5.23e-03 |
|
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: 41.21 E-value: 5.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGE----SGTIKIDDVEIDTIGLHQLR----SKLIIIPQEP 1305
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP 101
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1239-1434 |
5.46e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.19 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1239 KNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEIDTIGLHQ-LRSKLIIIPQEPVVfSGtlrFNLD 1317
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQS-SG---LYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1318 -PFNqysddqiWNcleICQLKQ-----FAQE--DDKTLDRYIAEGG----------KNMSVGERQLLCLCRALLRGARIV 1379
Cdd:PRK15439 356 aPLA-------WN---VCALTHnrrgfWIKParENAVLERYRRALNikfnhaeqaaRTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 1380 ILDEATASVDTVTDGIVQRAIRQHFPQSTTI-SIAHRLDTIVD-SDRIVVLDAGRVA 1434
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
942-1191 |
6.22e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 40.24 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGFGGLEMLLLALAFTVLTIGSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKLQDNIrmcTQ 1021
Cdd:cd18568 45 LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSA---LT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1022 TLLNACMILVLISI----STPIFLVCAApLILIYYFVMIYYIPTSRQLKRLESANRSPILSTIAESIHGASSIRAFdKTE 1097
Cdd:cd18568 122 TILDLLMVFIYLGLmfyyNLQLTLIVLA-FIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKAL-AAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 1098 RTT-----TALSTNVDKFAQCRYLSHMSNRwLATRLELLGNTCVLFASLSATLSTKyfgLTPG--MAGLSVsYALTITEV 1170
Cdd:cd18568 200 RPIrwrweNKFAKALNTRFRGQKLSIVLQL-ISSLINHLGTIAVLWYGAYLVISGQ---LTIGqlVAFNML-FGSVINPL 274
|
250 260
....*....|....*....|.
gi 392896924 1171 LNIcVRSVSEIESNIVSVERV 1191
Cdd:cd18568 275 LAL-VGLWDELQETRISVERL 294
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1237-1275 |
6.35e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.01 E-value: 6.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 392896924 1237 VLKNIDLKIEGGERIGVIGRTGSGKSSLTMAL-----YRMIEGE 1275
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKILEGD 65
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
942-1068 |
6.60e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 40.11 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 942 LIVYAGFGGLEMLLLALAftvltigSLRASYGLHSPLIHALLVAPISFFDTTPTGRIINRLSRDLDVIDKL--QDNIRMC 1019
Cdd:cd18551 46 FLLQAVLSALSSYLLGRT-------GERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELitSGLPQLV 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 392896924 1020 TQTLLNACMILVLISISTPIFLVCAApLILIYYFVMiyyIPTSRQLKRL 1068
Cdd:cd18551 119 TGVLTVVGAVVLMFLLDWVLTLVTLA-VVPLAFLII---LPLGRRIRKA 163
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
584-752 |
7.05e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 584 PVLKDLSATIKPGQLIAIVGSVGGGKSSLLSAVL--------DEMVLLDGRVKVGGSIAYVPQH----------SWIFNK 645
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysNDLTLFGRRRGSGETIWDIKKHigyvssslhlDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 646 TIKENIlfgneLSNYF-----YDQVVGSCQLKTDFRHFQQGENTMVGENGI-TLSGGQKARISLARAVYQDKDIYLLDDP 719
Cdd:PRK10938 354 SVRNVI-----LSGFFdsigiYQAVSDRQQKLAQQWLDILGIDKRTADAPFhSLSWGQQRLALIVRALVKHPTLLILDEP 428
|
170 180 190
....*....|....*....|....*....|....*
gi 392896924 720 LSAVDAhVGRALFDKVIgpDGLLR-SKTRVL-VTH 752
Cdd:PRK10938 429 LQGLDP-LNRQLVRRFV--DVLISeGETQLLfVSH 460
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
583-780 |
8.99e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.54 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 583 PPV--LKDLSATIKPGQLIAIVGSVGGGKSSL---LSAVLDE---MVLLDGR----------VKVGGSIAYvPQHSWIFN 644
Cdd:PRK09700 16 GPVhaLKSVNLTVYPGEIHALLGENGAGKSTLmkvLSGIHEPtkgTITINNInynkldhklaAQLGIGIIY-QELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 645 KTIKENILFGNELSNYF-------YDQVVGSCQLKTDFRHFQQGENTMVGEngitLSGGQKARISLARAVYQDKDIYLLD 717
Cdd:PRK09700 95 LTVLENLYIGRHLTKKVcgvniidWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896924 718 DPLSAV-DAHVgralfDKVIGPDGLLRS--KTRVLVTHNLQYTKYV-DTIYVIEDGQIVQHGSFEDI 780
Cdd:PRK09700 171 EPTSSLtNKEV-----DYLFLIMNQLRKegTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDV 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1232-1287 |
9.81e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.39 E-value: 9.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 392896924 1232 KNL--PLVLKNIDLKIEGGERIGVIGRTGSGKSSLTMALYRMIEGESGTIKIDDVEID 1287
Cdd:COG1129 260 EGLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR 317
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
273-547 |
9.81e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 39.72 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 273 PILLKQLIDYVSLHdQPLSFGIAIACIMFSCSTTRSLLQNYQIAGMCRQAVYYqtvLSNAILHKILRLSPSARSNRTAGE 352
Cdd:cd18551 19 PLLVKNLIDALSAG-GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLD---LRRRLWRRLLRLPVSFFDRRRSGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 353 ILNHAAVDI----EIIVHSVPylqNMWSVPFQVTLAMTMLAItLGW--AAMAGVCIMILFIPLNLCTSRFIKLSQQKQmk 426
Cdd:cd18551 95 LVSRVTNDTtllrELITSGLP---QLVTGVLTVVGAVVLMFL-LDWvlTLVTLAVVPLAFLIILPLGRRIRKASKRAQ-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896924 427 ikDERTKLS---NEMLNGIKVVKLYAWE----ESFEDQINRLRAKEVKMLRNVCILSRIVDVANAASpFLVAIGsftcYV 499
Cdd:cd18551 169 --DALGELSaalERALSAIRTVKASNAEeretKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLA-LLVVLG----VG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 392896924 500 LWSPDENGLTPS--VAFVaLTIFnQLRQPMRMVANLINTLVQARVSNKRL 547
Cdd:cd18551 242 GARVASGALTVGtlVAFL-LYLF-QLITPLSQLSSFFTQLQKALGALERI 289
|
|
| |
