|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
203-1478 |
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: 735.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 203 PFLSSESQE-TEVAEDGESWLSRFSYAWLAPLLARGVRGELQQP----------------------RDTCRLPRRlHPAF 259
Cdd:TIGR00957 190 PLFSETNHDpNPCPESSASFLSRITFWWITGMAVYGYRQPLEESdlwslnkedtsemvvpvlvenwKKECKKTRK-QPVS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 260 LA--RVFQAHWKEGAQ----------------------LWRALYRAFGCCYLALGLLKMVGTMLGFSGPLLLSLLVGFLE 315
Cdd:TIGR00957 269 AVygKKDPSKPKGSSQldaneevealivksphkprkpsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVN 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 316 EGQEPLSHGLLYvlglAGGTVISAVLQ----NQYGYEVRKVTLQARVAVLSTLYRKALKLGPS--RPPT-GEVLNLLGTD 388
Cdd:TIGR00957 349 DPMAPDWQGYFY----TGLLFVCACLQtlilHQYFHICFVSGMRIKTAVMGAVYRKALVITNSarKSSTvGEIVNLMSVD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 389 SERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLS 468
Cdd:TIGR00957 425 AQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILN 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 469 GIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYVLMGHQ--LTATKVFTALALVR 546
Cdd:TIGR00957 505 GIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFN 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 547 MLILPLNNFPWVINGLLESKVSLDRIQRFLDLPSYSPEAYYSPDPPAEPSTALELHEALFSW---DPIGASQKTFishlQ 623
Cdd:TIGR00957 585 ILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFTWardLPPTLNGITF----S 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 624 VKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselsKG-FGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEA 702
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM----KGsVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 703 CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI--LGVLSHTTRL 780
Cdd:TIGR00957 737 CALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRI 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 781 LCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAVPT-----AWAEKEQ---------VATSGQSP-------SVC 839
Cdd:TIGR00957 817 LVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEflrtyAPDEQQGhledswtalVSGEGKEAkliengmLVT 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 840 DLERTTEEELEVEQST-----------------------CGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAILVSLLL 896
Cdd:TIGR00957 897 DVVGKQLQRQLSASSSdsgdqsrhhgssaelqkaeakeeTWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVC 976
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 897 MQATRNGADWWLAHWlsqlkagrngsREDPAScspgstalfsprlllfspgnlytpllstplhkaasNGT-ADVHFYLIV 975
Cdd:TIGR00957 977 NHVSALASNYWLSLW-----------TDDPMV-----------------------------------NGTqNNTSLRLSV 1010
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 976 YATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANS 1055
Cdd:TIGR00957 1011 YGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSL 1090
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1056 VGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEEN 1135
Cdd:TIGR00957 1091 FNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQS 1170
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1136 QRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLVLSYALSLTGLLSGLVSSFTQTEA 1215
Cdd:TIGR00957 1171 DLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHS--LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMET 1248
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1216 MMVSVERLEEYSCDVPQEPHSQPLQSPHQqriSWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGK 1295
Cdd:TIGR00957 1249 NIVAVERLKEYSETEKEAPWQIQETAPPS---GWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGK 1325
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1296 SSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAV 1375
Cdd:TIGR00957 1326 SSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVS 1405
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1376 AM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN 1454
Cdd:TIGR00957 1406 ALpDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMD 1485
|
1370 1380
....*....|....*....|....
gi 24850123 1455 SDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:TIGR00957 1486 YTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
206-1475 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 685.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 206 SSESQETEVAEDGE--------SWLSRFSYAWLAPLLARGVRGELQQPrDTCRLPRRLHPAFLARVFQAHWKEGAQ---- 273
Cdd:PLN03130 211 SVDDYEYEELPGGEqicperhaNIFSRIFFGWMTPLMQLGYKRPLTEK-DVWKLDTWDQTETLYRSFQKCWDEELKkpkp 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 274 -LWRALYRAFGCCYLALGLLKMVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKV 352
Cdd:PLN03130 290 wLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNG-EPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRV 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 353 TLQARVAVLSTLYRKALKL---GPSRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLV 429
Cdd:PLN03130 369 GFRLRSTLVAAVFRKSLRLtheGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 430 LALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVY 509
Cdd:PLN03130 449 MLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSF 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 510 LWAALPVVICITIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLdlpsYSPEAYYSP 589
Cdd:PLN03130 529 ILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELL----LAEERVLLP 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 590 DPPAEPST-ALELHEALFSWDPigASQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKG 666
Cdd:PLN03130 605 NPPLEPGLpAISIKNGYFSWDS--KAERPTLSNinLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 667 FglATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKA 746
Cdd:PLN03130 683 Y--VPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 747 LYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL---PLVQAV---- 819
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSnngPLFQKLmena 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 820 --------PTAWAEKEQVATSGQSPSVCDLERTTEEELEVEQSTCGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAIL 891
Cdd:PLN03130 841 gkmeeyveENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWVVMIL 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 892 V-SLLLMQATRNGADWWLAHWLSQlkagrngsredpascspgstalfsprlllfSPGNLYTPLlstplhkaasngtadvh 970
Cdd:PLN03130 921 FlCYVLTEVFRVSSSTWLSEWTDQ------------------------------GTPKTHGPL----------------- 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 971 FYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNI 1050
Cdd:PLN03130 954 FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNM 1033
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1051 LLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYR 1130
Cdd:PLN03130 1034 FLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDR 1113
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1131 FEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLVLSYALSLTGLLSG 1205
Cdd:PLN03130 1114 MAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNgraenQAAFAS--TMGLLLSYALNITSLLTA 1191
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1206 LVSSFTQTEAMMVSVERLEEYsCDVPQEphSQPLQSPHQQRISWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKL 1285
Cdd:PLN03130 1192 VLRLASLAENSLNAVERVGTY-IDLPSE--APLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKV 1268
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1286 GIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQAL 1365
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESL 1348
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1366 EQCHLSEVAVAMG-GLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLT 1444
Cdd:PLN03130 1349 ERAHLKDVIRRNSlGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLI 1428
|
1290 1300 1310
....*....|....*....|....*....|.
gi 24850123 1445 IAHRLNTILNSDRVLVLQAGRVVELDSPSAL 1475
Cdd:PLN03130 1429 IAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
216-1475 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 683.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 216 EDGESWLSRFSYAWLAPLLARGVRGELQQpRDTCRLPRRLHPAFLARVFQAHWKEGAQ-----LWRALYRAFGCCYLALG 290
Cdd:PLN03232 229 ERYASIFSRIYFSWMTPLMQLGYRKPITE-KDVWQLDQWDQTETLIKRFQRCWTEESRrpkpwLLRALNNSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 291 LLKMVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALK 370
Cdd:PLN03232 308 IFKIGHDLSQFVGPVILSHLLQSMQEG-DPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 371 L---GPSRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMA 447
Cdd:PLN03232 387 LtheARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 448 SNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYV 527
Cdd:PLN03232 467 LTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 528 LMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLdlpsYSPEAYYSPDPPAEPST-ALELHEALF 606
Cdd:PLN03232 547 LLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL----LSEERILAQNPPLQPGApAISIKNGYF 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 607 SWDPIGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFglATQEPWIQCATIRDNIL 686
Cdd:PLN03232 623 SWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAY--VPQVSWIFNATVRENIL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 766
Cdd:PLN03232 701 FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 767 HRCILGVLSHTTRLLCTHRTEYLERADVVLLM------EAGQLVRTGPPSEILPLVQAVPTAWAEKEQVATSGQ-----S 835
Cdd:PLN03232 781 DSCMKDELKGKTRVLVTNQLHFLPLMDRIILVsegmikEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDEnilklG 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 836 PSV-CDLERTTEEELEVEQSTCGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAIL-VSLLLMQATRNGADWWLAHWLS 913
Cdd:PLN03232 861 PTVtIDVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILlVCYLTTEVLRVSSSTWLSIWTD 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 914 QlkagrngsrEDPASCSPGstalfsprlllfspgnlytpllstplhkaasngtadvhFYLIVYATIAGVNSLCTLLRAVL 993
Cdd:PLN03232 941 Q---------STPKSYSPG--------------------------------------FYIVVYALLGFGQVAVTFTNSFW 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 994 FAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLL 1073
Cdd:PLN03232 974 LISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISL 1053
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1074 LLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATM 1153
Cdd:PLN03232 1054 WAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSN 1133
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1154 QWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYsC 1228
Cdd:PLN03232 1134 RWLTIRLETLGGVMIWLTATFAVLRNgnaenQAGFAS--TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNY-I 1210
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1229 DVPQEphSQPLQSPHQQRISWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEP 1308
Cdd:PLN03232 1211 DLPSE--ATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEL 1288
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1309 NAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAMG-GLDGELGER 1387
Cdd:PLN03232 1289 EKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPfGLDAEVSEG 1368
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1388 GQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVV 1467
Cdd:PLN03232 1369 GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
....*...
gi 24850123 1468 ELDSPSAL 1475
Cdd:PLN03232 1449 EYDSPQEL 1456
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
274-1475 |
1.57e-169 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 550.92 E-value: 1.57e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 274 LWRALYRAFGCCYLALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVT 353
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 354 LQARVAVLSTLYRKALKLGP---SRPP--TGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGL 428
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSkslAQPDmnTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 429 VLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACV 508
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 509 YLWAALPVVICITIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFL-----------D 577
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLecdnatcstvqD 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 578 LPSYSPEAYYSP---------------------------------------------DPPAEPSTALELHEALFSWDPIG 612
Cdd:PTZ00243 554 MEEYWREQREHStacqlaavlenvdvtafvpvklprapkvktsllsralrmlcceqcRPTKRHPSPSVVVEDTDYGSPSS 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 613 AS------------QKTFIS--------------------------HLQVKKGMLVGIVGKVGCGKSSLLAAITGELhrl 654
Cdd:PTZ00243 634 ASrhiveggtggghEATPTSersaktpkmktddffelepkvllrdvSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF--- 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 655 cgwvavsELSKG-------FGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTL 727
Cdd:PTZ00243 711 -------EISEGrvwaersIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 728 SGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 808 PPSEIL--PLVQAVPTAWAEKEQVATSGQSPSVCDLERTTEEELEVEQS------------------TCGCLVQEESKSE 867
Cdd:PTZ00243 864 SSADFMrtSLYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPvakqegnaeggdgaaldaAAGRLMTREEKAS 943
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 868 GAVALHVYRAYWRAMGSGLAAAILVSLLLMQATRNGADwwlAHWLSQLKAGRNGSREDpascspgstalfspRLLLFSPG 947
Cdd:PTZ00243 944 GSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSS---GVWLSMWSTRSFKLSAA--------------TYLYVYLG 1006
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 948 NLYTPLLSTPLHkaasngtadvhFYLIVYATIAGVNSL-CTLLRAVlfaagalqaaaslhhrllhrlLMAPVTFYDSTPS 1026
Cdd:PTZ00243 1007 IVLLGTFSVPLR-----------FFLSYEAMRRGSRNMhRDLLRSV---------------------SRGTMSFFDTTPL 1054
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1027 GRVLNRFSSDVACVDDSLP----FLLNILLANSVGLLGLLAVLGSGLPWLLLLLpplsFVYYSVQGYYRASFRELRRLGS 1102
Cdd:PTZ00243 1055 GRILNRFSRDIDILDNTLPmsylYLLQCLFSICSSILVTSASQPFVLVALVPCG----YLYYRLMQFYNSANREIRRIKS 1130
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1103 LTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQG 1182
Cdd:PTZ00243 1131 VAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLR 1210
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1183 LA--NPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYSCDVPQE--------------------------- 1233
Cdd:PTZ00243 1211 ATsqEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEdmpeldeevdalerrtgmaadvtgtvv 1290
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1234 --PHSQPLQSPHQqriswLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAG 1311
Cdd:PTZ00243 1291 iePASPTSAAPHP-----VQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGG 1365
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1312 RVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQN 1390
Cdd:PTZ00243 1366 EIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRErVASESEGIDSRVLEGGSN 1445
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1391 LSLGQRQLLCLARALLT-DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVEL 1469
Cdd:PTZ00243 1446 YSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEM 1525
|
....*.
gi 24850123 1470 DSPSAL 1475
Cdd:PTZ00243 1526 GSPREL 1531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
220-1478 |
1.25e-118 |
|
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: 407.76 E-value: 1.25e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 220 SWLSRFSYAWLAPLLARGVRGELQQPrDTCRLPRRLHPAFLARVFQAHW-------KEGAQLWRALYRAFGCCYLALGLL 292
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELS-DIYQIPSFDSADNLSERLEREWdrelasaKKNPKLLNALRRCFFWRFVFYGIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 293 KMVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKL 371
Cdd:TIGR01271 89 LYFGEATKAVQPLLLGRIIAsYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 372 GP---SRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMAS 448
Cdd:TIGR01271 169 SSrvlDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 449 NQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVI---KYLDAACVYLWAALPVVICItifIT 525
Cdd:TIGR01271 249 RDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIaylRYFYSSAFFFSGFFVVFLSV---VP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 526 YVLMgHQLTATKVFTALALVRMLILPLN-NFPWVINGLLESKVSLDRIQRFLDLPSYSPEAYyspdppAEPSTALELHEA 604
Cdd:TIGR01271 326 YALI-KGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEY------NLTTTEVEMVNV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 605 LFSWDP-IG----------ASQKT-------FISHL-------------QVKKGMLVGIVGKVGCGKSSLLAAITGELHR 653
Cdd:TIGR01271 399 TASWDEgIGelfekikqnnKARKQpngddglFFSNFslyvtpvlknisfKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 654 LCGWVavsELSKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRA 733
Cdd:TIGR01271 479 SEGKI---KHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 734 RIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAG------------ 801
Cdd:TIGR01271 556 RISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGvcyfygtfselq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 802 ---------------------------------------------------QLVRTGPP--------SEIL--------- 813
Cdd:TIGR01271 636 akrpdfsslllgleafdnfsaerrnsiltetlrrvsidgdstvfsgpetikQSFKQPPPefaekrkqSIILnpiasarkf 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 814 PLVQAVPT-AWAEKEQVATSGQS-----------------PSVCDLERTTEEELEVEQSTCGcLVQEESKSEGAValHVY 875
Cdd:TIGR01271 716 SFVQMGPQkAQATTIEDAVREPSerkfslvpedeqgeeslPRGNQYHHGLQHQAQRRQSVLQ-LMTHSNRGENRR--EQL 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 876 RAYWRAMGSGLAAAILVSLLLMQATRNGADwwlahwlSQLKAGRNGSREDPASC-------SPGSTA-------LFSPRL 941
Cdd:TIGR01271 793 QTSFRKKSSITQQNELASELDIYSRRLSKD-------SVYEISEEINEEDLKECfaderenVFETTTwntylryITTNRN 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 942 LLFS----------------------PGNLYTPLLSTPLHKAASNG--------TADVHFYlIVYATIAGVNSLCTL--L 989
Cdd:TIGR01271 866 LVFVlifclviflaevaasllglwliTDNPSAPNYVDQQHANASSPdvqkpviiTPTSAYY-IFYIYVGTADSVLALgfF 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 990 RAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGL 1069
Cdd:TIGR01271 945 RGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQ 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1070 PWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFAS 1149
Cdd:TIGR01271 1025 PYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLY 1104
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1150 YATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYsCD 1229
Cdd:TIGR01271 1105 LSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKF-ID 1180
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1230 VPQEpHSQP--------------LQSPHQQRIsWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGK 1295
Cdd:TIGR01271 1181 LPQE-EPRPsggggkyqlstvlvIENPHAQKC-WPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGK 1258
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1296 SSLFLVLFRLLEPNaGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAV 1375
Cdd:TIGR01271 1259 STLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIE 1337
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1376 AM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN 1454
Cdd:TIGR01271 1338 QFpDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
1450 1460
....*....|....*....|....
gi 24850123 1455 SDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:TIGR01271 1418 CQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
289-572 |
5.42e-118 |
|
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: 371.88 E-value: 5.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 289 LGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKA 368
Cdd:cd18598 2 LGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 369 LKLGPSR---PPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRI 445
Cdd:cd18598 82 LRVRSSSlskFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 446 MASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFIT 525
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24850123 526 YVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1253-1472 |
9.57e-116 |
|
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: 362.58 E-value: 9.57e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1253 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 1332
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 1411
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLpGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1412 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1472
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
288-572 |
8.46e-107 |
|
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: 341.12 E-value: 8.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 288 ALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRK 367
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 368 ALKLGPS---RPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATR 444
Cdd:cd18559 81 ALRSPISffeRTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 445 IMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFI 524
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24850123 525 TYVLMGH--QLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18559 241 AYVSRHSlaGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
599-802 |
4.43e-96 |
|
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: 307.47 E-value: 4.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 599 LELHEALFSWDPiGASQKTFISH---LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelsKGFGLATQEPW 675
Cdd:cd03250 1 ISVEDASFTWDS-GEQETSFTLKdinLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP---GSIAYVSQEPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 676 IQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:cd03250 77 IQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24850123 756 AVDADVANHLLHRCILGVLSHT-TRLLCTHRTEYLERADVVLLMEAGQ 802
Cdd:cd03250 157 AVDAHVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
887-1226 |
1.64e-91 |
|
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: 298.67 E-value: 1.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 887 AAAILVSLLLMQATRNGADWWLAHWLSQLKagrngsredpascspgstalfsprlllfspgnlytpllstplHKAASNGT 966
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSN------------------------------------------NSFFNFIN 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 967 ADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPF 1046
Cdd:cd18605 39 DSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1047 LLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAG 1126
Cdd:cd18605 119 ILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1127 ATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGL-ANPGLVGLVLSYALSLTGLLSG 1205
Cdd:cd18605 199 KQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLsIDAGLIGLALSYALPITGLLSG 278
|
330 340
....*....|....*....|.
gi 24850123 1206 LVSSFTQTEAMMVSVERLEEY 1226
Cdd:cd18605 279 LLNSFTETEKEMVSVERVRQY 299
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1017-1478 |
4.35e-91 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 307.86 E-value: 4.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1017 PVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSG----LPWLLLLLPPLSFVYYSVQGYYRA 1092
Cdd:COG1132 108 PLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIdwrlALIVLLVLPLLLLVLRLFGRRLRK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1093 SFRELR-RLGSLTwsplySHLADTLAGLPVLRAAGATY----RFEEENQRLLELNQRcqfaSYATMQWLDIRLQLMGAAV 1167
Cdd:COG1132 188 LFRRVQeALAELN-----GRLQESLSGIRVVKAFGREEreleRFREANEELRRANLR----AARLSALFFPLMELLGNLG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1168 VSAIAGIALVQHQQGLANPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEY---SCDVPQEPHSQPLQSPhq 1244
Cdd:COG1132 259 LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELldePPEIPDPPGAVPLPPV-- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1245 qriswltQGSVEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLE 1324
Cdd:COG1132 337 -------RGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1325 LAELRSQLAVIPQEPFLFSGTIRENL---DPQglHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLC 1400
Cdd:COG1132 409 LESLRRQIGVVPQDTFLFSGTIRENIrygRPD--ATDEEVEEAAKAAQAHEFIEALpDGYDTVVGERGVNLSGGQRQRIA 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1401 LARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1249-1472 |
1.87e-85 |
|
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: 277.76 E-value: 1.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1249 WLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAEL 1328
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1329 RSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEqchlsevaVAMGGLdgelgergqNLSLGQRQLLCLARALLTD 1408
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR--------VSEGGL---------NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1409 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1472
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1081-1478 |
1.56e-79 |
|
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: 278.64 E-value: 1.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1081 FVYYSVQGYYRASFRELRRLGSLtwspLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRL 1160
Cdd:COG2274 310 LLGLLFQPRLRRLSREESEASAK----RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1161 QLMGAAVVSAI--AGIALVQHQQ-------------GLANPGLVGLVLSyalsltgllsglVSSFTQteaMMVSVERLEE 1225
Cdd:COG2274 386 GLLQQLATVALlwLGAYLVIDGQltlgqliafnilsGRFLAPVAQLIGL------------LQRFQD---AKIALERLDD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1226 YScDVPQEPHSQPLQSPHQQriswlTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL 1305
Cdd:COG2274 451 IL-DLPPEREEGRSKLSLPR-----LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1306 LEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQglHEDRALWQALEQCHLSEVAVAM-GGLD 1381
Cdd:COG2274 525 YEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALpMGYD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1382 GELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVL 1461
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
410
....*....|....*..
gi 24850123 1462 QAGRVVELDSPSALRNQ 1478
Cdd:COG2274 683 DKGRIVEDGTHEELLAR 699
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
289-572 |
1.06e-77 |
|
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: 258.95 E-value: 1.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 289 LGLLKMVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRK 367
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 368 ALKLGPS---RPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATR 444
Cdd:cd18579 82 ALRLSSSarqETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 445 IMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFI 524
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24850123 525 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1253-1478 |
1.31e-71 |
|
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: 239.05 E-value: 1.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1253 GSVEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 1332
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQ-ALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAK 1410
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLpNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1411 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1091-1478 |
5.78e-71 |
|
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: 249.29 E-value: 5.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1091 RASFRELRRLGSltwsplysHLADTLAGLPVLRAAGATyrfEEENQRLLELNQRcqfasY--ATMQWLdiRLQLM----- 1163
Cdd:COG4988 187 RRQWRALARLSG--------HFLDRLRGLTTLKLFGRA---KAEAERIAEASED-----FrkRTMKVL--RVAFLssavl 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1164 ------GAAVVSAIAGIALVQHQQGLAnPGLVGLVLS---YALSLTgllsglVSSFTQTEAM-MVSVERLEEyscdVPQE 1233
Cdd:COG4988 249 effaslSIALVAVYIGFRLLGGSLTLF-AALFVLLLApefFLPLRD------LGSFYHARANgIAAAEKIFA----LLDA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1234 PHSQPLQSphQQRISWLTQGSVEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV 1313
Cdd:COG4988 318 PEPAAPAG--TAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1314 LLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQ 1389
Cdd:COG4988 395 LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPDA--SDEELEAALEAAGLDEFVAALpDGLDTPLGEGGR 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1390 NLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVEL 1469
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
....*....
gi 24850123 1470 DSPSALRNQ 1478
Cdd:COG4988 553 GTHEELLAK 561
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
290-572 |
2.12e-67 |
|
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: 229.28 E-value: 2.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 290 GLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKAL 369
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 370 KLGP-SRP--PTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIM 446
Cdd:cd18595 83 RLSNsARKksTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 447 ASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITY 526
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24850123 527 VLMG--HQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18595 243 VLSDpdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1253-1478 |
4.03e-67 |
|
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: 227.48 E-value: 4.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1253 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 1332
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 1411
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1412 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1255-1465 |
7.97e-67 |
|
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: 223.03 E-value: 7.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSGTIRENLdpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCI 1414
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1415 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGR 1465
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1255-1468 |
2.83e-63 |
|
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: 215.56 E-value: 2.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAK 1410
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGATREE--VEEAARAANAHEFIMELpEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1411 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1016-1468 |
8.18e-60 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 216.89 E-value: 8.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1016 APVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFR 1095
Cdd:TIGR02203 100 LPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1096 ELRRLGSLTWSPLYSHLADTLAGLPVLRAAGA----TYRFEEENQRLLELNQRCQFASYAtmqwLDIRLQLMGAAVVSAI 1171
Cdd:TIGR02203 180 RISKEIQNSMGQVTTVAEETLQGYRVVKLFGGqayeTRRFDAVSNRNRRLAMKMTSAGSI----SSPITQLIASLALAVV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1172 AGIALVQHQQGLANPG-LVGLVLSYALSLTGLLSGL-VSSFTQTeaMMVSVERLEEYsCDVPQEPHSQPLqspHQQRIsw 1249
Cdd:TIGR02203 256 LFIALFQAQAGSLTAGdFTAFITAMIALIRPLKSLTnVNAPMQR--GLAAAESLFTL-LDSPPEKDTGTR---AIERA-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1250 ltQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 1329
Cdd:TIGR02203 328 --RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLR 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQEPFLFSGTIRENL---DPQGLHEDRALwQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARAL 1405
Cdd:TIGR02203 406 RQVALVSQDVVLFNDTIANNIaygRTEQADRAEIE-RALAAAYAQDFVDKLpLGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1406 LTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1255-1475 |
1.54e-59 |
|
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: 204.70 E-value: 1.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVY--RPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 1332
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSGTIRENL-----DPQGLHEDRALWQALeqCHlSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLT 1407
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDATDEEVEEAAKKAN--IH-DFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1408 DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 1475
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1255-1475 |
1.89e-59 |
|
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: 204.39 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAK 1410
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDATDEE--VIEAAKAAQIHDKIMRFpDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1411 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 1475
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
288-572 |
2.34e-58 |
|
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: 204.27 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 288 ALGLLKMVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYR 366
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDpGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 367 KALKL----GPSRPP------------------TGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAF 424
Cdd:cd18596 81 KALRRrdksGSSKSSeskkkdkeededekssasVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 425 LAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLD 504
Cdd:cd18596 161 LVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 505 AACVYLWAALPVVICITIFITYVL-MGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18596 241 LLLSLLWFLIPILVTVVTFATYTLvMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
888-1227 |
1.19e-57 |
|
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: 201.58 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 888 AAILVSLLLMQATRNGADWWLAHWLSQlkagrngsredpascspgstalfsprlllfspgnlytpllstplhkAASNGTA 967
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD----------------------------------------------WSSSPNS 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 968 DVHFYLIVYATIAGVNS-LCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPF 1046
Cdd:cd18580 36 SSGYYLGVYAALLVLASvLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1047 LLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAG 1126
Cdd:cd18580 116 ALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1127 ATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLVLSYALSLTGLLSGL 1206
Cdd:cd18580 196 WQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSS--ISAGLVGLALTYALSLTGSLQWL 273
|
330 340
....*....|....*....|.
gi 24850123 1207 VSSFTQTEAMMVSVERLEEYS 1227
Cdd:cd18580 274 VRQWTELETSMVSVERILEYT 294
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1253-1467 |
1.81e-56 |
|
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: 195.12 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1253 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 1332
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSGTIRENL---DPqgLHEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTD 1408
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAP--LADDERILRAAELAGVTDfVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1409 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVV 1467
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1255-1468 |
5.67e-54 |
|
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: 188.85 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSGTIRENL---DPqGLHEDRALWQA-LEQCH--LSEVAVamgGLDGELGERGQNLSLGQRQLLCLARALLTD 1408
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP-GMSMERVIEAAkLAGAHdfISELPE---GYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1409 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
290-572 |
1.02e-53 |
|
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: 189.97 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 290 GLLKMVGTMLGFSGPLLLSLLVGFLEEGQE-----PLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTL 364
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 365 YRKALKL-GPSR--PPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVI 441
Cdd:cd18597 83 YRKSLRLsGKSRheFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 442 ATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICIT 521
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 522 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1229-1468 |
1.91e-53 |
|
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: 198.51 E-value: 1.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1229 DVPQE----PHSQPLQsphqqriswLTQGSVEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFR 1304
Cdd:COG5265 337 DQPPEvadaPDAPPLV---------VGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1305 LLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSE-VAVAMGGL 1380
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDASEEE--VEAAARAAQIHDfIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1381 DGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLV 1460
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
....*...
gi 24850123 1461 LQAGRVVE 1468
Cdd:COG5265 565 LEAGRIVE 572
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
606-801 |
2.67e-52 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 183.30 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 606 FSWDPiGASQKTFIShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCG---WVAVSELSKGF-----------GLAT 671
Cdd:cd03290 8 FSWGS-GLATLSNIN-IRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhWSNKNESEPSFeatrsrnrysvAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 672 QEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:cd03290 86 QKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 752 DPLAAVDADVANHLLHRCILGVLSHTTR--LLCTHRTEYLERADVVLLMEAG 801
Cdd:cd03290 166 DPFSALDIHLSDHLMQEGILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDG 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1020-1479 |
1.29e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 195.33 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1020 FYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLA---VLGSGLPWLLLLLPPLSFVYYSVQG-YYRASFR 1095
Cdd:TIGR00958 251 FFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGfmlWLSPRLTMVTLINLPLVFLAEKVFGkRYQLLSE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1096 ELRR-LGSLTWSPLyshlaDTLAGLPVLRAAGA----TYRFEEENQRLLELNQRCQFAsYATMQWLDiRLQLMGAAVVSA 1170
Cdd:TIGR00958 331 ELQEaVAKANQVAE-----EALSGMRTVRSFAAeegeASRFKEALEETLQLNKRKALA-YAGYLWTT-SVLGMLIQVLVL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1171 IAGIALVQHQQgLANPGLVGLVLsYALSLTGLLSGLVSSFTQteaMMVSV---ERLEEYSCDVPQEPHSQPLQSPHqqri 1247
Cdd:TIGR00958 404 YYGGQLVLTGK-VSSGNLVSFLL-YQEQLGEAVRVLSYVYSG---MMQAVgasEKVFEYLDRKPNIPLTGTLAPLN---- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1248 swlTQGSVEFQDVVLVY--RPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL 1325
Cdd:TIGR00958 475 ---LEGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1326 AELRSQLAVIPQEPFLFSGTIRENLdPQGLH--EDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLA 1402
Cdd:TIGR00958 551 HYLHRQVALVGQEPVLFSGSVRENI-AYGLTdtPDEEIMAAAKAANAHDFIMEFpNGYDTEVGEKGSQLSGGQKQRIAIA 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1403 RALLTDAKILCIDEATASVDQKTDQLLQQTicKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
269-813 |
8.99e-51 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 189.99 E-value: 8.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 269 KEGAQLWRALYRAFGCC---YLALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQePLSHGLLYVLGLAGGTVISAVLQNQY 345
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 346 GYEVRKVTLQARVAVLSTLYRKALKLGPS---RPPTGEVLNLLGTDSERLLNFAG-SFHEAWGLPLQLAITL-YLLYQQV 420
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSffdRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALvVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 421 GMAFLAGLVLALLLVPVnKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKAcRTKELGR--LR 498
Cdd:COG1132 162 RLALIVLLVLPLLLLVL-RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE-ANEELRRanLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 499 VIKYLDA--ACVYLWAALPVVICITIFITYVLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFL 576
Cdd:COG1132 240 AARLSALffPLMELLGNLGLALVLLVGGLLVLSG-SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 577 DLPSYSPEAYySPDPPAEPSTALELHEALFSWDPigaSQKTF--IShLQVKKGMLVGIVGKVGCGKSSLLAAIT------ 648
Cdd:COG1132 319 DEPPEIPDPP-GAVPLPPVRGEIEFENVSFSYPG---DRPVLkdIS-LTIPPGETVALVGPSGSGKSTLVNLLLrfydpt 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 649 -GELhRLCGwVAVSELS-----KGFGLATQEPWIQCATIRDNILFGK---TfDAQLyREVLEACALNDDLSILPAGDQTE 719
Cdd:COG1132 394 sGRI-LIDG-VDIRDLTleslrRQIGVVPQDTFLFSGTIRENIRYGRpdaT-DEEV-EEAAKAAQAHEFIEALPDGYDTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 720 VGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLME 799
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE-ALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
570
....*....|....
gi 24850123 800 AGQLVRTGPPSEIL 813
Cdd:COG1132 549 DGRIVEQGTHEELL 562
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
963-1227 |
6.38e-49 |
|
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: 176.52 E-value: 6.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 963 SNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDD 1042
Cdd:cd18603 34 TQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1043 SLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVL 1122
Cdd:cd18603 114 TLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1123 RAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlaNPGLVGLVLSYALSLTGL 1202
Cdd:cd18603 194 RAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSL--SPGLVGLSISYALQITQT 271
|
250 260
....*....|....*....|....*
gi 24850123 1203 LSGLVSSFTQTEAMMVSVERLEEYS 1227
Cdd:cd18603 272 LNWLVRMTSELETNIVSVERIKEYS 296
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1106-1468 |
1.34e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 184.01 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1106 SPLYSHLADTLAGLPVLRaagaTY-RFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAA-----VVSAIAGIALvqH 1179
Cdd:PRK13657 192 HDLFAHVSDAIGNVSVVQ----SYnRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAAstitmLAILVLGAAL--V 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1180 QQGLANPGLVGLVLSYALSLTGLLSGLVSSFTQTeamMVSVERLEEY------SCDVPQEPHSQPLQSphqqriswlTQG 1253
Cdd:PRK13657 266 QKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQV---FMAAPKLEEFfevedaVPDVRDPPGAIDLGR---------VKG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLA 1333
Cdd:PRK13657 334 AVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1334 VIPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 1409
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIrvgRPDATDEE--MRAAAERAQAHDfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1410 KILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
322-813 |
8.65e-47 |
|
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: 180.80 E-value: 8.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 322 SHGLLYVL--GLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKLGPS---RPPTGEVLNLLGtDSERLLNF- 395
Cdd:COG2274 191 DLSTLWVLaiGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSffeSRSVGDLASRFR-DVESIREFl 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 396 AGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKF 475
Cdd:COG2274 270 TGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 476 F--------RWEQALGDRVKAcrtkelgRLRVIKYLDAAcvYLWA-ALPVV--ICITIFITYVLMGHQLTATKVFTALAL 544
Cdd:COG2274 350 LgaesrfrrRWENLLAKYLNA-------RFKLRRLSNLL--STLSgLLQQLatVALLWLGAYLVIDGQLTLGQLIAFNIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 545 VRMLILPLNNFPWVINGLLESKVSLDRIQRFLDLPSySPEAYYSPDPPAEPSTALELHEALFSWDPigASQKTF--IShL 622
Cdd:COG2274 421 SGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPP-EREEGRSKLSLPRLKGDIELENVSFRYPG--DSPPVLdnIS-L 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 623 QVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKTF- 691
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidpASLRRQIGVVLQDVFLFSGTIRENITLGDPDa 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 692 -DAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcI 770
Cdd:COG2274 577 tDEEI-IEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-L 654
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24850123 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG2274 655 RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
889-1227 |
1.53e-46 |
|
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: 169.19 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 889 AILVSLLLMQATRNGADWWLAHWLSQlkagrngsredpascspgstalfsprlllfspgnlyTPLLSTplhkaasngtad 968
Cdd:cd18606 3 LLLLLLILSQFAQVFTNLWLSFWTED------------------------------------FFGLSQ------------ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 969 vHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLL 1048
Cdd:cd18606 35 -GFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1049 NILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGAT 1128
Cdd:cd18606 114 RMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1129 YRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVqhQQGLANPGLVGLVLSYALSLTGLLSGLVS 1208
Cdd:cd18606 194 DRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVT--RRFSISPSSTGLVLSYVLQITQVLSWLVR 271
|
330
....*....|....*....
gi 24850123 1209 SFTQTEAMMVSVERLEEYS 1227
Cdd:cd18606 272 QFAEVENNMNSVERLLHYA 290
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1253-1478 |
4.57e-46 |
|
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: 167.34 E-value: 4.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1253 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNaGRVLLDNVDTSQLELAELRSQL 1332
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 1411
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1412 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
887-1227 |
4.36e-45 |
|
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: 165.85 E-value: 4.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 887 AAAILVSLLLMQATRNGADWWLAHWLSQ-LKAGRNGSREDPASCSPGSTALFSPRLLLFSPGNLYTPLLSTPLHKAAS-N 964
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEAnHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGlR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 965 GTADVHFylivyatiagvnslcTLLRAVLfaagalqaaaslhhrllhrllMAPVTFYDSTPSGRVLNRFSSDVACVDDSL 1044
Cdd:cd18602 81 AARRLHD---------------RMLRNIV---------------------RAPMRFFDTTPIGRILNRFSSDTNVIDQKL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1045 PFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRA 1124
Cdd:cd18602 125 PTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1125 AGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLVLSYALSLTGLLS 1204
Cdd:cd18602 205 FRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLN 284
|
330 340
....*....|....*....|...
gi 24850123 1205 GLVSSFTQTEAMMVSVERLEEYS 1227
Cdd:cd18602 285 WVVRNLADVEMQMNSVERVLEYT 307
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1091-1461 |
2.77e-44 |
|
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: 169.77 E-value: 2.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1091 RASFRELRRLGSltwsplysHLADTLAGLPVLRAAGATyrfEEENQRLLELNQrcQFASyATMQWLdiRLQLMGAAVVSA 1170
Cdd:TIGR02857 173 RKQWAALSRLSG--------HFLDRLRGLPTLKLFGRA---KAQAAAIRRSSE--EYRE-RTMRVL--RIAFLSSAVLEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1171 IA--GIALVQHQQGLA--------NPGLVGLVLsyALSLTGLLSGLVSSFTQTEAMMVSVERLEEYscdvpQEPHSQPLQ 1240
Cdd:TIGR02857 237 FAtlSVALVAVYIGFRllagdldlATGLFVLLL--APEFYLPLRQLGAQYHARADGVAAAEALFAV-----LDAAPRPLA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1241 SphQQRISWLTQGSVEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDT 1320
Cdd:TIGR02857 310 G--KAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1321 SQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQR 1396
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEfVAALPQGLDTPIGEGGAGLSGGQA 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1397 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVL 1461
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
622-812 |
3.69e-44 |
|
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: 162.33 E-value: 3.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavsELSKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLE 701
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 702 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLL 781
Cdd:cd03291 135 ACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRIL 214
|
170 180 190
....*....|....*....|....*....|.
gi 24850123 782 CTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03291 215 VTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1252-1466 |
4.51e-44 |
|
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: 159.94 E-value: 4.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1252 QGSVEFQDVVLVY--RPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 1329
Cdd:cd03248 9 KGIVKFQNVTFAYptRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQEPFLFSGTIRENLdPQGLH--EDRALWQALEQCH----LSEVAVamgGLDGELGERGQNLSLGQRQLLCLAR 1403
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNI-AYGLQscSFECVKEAAQKAHahsfISELAS---GYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1404 ALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRV 1466
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1250-1468 |
1.13e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 168.85 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1250 LTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 1329
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALL 1406
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1407 TDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
888-1227 |
1.14e-43 |
|
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: 161.10 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 888 AAILVSLLLMQATRNGADWWLAHWLSQlkagrngsredpascspgstalfsprlllfspgnlYTPLLSTPlhkaasngTA 967
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASA-----------------------------------YETSSALP--------PS 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 968 DVH--FYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLP 1045
Cdd:cd18604 39 EVSvlYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1046 FLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSV-QGYYRASfRELRRLGSLTWSPLYSHLADTLAGLPVLRA 1124
Cdd:cd18604 119 DSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIgRLYLRAS-RELKRLESVARSPILSHFGETLAGLVTIRA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1125 AGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQqglANPGLVGLVLSYALSLTGLLS 1204
Cdd:cd18604 198 FGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPG---IDAGLAGFSLSFALGFSSAIL 274
|
330 340
....*....|....*....|...
gi 24850123 1205 GLVSSFTQTEAMMVSVERLEEYS 1227
Cdd:cd18604 275 WLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
883-1227 |
9.51e-43 |
|
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: 159.27 E-value: 9.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 883 GSGLAAAILVSLLLMQATRNGADWWLAHWLSQlKAGRNGSREDPASCSPGSTalfsprlllfspgnlytpllstplhkaa 962
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQ-GSGNTTNNVDNSTVDSGNI---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 963 sNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDD 1042
Cdd:cd18599 52 -SDNPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1043 SLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVL 1122
Cdd:cd18599 131 RLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1123 RAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHqqGLANPGLVGLVLSYALSLTGL 1202
Cdd:cd18599 211 HAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLK--GSISPAFAGLALSYALQLSGL 288
|
330 340
....*....|....*....|....*
gi 24850123 1203 LSGLVSSFTQTEAMMVSVERLEEYS 1227
Cdd:cd18599 289 FQFTVRLASETEARFTSVERILEYI 313
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1252-1468 |
1.15e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 165.96 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1252 QGSVEFQDVVLVYrPGLPN-ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRS 1330
Cdd:PRK11176 339 KGDIEFRNVTFTY-PGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1331 QLAVIPQEPFLFSGTIRENLD--PQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLT 1407
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMdNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1408 DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
313-573 |
2.25e-42 |
|
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: 157.41 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 313 FLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKLGP---SRPPTGEVLNLLGTDS 389
Cdd:cd18594 27 FVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSsalSKITTGHIVNLLSNDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 390 ERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSG 469
Cdd:cd18594 107 QKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 470 IRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYVLMGHQLTATKVFTALAL---VR 546
Cdd:cd18594 187 MRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLlnaLR 266
|
250 260
....*....|....*....|....*..
gi 24850123 547 MLIlpLNNFPWVINGLLESKVSLDRIQ 573
Cdd:cd18594 267 MTI--TRFFPESIQTLSESRVSLKRIQ 291
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1115-1479 |
1.67e-41 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 163.97 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1115 TLAGLPVLRAAGATYRFeeenqrllelnqrcqFAS----YATMQWLDIRLQLMGAAVVSAIAGIALVQhqqGLANPGLVG 1190
Cdd:TIGR03797 320 LINGISKLRVAGAENRA---------------FARwaklFSRQRKLELSAQRIENLLTVFNAVLPVLT---SAALFAAAI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1191 LVLSYALSLTGLLSGLVSSFTQ-TEAMMVSVERLEEYSCDVPQEPHSQPL---------QSPHQQRISwltqGSVEFQDV 1260
Cdd:TIGR03797 382 SLLGGAGLSLGSFLAFNTAFGSfSGAVTQLSNTLISILAVIPLWERAKPIlealpevdeAKTDPGKLS----GAIEVDRV 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1261 VLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPF 1340
Cdd:TIGR03797 458 TFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGR 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1341 LFSGTIRENL-DPQGLHEDRAlWQALEQCHLSEVAVAMG-GLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEAT 1418
Cdd:TIGR03797 538 LMSGSIFENIaGGAPLTLDEA-WEAARMAGLAEDIRAMPmGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1419 ASVDQKTDQLLQQTICKrfANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:TIGR03797 617 SALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1211-1468 |
3.75e-41 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 161.42 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1211 TQTEAMM----VSVERLEEYsCDVPQEPH---SQPLQSphqqriswltqGSVEFQDVVLVYRPGLPnALDGVTFRVEPGE 1283
Cdd:PRK10790 302 TTQQSMLqqavVAGERVFEL-MDGPRQQYgndDRPLQS-----------GRIDIDNVSFAYRDDNL-VLQNINLSVPSRG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1284 KLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLD-PQGLHEDRaLW 1362
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTlGRDISEEQ-VW 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1363 QALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKT 1441
Cdd:PRK10790 448 QALETVQLAELARSLpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT 527
|
250 260
....*....|....*....|....*..
gi 24850123 1442 VLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:PRK10790 528 LVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1256-1466 |
8.45e-41 |
|
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: 148.52 E-value: 8.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1256 EFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 1335
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1336 PQEPFLFSGTIRENLdpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCID 1415
Cdd:cd03246 82 PQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1416 EATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 1466
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1108-1449 |
9.92e-41 |
|
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: 159.06 E-value: 9.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1108 LYSHLADTLAGLPVLRAAGATYRF----EEENQRLLELNQRcqfasyatmqwlDIRLQLMGAAVVSAIAGIA----LVQH 1179
Cdd:TIGR02868 192 LAAQLTDALDGAAELVASGALPAAlaqvEEADRELTRAERR------------AAAATALGAALTLLAAGLAvlgaLWAG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1180 QQGLANPGLVGLVLSYALSLTGLLSGLVSSFT----QTEAMMVSVERLEEyscdVPQEPHSQPLQSPHQQRISWLTQGSV 1255
Cdd:TIGR02868 260 GPAVADGRLAPVTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAERIVE----VLDAAGPVAEGSAPAAGAVGLGKPTL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1256 EFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 1335
Cdd:TIGR02868 336 ELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1336 PQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 1411
Cdd:TIGR02868 415 AQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADwLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
330 340 350
....*....|....*....|....*....|....*...
gi 24850123 1412 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRL 1449
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1236-1479 |
1.14e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 160.01 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1236 SQPLQSPHQQRISWLTQGSVEF--QDVVlVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRV 1313
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIeaEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1314 LLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQ 1389
Cdd:PRK11174 407 KINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEfLPLLPQGLDTPIGDQAA 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1390 NLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVEL 1469
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
250
....*....|
gi 24850123 1470 DSPSALRNQP 1479
Cdd:PRK11174 565 GDYAELSQAG 574
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1255-1468 |
1.22e-40 |
|
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: 148.23 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAV 1334
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSGTIRENLdpqglhedralwqaleqchlsevavamggldgelgerGQNLSLGQRQLLCLARALLTDAKILCI 1414
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1415 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
522-813 |
7.06e-40 |
|
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: 157.23 E-value: 7.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 522 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFpwvinGL-----LESKVSLDRIQRFLDLPSYSPEAYYSPDPPAEPS 596
Cdd:COG4988 261 VYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDL-----GSfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPP 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 597 TaLELHEALFSWDPIGASQKtFIShLQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS-----K 665
Cdd:COG4988 336 S-IELEDVSFSYPGGRPALD-GLS-LTIPPGERVALVGPSGAGKSTLLNLLLGFLPpysgsiLING-VDLSDLDpaswrR 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 666 GFGLATQEPWIQCATIRDNILFGKTF--DAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ 743
Cdd:COG4988 412 QIAWVPQNPYLFAGTIRENLRLGRPDasDEEL-EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLR 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 744 EKALYLLDDPLAAVDADVANHLLHRcILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1231-1479 |
6.67e-39 |
|
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: 153.14 E-value: 6.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1231 PQEPHSQPLQSPHQQRISWLTQGS---VEFQDVVLVYRPGLPN---ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFR 1304
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1305 LLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPF--LFSG-TIRENL-DPQGLH--------EDRALwQALEQCh 1369
Cdd:COG1123 314 LLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPYssLNPRmTVGDIIaEPLRLHgllsraerRERVA-ELLERV- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1370 lsevavamgGLDGELGER--GQnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLT 1444
Cdd:COG1123 392 ---------GLPPDLADRypHE-LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVqAQILNllRDLQREL-GLTYLF 460
|
250 260 270
....*....|....*....|....*....|....*.
gi 24850123 1445 IAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:COG1123 461 ISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
447-813 |
9.80e-39 |
|
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: 153.77 E-value: 9.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 447 ASNQEMLRHKDARVKLMTELLSGIRVIKFF-RWEQALG--DRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIF 523
Cdd:COG4987 182 RAGRRLAAARAALRARLTDLLQGAAELAAYgALDRALArlDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 524 ITYVLMGHQ---LTATKVFTALALVRMLiLPLnnfPWVINGLLESKVSLDRIQRFLDLPSYSPEAYYSPDPPAEPStaLE 600
Cdd:COG4987 262 APLVAAGALsgpLLALLVLAALALFEAL-APL---PAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPS--LE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 601 LHEALFSWDpiGASQKTF--IShLQVKKGMLVGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSKGF 667
Cdd:COG4987 336 LEDVSFRYP--GAGRPVLdgLS-LTLPPGERVAIVGPSGSGKSTLLALLLRFLdpqsgsitlggVDLRDL-DEDDLRRRI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 668 GLATQEPWIQCATIRDNILFGK---TfDAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE 744
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLRLARpdaT-DEEL-WAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRD 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 745 KALYLLDDPLAAVDADVANHLLHRcILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
290-572 |
1.92e-38 |
|
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: 146.61 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 290 GLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLS-----HGLLYV-----LG----LAGGTVISAVLQN---QYGYEVRKV 352
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEENTYSSSnstdkLSVSYVtveefFSngyvLAVILFLALLLQAtfsQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 353 T-LQARVAVLSTLYRKALKLGPSRPP-----TGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLA 426
Cdd:cd18591 83 EgIRLKTALQAMIYEKALRLSSWNLSsgsmtIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 427 GLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELgrlrviKYLDAA 506
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKEL------KLLLKD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 507 CVY------LWAALPVVICITIFITYVLMGHQ-LTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18591 237 AVYwslmtfLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1253-1478 |
3.03e-38 |
|
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: 154.51 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1253 GSVEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 1332
Cdd:TIGR01193 472 GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSGTIRENL---DPQGLHEDRaLWQALEQCHLSEVAVAMG-GLDGELGERGQNLSLGQRQLLCLARALLTD 1408
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLllgAKENVSQDE-IWAACEIAEIKDDIENMPlGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1409 AKILCIDEATASVdqktDQLLQQTICKRFAN---KTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:TIGR01193 630 SKVLILDESTSNL----DTITEKKIVNNLLNlqdKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1221-1467 |
1.52e-37 |
|
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: 150.28 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1221 ERLEEYSCDVPQEPHSQPLQSPhqqriswltQGSVEFQDVVLVYrPGLPNA-LDGVTFRVEPGEKLGIVGRTGSGKSSLF 1299
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPRP---------KGRLSVENLTVVP-PGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1300 LVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIREN------LDPQ---------GLHEdraLWQA 1364
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENiarfgdADPEkvvaaaklaGVHE---MILR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1365 LEQchlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVL 1443
Cdd:COG4618 453 LPD-----------GYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVV 521
|
250 260
....*....|....*....|....
gi 24850123 1444 TIAHRLNTILNSDRVLVLQAGRVV 1467
Cdd:COG4618 522 VITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
885-1227 |
2.49e-37 |
|
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: 143.62 E-value: 2.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 885 GLAAAILVSLL--LMQATRNGADWWLAHWL-SQLKAGRNgsredpascspgstalfsprlllFSPGNLYTPLLSTPLHKa 961
Cdd:cd18601 1 GVFVFILLVLLniAAQVLYVLSDWWLSYWAnLEEKLNDT-----------------------TDRVQGENSTNVDIEDL- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 962 asngtaDVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVD 1041
Cdd:cd18601 57 ------DRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1042 DSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPV 1121
Cdd:cd18601 131 DLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1122 LRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVqhqqgLA---NPGLVGLVLSYALS 1198
Cdd:cd18601 211 IRAYSAQERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLF-----LAeslDAGLVGLSLSYALT 285
|
330 340
....*....|....*....|....*....
gi 24850123 1199 LTGLLSGLVSSFTQTEAMMVSVERLEEYS 1227
Cdd:cd18601 286 LMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1256-1465 |
3.40e-37 |
|
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: 139.52 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1256 EFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 1335
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1336 PQEPF--LFSGTIRE----NLDPQGLHED---RALWQALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLARALL 1406
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafGLENLGLPEEeieERVEEALELV----------GLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1407 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGR 1465
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1255-1468 |
1.10e-36 |
|
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: 138.79 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRP--GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 1329
Cdd:cd03257 2 LEVKNLSVSFPTggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQEPFL---FSGTIRENL-DPQGLHE-DRALWQALEQCHLSEVAVamgGLDGELGER--GQnLSLGQRQLLCLA 1402
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIaEPLRIHGkLSKKEARKEAVLLLLVGV---GLPEEVLNRypHE-LSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1403 RALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
320-572 |
1.39e-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: 140.43 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 320 PLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKLGPS---RPPTGEVLNLLGTDSERLLNFA 396
Cdd:cd18593 35 SLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAalgKTTVGQIVNLLSNDVNRFDQAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 397 GSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIAtRIMASN-QEMLRHKDARVKLMTELLSGIRVIKF 475
Cdd:cd18593 115 LFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-KLFSKLrRKTAARTDKRIRIMNEIINGIRVIKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 476 FRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYVLMGHQLTATKVFTALALVRMLILPLNN- 554
Cdd:cd18593 194 YAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLf 273
|
250
....*....|....*...
gi 24850123 555 FPWVINGLLESKVSLDRI 572
Cdd:cd18593 274 FPFAIQFGSELSVSIRRI 291
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1272-1419 |
2.82e-36 |
|
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: 134.70 E-value: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG-TIRENL 1350
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1351 -------DPQGLHEDRALWQALEQchlsevaVAMGGLDGE-LGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1255-1465 |
3.38e-34 |
|
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: 130.67 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPG---LPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlelaELRSQ 1331
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1332 LAVIPQEPFLFSGTIRENL---DPqgLHEDRaLWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLT 1407
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKP--FDEER-YEKVIKACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1408 DAKILCIDEATASVDQKT-DQLLQQTICKRFA-NKTVLTIAHRLNTILNSDRVLVLQAGR 1465
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1271-1479 |
1.44e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 138.31 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL 1350
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 dpqGLHEDRALWQALEQ-CHLSEVAVAM----GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1425
Cdd:PRK10789 410 ---ALGRPDATQQEIEHvARLASVHDDIlrlpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1426 DQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK10789 487 EHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
622-807 |
2.06e-33 |
|
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: 128.86 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKTF 691
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpADLRRNIGYVPQDVTLFYGTLRDNITLGAPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 692 -DAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcI 770
Cdd:cd03245 105 aDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER-L 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 24850123 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03245 184 RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1256-1465 |
4.20e-33 |
|
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: 125.82 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1256 EFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 1335
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1336 PQepflfsgtirenldpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCID 1415
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1416 EATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGR 1465
Cdd:cd00267 106 EPTSGLDPASRERLLELL-RELAeeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1255-1479 |
1.47e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 134.26 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQLELAELRSQ 1331
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1332 LAVIPQEPF--LFSGT----IRENLDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARAL 1405
Cdd:COG1123 85 IGMVFQDPMtqLNPVTvgdqIAEALENLGLSRAEARARVLE-------LLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1406 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1255-1475 |
2.55e-32 |
|
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: 126.14 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGlpNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE-----PNAGRVLLD--NVDTSQLELAE 1327
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1328 LRSQLAVIPQEPFLFSGTIRENLD----PQGLHEDRALWQaleqchLSEVAVAMGGLDGELGER--GQNLSLGQRQLLCL 1401
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELDE------RVEEALRKAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1402 ARALLTDAKILCIDEATASVD----QKTDQLLQQtICKRFankTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDpistAKIEELIAE-LKKEY---TIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1255-1480 |
3.52e-32 |
|
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: 126.46 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 1332
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFL-----FS--GTIRENLDPQGL-HEDRALWQALEQChlsevavamgGLDGELGER--GQnLSLGQRQLLCLA 1402
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRIHGLpDREERIAELLEQV----------GLPPSFLDRypHQ-LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1403 RALLTDAKILCIDEATASVD---Q-KTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRN 1477
Cdd:COG1124 151 RALILEPELLLLDEPTSALDvsvQaEILNLLKDL--REERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
...
gi 24850123 1478 QPH 1480
Cdd:COG1124 229 GPK 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1255-1479 |
4.45e-32 |
|
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: 125.77 E-value: 4.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVY--RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLfLVLFRLLE-PNAGRVLLDNVDTSQL---ELAEL 1328
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1329 RSQLAVIPQEPFLFSG-TIREN----LDPQGLHEDRALWQALEQCHLSevavamgGLDGELGERGQNLSLGQRQLLCLAR 1403
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVLELLELV-------GLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1404 ALLTDAKILCIDEATASVDQKTDQ----LLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQsilaLLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
.
gi 24850123 1479 P 1479
Cdd:cd03258 232 P 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
465-798 |
1.34e-31 |
|
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: 131.64 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 465 ELLSGIRVIKFFRWEQALGDRVKAC----RTKELGRLRvIKYLDAACVYLWAALPVVIcITIFITYVLMGHQLTATKVFT 540
Cdd:TIGR02857 188 DRLRGLPTLKLFGRAKAQAAAIRRSseeyRERTMRVLR-IAFLSSAVLELFATLSVAL-VAVYIGFRLLAGDLDLATGLF 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 541 ALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLDLPSysPEAYYSPDPPAEPSTALELHEALFSWDPIGASQKTFis 620
Cdd:TIGR02857 266 VLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAP--RPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPV-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKT 690
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadaDSWRDQIAWVPQHPFLFAGTIAENIRLARP 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 F-DAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRc 769
Cdd:TIGR02857 422 DaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA- 500
|
330 340
....*....|....*....|....*....
gi 24850123 770 ILGVLSHTTRLLCTHRTEYLERADVVLLM 798
Cdd:TIGR02857 501 LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1255-1468 |
3.00e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.84 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 1329
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQ-LAVIPQEPFLFSG-TIREN----LDPQGLHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQLLCLAR 1403
Cdd:COG1136 85 RRhIGFVFQFFNLLPElTALENvalpLLLAGVSRKERRERAREL--LERV-----GLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1404 ALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1255-1466 |
9.30e-31 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 121.44 E-value: 9.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 1329
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 -SQLAVIPQE----PFLfsgTIRENL--------DPQGLHEDRALwQALEQChlsevavamgGLDGELGERGQNLSLGQR 1396
Cdd:cd03255 81 rRHIGFVFQSfnllPDL---TALENVelplllagVPKKERRERAE-ELLERV----------GLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1397 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 1466
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
291-572 |
2.64e-30 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 122.28 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 291 LLKMVGTMLGFSGPLLL-SLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKAL 369
Cdd:cd18592 4 LLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 370 KL-GPSRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQL----AITLYLL--YQQVGMAFLAGLVLAlllvpvnKVIA 442
Cdd:cd18592 84 RLrSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLilgiVYSTYLLgpWALLGMLVFLLFYPL-------QAFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 443 TRIMAS-NQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICIT 521
Cdd:cd18592 157 AKLTGKfRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 522 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18592 237 TFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1255-1466 |
3.80e-30 |
|
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: 117.88 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAV 1334
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSG-TIRENLDpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILC 1413
Cdd:cd03230 78 LPEEPSLYENlTVRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1414 IDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:cd03230 119 LDEPTSGLDPESRREFWELL-RELKkeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1272-1475 |
1.02e-29 |
|
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: 119.38 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFL-FSGTIRE-- 1348
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRElv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 --------NLDPQGLHEDRAL-WQALEQCHLSEvavamggldgeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEAT 1418
Cdd:COG1120 97 algryphlGLFGRPSAEDREAvEEALERTGLEH-----------LADRPvDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1419 ASVD---QKtdQLLQqtICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:COG1120 166 SHLDlahQL--EVLE--LLRRLArerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1271-1480 |
3.06e-29 |
|
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: 117.54 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAEL---RS-QlavIPQepfLFS 1343
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpphEIARLgigRTfQ---IPR---LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 G-TIRENLD-PQGLHEDRALWQALEQCHLSEV------AVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 1415
Cdd:cd03219 89 ElTVLENVMvAAQARTGSGLLLARARREEREAreraeeLLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1416 EATASV-DQKTDQLLqQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQPH 1480
Cdd:cd03219 169 EPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1255-1480 |
4.80e-29 |
|
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: 117.02 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSG-TIREN--LDPQGLHEDRALWQ--ALEqchlsevAVAMGGLD-GELGER-GQNLSLGQRQLLCLARALLT 1407
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKWPKEKIRerADE-------LLALVGLDpAEFADRyPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1408 DAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPSALRNQPH 1480
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFkrLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1255-1470 |
6.05e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.31 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ 1331
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1332 LAVIPQE-PFLFSGTIREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALL 1406
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENvalpLRVTGKSRKEIRRRVRE-------VLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1407 TDAKILCIDEATASVDQKT-DQLLQ--QTICKRfaNKTVLtIA-HRLNtILNS--DRVLVLQAGRVVELD 1470
Cdd:COG2884 154 NRPELLLADEPTGNLDPETsWEIMEllEEINRR--GTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVRDE 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1262-1467 |
1.42e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 113.68 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1262 LVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQepfl 1341
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 fsgtirenldpqglhedralwqALEQCHLSEvavamggldgeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:cd03214 81 ----------------------ALELLGLAH-----------LADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1421 VD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:cd03214 128 LDiahqIELLELLRRL--ARERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1250-1473 |
1.66e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.63 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1250 LTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 1329
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQEP-FLFSGTIRENLDPQGLhEDRALWQALEQCHLSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTD 1408
Cdd:PRK13632 83 KKIGIIFQNPdNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKV-GMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1409 AKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPS 1473
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPK 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1255-1468 |
1.86e-28 |
|
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: 114.88 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVdtsqlELAELRSQL 1332
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFS-GTIREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLT 1407
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvalgLELQGVPKAEARERAEE-------LLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1408 DAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLN-TILNSDRVLVLQA--GRVVE 1468
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
622-802 |
5.56e-28 |
|
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: 111.71 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILfgkt 690
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdptsgeilidgVDLRDL-DLESLRKNIAYVPQDPFLFSGTIRENIL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 fdaqlyrevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCI 770
Cdd:cd03228 98 -------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPE-TEALILEAL 139
|
170 180 190
....*....|....*....|....*....|..
gi 24850123 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQ 802
Cdd:cd03228 140 RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1250-1461 |
6.96e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 123.22 E-value: 6.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1250 LTQGSVEFQDVVLVY--RPGLPNALDgVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE-------------------- 1307
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1308 ----------------------------------PNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLdpQ 1353
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI--K 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1354 GLHEDRALWQALEQCHLSEVAVAMGGL----DGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLL 1429
Cdd:PTZ00265 1318 FGKEDATREDVKRACKFAAIDEFIESLpnkyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260 270
....*....|....*....|....*....|....
gi 24850123 1430 QQTIC--KRFANKTVLTIAHRLNTILNSDRVLVL 1461
Cdd:PTZ00265 1398 EKTIVdiKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1272-1480 |
1.79e-27 |
|
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: 112.21 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFLFSG-TIR 1347
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLD-PqgLHEDRALWQAlEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD 1426
Cdd:cd03261 96 ENVAfP--LREHTRLSEE-EIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1427 QLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQPH 1480
Cdd:cd03261 173 GVIDDLIrsLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
621-813 |
3.29e-27 |
|
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: 111.55 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITgelhRLCGW--------------VAVSELSKGFGLATQEPWIQCATIRDNIL 686
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLM----RFYDPqkgqilidgidirdISRKSLRSMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FGK-TFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANhL 765
Cdd:cd03254 99 LGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK-L 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24850123 766 LHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03254 178 IQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1255-1480 |
3.53e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.72 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRpGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDtsqleLAELRSQLAV 1334
Cdd:COG1121 7 IELENLTVSYG-GRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQepflfsgtiRENLDPQ-----------GL-----------HEDRAL-WQALEQCHLSEVAvamgglDGELGErgqnL 1391
Cdd:COG1121 80 VPQ---------RAEVDWDfpitvrdvvlmGRygrrglfrrpsRADREAvDEALERVGLEDLA------DRPIGE----L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1392 SLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTIL-NSDRVLVLqAGRVVEL 1469
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAH 219
|
250
....*....|.
gi 24850123 1470 DSPSALRNQPH 1480
Cdd:COG1121 220 GPPEEVLTPEN 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1271-1468 |
4.16e-27 |
|
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: 113.61 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQL---ELAELR-SQLAVIPQEPF--- 1340
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLsekELRKIRgREIQMIFQDPMtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1341 --LFsgTIRENL-DPQGLH--------EDRALwQALEQCHLSEVAvamggldgelgERGQN----LSLGQRQLLCLARAL 1405
Cdd:COG0444 100 npVM--TVGDQIaEPLRIHgglskaeaRERAI-ELLERVGLPDPE-----------RRLDRypheLSGGMRQRVMIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1406 LTDAKILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:COG0444 166 ALEPKLLIADEPTTALDvtiQA--QILNllKDLQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
622-813 |
5.05e-27 |
|
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: 111.09 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGEL----HRLCGwVAVSELSKGFGLATQEPWIQCATIRDNILFGKt 690
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEIlldgVDIRD-LNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 FDAQLyREVLEAC--ALNDDLSI-LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD---VANH 764
Cdd:cd03249 102 PDATD-EEVEEAAkkANIHDFIMsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24850123 765 LLHRCILGvlshTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03249 181 ALDRAMKG----RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1256-1474 |
9.04e-27 |
|
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: 110.74 E-value: 9.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1256 EFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAEL---RSQL 1332
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFL----------------FSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAmggldgelgeRGQNLSLGQR 1396
Cdd:cd03256 81 GMIFQQFNLierlsvlenvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQ----------RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1397 QLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTIL-NSDRVLVLQAGRVVeLDS 1471
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRqvmdLLKR-INREE-GITVIVSLHQVDLAReYADRIVGLKDGRIV-FDG 227
|
...
gi 24850123 1472 PSA 1474
Cdd:cd03256 228 PPA 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
503-785 |
1.26e-26 |
|
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: 116.31 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 503 LDAACVYLWAALPVVICITIFITYVlMGHQLT----ATKVFTALALVRmlilPLNNFPWVINGLLESKVSLDRIQRFLDL 578
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAV-ADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 579 PSYSPEAYYSPDPPAEPSTA-LELHEALFSWDPiGASQKTFIShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGW 657
Cdd:TIGR02868 314 AGPVAEGSAPAAGAVGLGKPtLELRDLSAGYPG-APPVLDGVS-LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 658 VAV----------SELSKGFGLATQEPWIQCATIRDNILFGK--TFDAQLYReVLEACALNDDLSILPAGDQTEVGEKGV 725
Cdd:TIGR02868 392 VTLdgvpvssldqDEVRRRVSVCAQDAHLFDTTVRENLRLARpdATDEELWA-ALERVGLADWLRALPDGLDTVLGEGGA 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 726 TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSHTTRLLCTHR 785
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHH 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
621-807 |
1.57e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 116.48 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITG-------------ELHRL--------CGWVAvselskgfglatQEPWIQCA 679
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELdpeswrkhLSWVG------------QNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 680 TIRDNILFGKTF--DAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK11174 438 TLRDNVLLGNPDasDEQLQ-QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 758 DADVANHLLhRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:PRK11174 517 DAHSEQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
622-813 |
1.74e-26 |
|
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: 109.63 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAIT-------GEL----HRLCGwVAVSELSKGFGLATQEPWIQCATIRDNILFGKt 690
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsGRIlidgHDVRD-YTLASLRRQIGLVSQDVFLFNDTVAENIAYGR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 FDAQL--YREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaDVANHLLHR 768
Cdd:cd03251 101 PGATReeVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD-TESERLVQA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24850123 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03251 180 ALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1255-1468 |
3.14e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 111.71 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLfLVLFRLLE-PNAGRVLLDNVDTSQL---ELAEL 1328
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTL-IRCINLLErPTSGSVLVDGVDLTALserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1329 RSQLAVIPQEPFLFSG-TIRENLdpqglhedrALwqALEQCHLSEVAVA--------MGGLDGELGERGQNLSLGQRQLL 1399
Cdd:COG1135 81 RRKIGMIFQHFNLLSSrTVAENV---------AL--PLEIAGVPKAEIRkrvaelleLVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1400 CLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRsildLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1255-1468 |
4.30e-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: 104.91 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSqLAV 1334
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-PERRN-IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSG-TIREN----LDPQGLHEDralwQALEQCHLsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 1409
Cdd:cd03259 77 VFQDYALFPHlTVAENiafgLKLRGVPKA----EIRARVRE---LLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1410 KILCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1256-1467 |
5.41e-25 |
|
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: 104.54 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1256 EFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqLELAELRSQLAVI 1335
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1336 PQepflfsgtiRENLDPQ-----------GLHEDRALWQAL--EQCHLSEVAVAMGGLdGELGER--GQnLSLGQRQLLC 1400
Cdd:cd03235 74 PQ---------RRSIDRDfpisvrdvvlmGLYGHKGLFRRLskADKAKVDEALERVGL-SELADRqiGE-LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1401 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNS-DRVLVLqAGRVV 1467
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLL-NRTVV 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1219-1464 |
9.48e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.05 E-value: 9.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1219 SVERLEEYScDVPQEPHSQPLQSPHQQRIswlTQGSVEFQDVVLVyrpgLPNA---LDGVTFRVEPGEKLGIVGRTGSGK 1295
Cdd:COG4178 331 TVDRLAGFE-EALEAADALPEAASRIETS---EDGALALEDLTLR----TPDGrplLEDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1296 SSLFLVLFRLLEPNAGRVLLDNVDtsqlelaelrsQLAVIPQEPFLFSGTIRENL---DPQGLHEDRALWQALEQCHLSE 1372
Cdd:COG4178 403 STLLRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1373 VAvamGGLDGELgERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTI 1452
Cdd:COG4178 472 LA---ERLDEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLA 547
|
250
....*....|..
gi 24850123 1453 LNSDRVLVLQAG 1464
Cdd:COG4178 548 AFHDRVLELTGD 559
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1271-1477 |
9.80e-25 |
|
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: 104.05 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQEPFLFSG-TIRE 1348
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NLdpqglhedRALWQALEQCHLSEVAVAMGGLDGELGER----GQNLSLGQRQLLCLARALLTDAKILCIDEATAS---- 1420
Cdd:cd03224 95 NL--------LLGAYARRRAKRKARLERVYELFPRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGlapk 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1421 -VDQKTDQLlqQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRN 1477
Cdd:cd03224 167 iVEEIFEAI--RELRDE--GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1255-1471 |
4.93e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 105.27 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLP--NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 1329
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQEpF--LFSGTIRENLdpqglhedrALwqALEQCHLSEVAV--------AMGGLdGELGER-GQNLSLGQRQL 1398
Cdd:PRK11153 82 RQIGMIFQH-FnlLSSRTVFDNV---------AL--PLELAGTPKAEIkarvtellELVGL-SDKADRyPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1399 LCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 1471
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRsileLLKD-INREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1271-1479 |
5.38e-24 |
|
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: 103.49 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ-LAVIPQEPFLFSG-T 1345
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPHrT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASV 1421
Cdd:cd03294 119 VLENvafgLEVQGVPRAEREERAAE-------ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1422 D-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:cd03294 192 DplirrEMQDELLR---LQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
622-813 |
6.31e-24 |
|
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: 102.18 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITG----ELHRLC------GWVAVSELSKGFGLATQEPWIQCATIRDNILFGKTf 691
Cdd:cd03252 23 LRIKPGEVVGIVGRSGSGKSTLTKLIQRfyvpENGRVLvdghdlALADPAWLRRQVGVVLQENVLFNRSIRDNIALADP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 692 dAQLYREVLEACAL---NDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHR 768
Cdd:cd03252 102 -GMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHAIMR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24850123 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03252 180 NMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1255-1465 |
7.41e-24 |
|
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: 99.95 E-value: 7.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD--NVDTSQLELAELRSQL 1332
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSG-TIRENldpqglhedralwqaleqchlsevaVAMGgldgelgergqnLSLGQRQLLCLARALLTDAKI 1411
Cdd:cd03229 79 GMVFQDFALFPHlTVLEN-------------------------IALG------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1412 LCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGR 1465
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1271-1467 |
9.37e-24 |
|
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: 101.29 E-value: 9.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAVIPQEPFLFSG-TIREN 1349
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 LDP-QGLH--EDRALWQALEqchlsEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD 1426
Cdd:cd03266 99 LEYfAGLYglKGDELTARLE-----ELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24850123 1427 QLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:cd03266 173 RALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
622-809 |
1.51e-23 |
|
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: 100.65 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAitgeLHRLcgwvavSELSKG--------------------FGLATQEPWIQCATI 681
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLA----LFRL------VELSSGsilidgvdiskiglhdlrsrISIIPQDPVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 682 RDNI-LFGKTFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:cd03244 95 RSNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24850123 761 VAnHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPP 809
Cdd:cd03244 174 TD-ALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1271-1467 |
1.78e-23 |
|
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: 98.65 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQepflfsgtiren 1349
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 ldpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQL 1428
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24850123 1429 LQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:cd03216 122 FK--VIRRLRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1271-1468 |
2.06e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 106.31 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFlfsG--- 1344
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDPF---Gsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 -------TIRENLDPQGLHEDRA-----LWQALEqchlsEVavamgGLDGELGERGQN-LSLGQRQLLCLARALLTDAKI 1411
Cdd:COG4172 377 prmtvgqIIAEGLRVHGPGLSAAerrarVAEALE-----EV-----GLDPAARHRYPHeFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1412 LCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTI--LnSDRVLVLQAGRVVE 1468
Cdd:COG4172 447 LVLDEPTSALDvsvQA--QILDllRDLQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1271-1479 |
2.80e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.89 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPF--L---- 1341
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPYasLnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 -FSGTIRENLDPQGLH-----EDRALwQALEQChlsevavamgGLDGELGER-GQNLSLGQRQLLCLARALLTDAKILCI 1414
Cdd:COG4608 113 tVGDIIAEPLRIHGLAskaerRERVA-ELLELV----------GLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1415 DEATASVD---QKtdQ---LLQ--QticKRFaNKTVLTIAHRLNT---IlnSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:COG4608 182 DEPVSALDvsiQA--QvlnLLEdlQ---DEL-GLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1272-1433 |
3.15e-23 |
|
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: 99.09 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAVIPQEPFLFSG-TIRENL 1350
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 D-----PQGLHEDRALWQALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1425
Cdd:COG4133 97 RfwaalYGLRADREAIDEALEAV----------GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
....*...
gi 24850123 1426 DQLLQQTI 1433
Cdd:COG4133 167 VALLAELI 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1271-1468 |
3.28e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQEPFLFSG-TIRE 1348
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NL----DPQ--GLHEDRALWQALEQcHLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 1422
Cdd:COG1129 99 NIflgrEPRrgGLIDWRAMRRRARE-LLARL-----GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 1423 QK-TDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:COG1129 173 EReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1266-1464 |
4.86e-23 |
|
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: 98.94 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1266 PGLPNaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQ----LAVIPQEPFL 1341
Cdd:cd03290 12 SGLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 FSGTIRENLDPQGLHEDRALWQALEQCHLS-EVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24850123 1421 VD-QKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAG 1464
Cdd:cd03290 171 LDiHLSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1272-1473 |
1.64e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFL-FSGTIRE-- 1348
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEvv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 --NLDPQGL---HEDRALWQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALL------TDAKILCIDEA 1417
Cdd:PRK13548 98 amGRAPHGLsraEDDALVAAALAQVDLAHLA----------GRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1418 TASVDqktdqLLQQ----TICKRFANK---TVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPS 1473
Cdd:PRK13548 168 TSALD-----LAHQhhvlRLARQLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1254-1475 |
1.99e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD----NVDTSQLELA 1326
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhiTPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1327 ELRSQLAVIPQ--EPFLFSGTIRENLD--PQ--GLHEDRALWQALEQchLSEVavamgGLDGELGERGQ-NLSLGQRQLL 1399
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEfgPKnfGFSEDEAKEKALKW--LKKV-----GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1400 CLARALLTDAKILCIDEATASVDQKT-DQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1254-1473 |
4.94e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTS--QLELAEL 1328
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1329 RSQLAVIPQEP--FLFSGTIRENLD--PQ--GLHEDRALWQALEqchlsevAVAMGGLDGE-LGERGQ-NLSLGQRQLLC 1400
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAfgPInlGLSEEEIENRVKR-------AMNIVGLDYEdYKDKSPfELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1401 LARALLTDAKILCIDEATASVDQKT-DQLLQQ--TICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPS 1473
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGrDEILNKikELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1271-1480 |
1.20e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 96.26 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPNA---GRVLLDNVD--TSQLELAELRSQLAVIPQEPFLFS 1343
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 GTIREN----LDPQGLHEDRAL----WQALEQCHL-SEVAvamgglDgELGERGQNLSLGQRQLLCLARALLTDAKILCI 1414
Cdd:COG1117 106 KSIYDNvaygLRLHGIKSKSELdeivEESLRKAALwDEVK------D-RLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1415 DEATASVD----QKTDQLLQQtICKRFankTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSALRNQPH 1480
Cdd:COG1117 179 DEPTSALDpistAKIEELILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQIFTNPK 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
599-807 |
1.58e-21 |
|
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: 93.53 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 599 LELHEALFSWDPigaSQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE---------LSKGF 667
Cdd:cd03247 1 LSINNVSFSYPE---QEQQVLKNlsLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekaLSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 668 GLATQEPWIQCATIRDNIlfgktfdaqlyrevleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKAL 747
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 748 YLLDDPLAAVDADVANHLLhRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03247 120 VLLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1255-1479 |
1.78e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL-ELAELRSQLA 1333
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1334 VIPQEP-FLFSG-TIRENL--DPQGLhedraLWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 1409
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLafGPENL-----CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1410 KILCIDEATASVDQKTDQLLQQTIcKRF--ANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERI-KKLheKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1255-1473 |
2.38e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.85 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEP-FLFSGTIREN-----LDPQGLHED---RALWQALEQCHLSEVavamggLDGElgerGQNLSLGQRQLLCLARAL 1405
Cdd:PRK13635 86 VFQNPdNQFVGATVQDdvafgLENIGVPREemvERVDQALRQVGMEDF------LNRE----PHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1406 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPS 1473
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
621-808 |
3.71e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.79 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGE-------LHRLcgwvAVSELSKGFGLATQEPWIQCATIRDNIL 686
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvsEGDirfhdipLTKL----QLDSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FGKTfDA--QLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:PRK10789 411 LGRP-DAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQ 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24850123 765 LLHRcilgvLS----HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGP 808
Cdd:PRK10789 490 ILHN-----LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
541-822 |
5.42e-21 |
|
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: 99.05 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 541 ALALVRMLIlplNNfpWviNGLLESKVSLDRIQRFLDlpSYSPEAYYSPDPpaEPSTALELhEALfSWDPIGASQKTF-- 618
Cdd:COG4618 284 ALAPIEQAI---GG--W--KQFVSARQAYRRLNELLA--AVPAEPERMPLP--RPKGRLSV-ENL-TVVPPGSKRPILrg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 619 IShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVS-----ELSKGFGLATQEPWIQCATIRDNI-LF 687
Cdd:COG4618 351 VS-FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgaDLSqwdreELGRHIGYLPQDVELFDGTIAENIaRF 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 GKTfDAQlyrEVLEACALND--DLsI--LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:COG4618 430 GDA-DPE---KVVAAAKLAGvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 764 HLLhRCILGVLSH-TTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAVPTA 822
Cdd:COG4618 505 ALA-AAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
624-813 |
5.49e-21 |
|
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: 93.45 E-value: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 624 VKKGMLVGIVGKVGCGKSSLL-------------AAITGELHRLcgwVAVSELSKGFGLATQEPWIQCATIRDNILFGK- 689
Cdd:cd03253 24 IPAGKKVAIVGPSGSGKSTILrllfrfydvssgsILIDGQDIRE---VTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 -TFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHR 768
Cdd:cd03253 101 dATDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT-HTEREIQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24850123 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03253 179 ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
465-812 |
6.08e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 465 ELLSGIRVIKFFRWEQALGDR--VKACRTKELGRLRVIKYLdaacVYLWAAlpVVICITIFITYVLMGHQLTATKVFTAL 542
Cdd:TIGR00958 345 EALSGMRTVRSFAAEEGEASRfkEALEETLQLNKRKALAYA----GYLWTT--SVLGMLIQVLVLYYGGQLVLTGKVSSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 543 ALVRMLILP------LNNFPWVINGLLESKVSLDRIQRFLDL-PSYSPEAYYSPDPPaepSTALELHEALFSWdPIGASQ 615
Cdd:TIGR00958 419 NLVSFLLYQeqlgeaVRVLSYVYSGMMQAVGASEKVFEYLDRkPNIPLTGTLAPLNL---EGLIEFQDVSFSY-PNRPDV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 616 KTFIS-HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSE-----LSKGFGLATQEPWIQCATIR 682
Cdd:TIGR00958 495 PVLKGlTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQV--LLDGVPLVQydhhyLHRQVALVGQEPVLFSGSVR 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 683 DNILFGKTF--DAQLYREVLEACAlNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:TIGR00958 573 ENIAYGLTDtpDEEIMAAAKAANA-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 761 VaNHLLH--RCILGvlshTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:TIGR00958 652 C-EQLLQesRSRAS----RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1272-1466 |
6.26e-21 |
|
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: 93.38 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElRSQLAVI--PQEPFLFSG-TIRE 1348
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NLDP--QGLHEDRALWQA-----LEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASV 1421
Cdd:cd03218 95 NILAvlEIRGLSKKEREEkleelLEEFHITHLR----------KSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24850123 1422 DQKTDQLLQQTIcKRFANKT--VLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:cd03218 165 DPIAVQDIQKII-KILKDRGigVLITDHNVRETLSiTDRAYIIYEGKV 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1255-1466 |
6.88e-21 |
|
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: 92.86 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ 1331
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1332 LAVIPQEPFLFSG-TIREN--LDPQGLHEDRALWQ-----ALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLAR 1403
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENvaFALEVTGVPPREIRkrvpaALELV----------GLSHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1404 ALLTDAKILCIDEATASVDQKTD----QLLQQtICKRFANKTVLTIAHRL-NTIlnSDRVLVLQAGRV 1466
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKK-INKAGTTVVVATHAKELvDTT--RHRVIALERGKL 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1254-1478 |
1.40e-20 |
|
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: 93.77 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYRPGLPNaldgVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlelaELRSQLA 1333
Cdd:cd03291 39 NLFFSNLCLVGAPVLKN----INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1334 VIPQEPFLFSGTIRENLdPQGLHEDRALWQA-LEQCHLSEVAVAMGGLDGE-LGERGQNLSLGQRQLLCLARALLTDAKI 1411
Cdd:cd03291 102 FSSQFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTvLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1412 LCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:cd03291 181 YLLDSPFGYLDVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1270-1474 |
2.89e-20 |
|
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: 91.34 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1270 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLA--VIPQEPFLFSG 1344
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARHVgfVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 TIREN----LDPQGLHEDRALWQALeqchLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:COG4181 106 TALENvmlpLELAGRRDARARARAL----LERV-----GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1421 VDQKT-----DQLLQQTickRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSA 1474
Cdd:COG4181 177 LDAATgeqiiDLLFELN---RERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1272-1475 |
3.59e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEP-FLFSGTIREN- 1349
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGATVEDd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 ----LDPQGL-HED--RALWQALEqchlsevAVAMGGLDGELGERgqnLSLGQRQLLCLARALLTDAKILCIDEATASVD 1422
Cdd:PRK13650 103 vafgLENKGIpHEEmkERVNEALE-------LVGMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1423 QKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK13650 173 PEGRLELIKTIkgIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
622-803 |
5.89e-20 |
|
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: 90.22 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLlAAITGELHRLC-GWVAVSE----------LSKGFGLATQEPWIQCATIRDNILFG-K 689
Cdd:cd03248 35 FTLHPGEVTALVGPSGSGKSTV-VALLENFYQPQgGQVLLDGkpisqyehkyLHSKVSLVGQEPVLFARSLQDNIAYGlQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 TFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRC 769
Cdd:cd03248 114 SCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQA 192
|
170 180 190
....*....|....*....|....*....|....
gi 24850123 770 ILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03248 193 LYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1271-1467 |
8.89e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD----NVDTSQlelAELRSQLAVIPQEPFLFSG-T 1345
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvRIRSPR---DAIALGIGMVHQHFMLVPNlT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IRENL-----DPQGLHEDRAlwQALEQchLSEVAVAMGgLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAs 1420
Cdd:COG3845 97 VAENIvlglePTKGGRLDRK--AARAR--IRELSERYG-LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1421 V--DQKTDQLLQqtICKRFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV 1467
Cdd:COG3845 171 VltPQEADELFE--ILRRLAAegKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1272-1479 |
1.81e-19 |
|
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: 89.32 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSqlELAELRSQLAVIPQEPFLFSG-TIRENL 1350
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 DpQGL---HEDRAlwQALEQCHlsEVAvAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 1427
Cdd:cd03299 93 A-YGLkkrKVDKK--EIERKVL--EIA-EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1428 LLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:cd03299 167 KLREELKKirKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1265-1479 |
2.56e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.02 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1265 RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRS----QLAVIPQEPF 1340
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1341 LFSGTIRenLDPQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:PRK10070 117 LMPHMTV--LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1421 VDQKTDQLLQQTICKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1275-1461 |
4.51e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 94.33 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1275 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL--- 1350
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 ----------------------------------------------DPQGLHEDRALWQALEQCHLSEVAVAM------- 1377
Cdd:PTZ00265 484 lyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDSEVVDVSKKVlihdfvs 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1378 ---GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTI 1452
Cdd:PTZ00265 564 alpDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTI 643
|
....*....
gi 24850123 1453 LNSDRVLVL 1461
Cdd:PTZ00265 644 RYANTIFVL 652
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
568-813 |
6.55e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 93.89 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 568 SLDRIQRFLDLPSYSPEAYYSPDPPAepstalelhealfSWdPIGASQKTFISHLQVKKGM---------------LVGI 632
Cdd:PLN03232 1202 SVERVGNYIDLPSEATAIIENNRPVS-------------GW-PSRGSIKFEDVHLRYRPGLppvlhglsffvspseKVGV 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 633 VGKVGCGKSSLLAAI--TGELHRlcGWVAV----------SELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYrEV 699
Cdd:PLN03232 1268 VGRTGAGKSSMLNALfrIVELEK--GRIMIddcdvakfglTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLW-EA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 700 LEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVaNHLLHRCILGVLSHTTR 779
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTM 1423
|
250 260 270
....*....|....*....|....*....|....
gi 24850123 780 LLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PLN03232 1424 LVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
622-807 |
7.01e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 86.80 E-value: 7.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHRLCG---------WVAVSELSKGFGLATQE----PWIqcaTIRDNILFG 688
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRLIAG-LERPDSgeilidgrdVTGVPPERRNIGMVFQDyalfPHL---TVAENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ----KTFDAQLYREVLEACALNDDLSILpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:cd03259 97 lklrGVPKAEIRARVRELLELVGLEGLL--------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24850123 765 LLHRcILGVLS--HTTRLLCTH-RTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03259 169 LREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
622-816 |
7.58e-19 |
|
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: 86.76 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWiqcATIRDNILFGKTF 691
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDG-EPVTGPGPDRGYVFQQdallPW---LTVLDNVALGLEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 692 ----DAQLYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV 761
Cdd:cd03293 101 qgvpKAEARERAEELLEL--------------VGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 762 ANHlLHRCILGVLSHT--TRLLCTHRTE---YLerADVVLLMeagqlvrTGPPSEILPLV 816
Cdd:cd03293 167 REQ-LQEELLDIWRETgkTVLLVTHDIDeavFL--ADRVVVL-------SARPGRIVAEV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
517-807 |
7.77e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 517 VICITIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVsldRIQRFLDLPSYSPEAYYSPD--PPAE 594
Cdd:PRK13657 254 MLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAP---KLEEFFEVEDAVPDVRDPPGaiDLGR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 595 PSTALELHEALFSWDpiGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAitgeLHRL--------------CGWVAV 660
Cdd:PRK13657 331 VKGAVEFDDVSFSYD--NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL----LQRVfdpqsgrilidgtdIRTVTR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 661 SELSKGFGLATQEPWIQCATIRDNILFGKT--FDAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALA 738
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEM-RAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 739 RAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:PRK13657 484 RALLKDPPILILDEATSALDV-ETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1255-1467 |
9.81e-19 |
|
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: 86.18 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPglPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtSQLElAELRSQLAV 1334
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLD-IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSG-TIRENL----DPQGLHEDRALWQA---LEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALL 1406
Cdd:cd03269 75 LPEERGLYPKmKVIDQLvylaQLKGLKKEEARRRIdewLERLELSEYA----------NKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1407 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
622-813 |
1.23e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAIT-------GEL----HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILFGK- 689
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqGEIllngQPIADY-SEAALRQAISVVSQRVHLFSATLRDNLLLAAp 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 -TFDAQLyREVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhR 768
Cdd:PRK11160 440 nASDEAL-IEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-E 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24850123 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK11160 517 LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1254-1475 |
1.44e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLvyrpglpnaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLA 1333
Cdd:PRK09536 10 SVEFGDTTV---------LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1334 VIPQE---PFLFSG-TI--------RENLDPQGLHEDRALWQALEQCHLSEVAvamgglDGELGErgqnLSLGQRQLLCL 1401
Cdd:PRK09536 81 SVPQDtslSFEFDVrQVvemgrtphRSRFDTWTETDRAAVERAMERTGVAQFA------DRPVTS----LSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1402 ARALLTDAKILCIDEATASVDqKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD-INHQVRTLELVRRLVDdgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADV 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
621-755 |
1.71e-18 |
|
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: 83.85 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV----------AVSELSKGFGLATQEPWIQCA-TIRDNILFG- 688
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddERKSLRKEIGYVFQDPQLFPRlTVRENLRLGl 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 689 -------KTFDAQLYrEVLEACALNDDLSilpagdqTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:pfam00005 85 llkglskREKDARAE-EALEKLGLGDLAD-------RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
622-812 |
1.94e-18 |
|
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: 86.24 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQE-PWIQCATIRDNILFG---- 688
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedATDVPvqeRNVGFVFQHyALFRHMTVFDNVAFGlrvk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 -------KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV 761
Cdd:cd03296 103 prserppEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 762 ANHL------LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03296 172 RKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1255-1448 |
2.90e-18 |
|
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: 83.74 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlELAElRSQLAV 1334
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPE-GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSGTIRENLdpqglhedRALWQaleqchlsevavamggldgelgergQNLSLGQRQLLCLARALLTDAKILCI 1414
Cdd:cd03223 69 LPQRPYLPLGTLREQL--------IYPWD-------------------------DVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 24850123 1415 DEATASVDQKTDQLLQQTICKRFAnkTVLTIAHR 1448
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1271-1467 |
2.92e-18 |
|
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: 84.85 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFR-----------VEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLAVIPQEP 1339
Cdd:cd03298 2 RLDKIRFSygeqpmhfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1340 FLFSG-TIRENLdpqGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEAT 1418
Cdd:cd03298 80 NLFAHlTVEQNV---GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1419 ASVDQKTDQLLQQ---TICKRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:cd03298 157 AALDPALRAEMLDlvlDLHAETKM-TVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
622-801 |
3.97e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.91 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELSKGFGLATQE----PWiqcATIRDNILFG--- 688
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKptsgevLVDGKPVTGPGPDRGVVFQEpallPW---LTVLDNVALGlel 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ----KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:COG1116 108 rgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24850123 765 lLHRCILGVL--SHTTRLLCTHRTE---YLerADVVLLMEAG 801
Cdd:COG1116 177 -LQDELLRLWqeTGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1272-1470 |
7.15e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelRSQLAVIPQEPFLFSG-TIRENL 1350
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 DpQGLHEDRALWQALEQC-----HLSEVAVAMGGLDGELGERG--------------------------QNLSLGQRQLL 1399
Cdd:COG0488 83 L-DGDAELRALEAELEELeaklaEPDEDLERLAELQEEFEALGgweaearaeeilsglgfpeedldrpvSELSGGWRRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1400 CLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANkTVLTIAHrlntilnsDRVLvLQ--AGRVVELD 1470
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL-KNYPG-TVLVVSH--------DRYF-LDrvATRILELD 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1271-1422 |
9.54e-18 |
|
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: 83.73 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD--NVDTSQLELAELRSQLAVIPQEPFLFSG-TIR 1347
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglKLTDDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 EN--LDP---QGLHEDRALWQALEqcHLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 1422
Cdd:cd03262 95 ENitLAPikvKGMSKAEAEERALE--LLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1255-1472 |
1.04e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.80 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEP-FLFSGTIRENLDPQGL------HED--RALWQALEQCHLSEVAvamgglDGElgerGQNLSLGQRQLLCLARAL 1405
Cdd:PRK13648 88 VFQNPdNQFVGSIVKYDVAFGLenhavpYDEmhRRVSEALKQVDMLERA------DYE----PNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1406 LTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1472
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1251-1468 |
2.00e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1251 TQGSVEFQDVVLVYrPGLpNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTS-QLELAELR 1329
Cdd:PRK11288 1 SSPYLSFDGIGKTF-PGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQE----PFLfsgTIRENLD----PQG---LHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQL 1398
Cdd:PRK11288 79 AGVAIIYQElhlvPEM---TVAENLYlgqlPHKggiVNRRLLNYEAREQ--LEHL-----GVDIDPDTPLKYLSIGQRQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1399 LCLARALLTDAKILCIDEATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSAReIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1272-1467 |
2.11e-17 |
|
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: 81.83 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLF-RLLEPNA-GRVLLDNVdtsQLELAELRSQLAVIPQEPFLFSG-TIRE 1348
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGVsGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NLDpqglhedralwqaleqchlseVAVAMGGLDGelgergqnlslGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1428
Cdd:cd03213 102 TLM---------------------FAAKLRGLSG-----------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24850123 1429 LQQTIcKRFA--NKTVLTIAHRL-NTILNS-DRVLVLQAGRVV 1467
Cdd:cd03213 150 VMSLL-RRLAdtGRTIICSIHQPsSEIFELfDKLLLLSQGRVI 191
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
622-803 |
2.81e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 82.17 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSELSKGFGLATQEP-WIQcATIRDNILF--- 687
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALadldpptSGEIYldgKPLSAMPPPEWRRQVAYVPQEPaLWG-GTVRDNLPFpfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 --GKTFDAQLYREVLEACALNDDlsILpagdQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHL 765
Cdd:COG4619 100 lrERKFDRERALELLERLGLPPD--IL----DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT-RR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24850123 766 LHRCILGVLSH--TTRLLCTHRTEYLER-ADVVLLMEAGQL 803
Cdd:COG4619 169 VEELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
621-812 |
3.12e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 82.61 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLL------------AAITGELH----RLCGW-VAVSELSKGFGLATQEPWIQCATIRD 683
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLrllnrlndlipgAPDEGEVLldgkDIYDLdVDVLELRRRVGMVFQKPNPFPGSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NILFG--------KTFDAQLYREVLEACALNDDLSilpagDQTevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:cd03260 100 NVAYGlrlhgiklKEELDERVEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 756 AVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03260 171 ALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1276-1475 |
3.29e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.50 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1276 TFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElRSqLAVIPQEPFLFSG-TIREN----L 1350
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQNiglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 DPqGLHEDRALWQALEQchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD----QKTD 1426
Cdd:COG3840 97 RP-GLKLTAEQRAQVEQ------ALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 1427 QLLQQtICKRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:COG3840 170 DLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1271-1467 |
3.82e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQL--AVIPQEPFLFSG-TIR 1347
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLdPQGLHEDRALW--QALEQCHLSEVAVAMG---GLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 1422
Cdd:PRK09700 99 ENL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLlrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24850123 1423 QK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:PRK09700 178 NKeVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
622-838 |
4.10e-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: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL---HRLCGWVAV----------SELSKGFGLATQEPWIQ--CATIRDNIL 686
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLdgrdllelseALRGRRIGMVFQDPMTQlnPVTVGDQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FG----KTFDAQLYREVLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:COG1123 107 EAlenlGLSRAEARARVLELLEA--------VGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 763 NHLLHR-CILGVLSHTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEILPLVQ---AVPTAWAEKEQVATSGQSPS 837
Cdd:COG1123 179 AEILDLlRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQalaAVPRLGAARGRAAPAAAAAE 258
|
.
gi 24850123 838 V 838
Cdd:COG1123 259 P 259
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1272-1473 |
4.13e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG-TIRE-- 1348
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRElv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 --------NLDPQGLHEDRAL-WQALEQCHLSEVAVamggldgelgERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:PRK11231 98 aygrspwlSLWGRLSAEDNARvNQAMEQTRINHLAD----------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1420 SVD-------QKTDQLLQQtickrfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPS 1473
Cdd:PRK11231 168 YLDinhqvelMRLMRELNT------QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPE 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1271-1479 |
5.10e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 81.90 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAelRSQLAVIPQEPFLFSG-TIREN 1349
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 ----LDPQGLHEDRALWQALEQCHLsevaVAMGGLdgeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1425
Cdd:cd03300 93 iafgLRLKKLPKAEIKERVAEALDL----VQLEGY---ANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1426 DQLLQQTIcKRFANK---TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:cd03300 166 RKDMQLEL-KRLQKElgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1254-1475 |
5.58e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVD-TSQ---LELA 1326
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1327 ELRSQLAVIPQ--EPFLFSGTIRENL--DPQ--GLHEDRALWQALEQchlsevaVAMGGLDGELGERGQ-NLSLGQRQLL 1399
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVafGPQnfGVSQEEAEALAREK-------LALVGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1400 CLARALLTDAKILCIDEATASVDQKTDQLLqQTICKRF--ANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKEL-MTLFKKLhqSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
622-802 |
5.73e-17 |
|
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: 81.36 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQ--CATIRDNILFG- 688
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkELRRKVGLVFQNPDDQffGPTVEEEVAFGl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ------KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03225 102 enlglpEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24850123 763 NHLLHrcILGVL--SHTTRLLCTHRTEYLER-ADVVLLMEAGQ 802
Cdd:cd03225 171 RELLE--LLKKLkaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1255-1478 |
6.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.48 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:PRK13647 5 IEVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEP--FLFSGTIRENL--DPQGLHEDRAlwQALEQCHLSEVAVAMggldGELGERG-QNLSLGQRQLLCLARALLTDA 1409
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVafGPVNMGLDKD--EVERRVEEALKAVRM----WDFRDKPpYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1410 KILCIDEATASVDQKTDQLLqQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETL-MEILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
622-813 |
8.58e-17 |
|
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: 81.22 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWV----AVSELSKGFGLATQEPWIQ--CATIRDNILFG- 688
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKptsgevLVDGKDitkkNLRELRRKVGLVFQNPDDQlfAPTVEEDVAFGp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 -------KTFDAQLyREVLEACALND--DLSILpagdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:COG1122 102 enlglprEEIRERV-EEALELVGLEHlaDRPPH-------------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 760 DVANHLLHrcILGVL--SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1122 168 RGRRELLE--LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
961-1223 |
9.38e-17 |
|
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: 83.31 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 961 AASNGTADVH----FYLIVYATIAGVNSLCTL--LRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFS 1034
Cdd:cd18600 55 SSSNTYAVIVtftsSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1035 SDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLAD 1114
Cdd:cd18600 135 KDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1115 TLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLVLS 1194
Cdd:cd18600 215 SLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG---EGRVGIILT 291
|
250 260
....*....|....*....|....*....
gi 24850123 1195 YALSLTGLLSGLVSSFTQTEAMMVSVERL 1223
Cdd:cd18600 292 LAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1255-1475 |
1.26e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVY-RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLA 1333
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1334 VIPQEP-FLFSGTIREN-----LDPQGLHEDRALWQaleqchLSEVAVAMGGLDGELGERGQnLSLGQRQLLCLARALLT 1407
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDdvafgMENQGIPREEMIKR------VDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1408 DAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1264-1463 |
1.27e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1264 YRPGLPNALDGVTFRVEPGE-KLgIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLF 1342
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEfKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1343 SGTIRENL-----------DPQGLHEDRALWqaleqchlsevavamgGLDGELGERGQN-LSLGQRQLLCLARALLTDAK 1410
Cdd:PRK10247 94 GDTVYDNLifpwqirnqqpDPAIFLDDLERF----------------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1411 ILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQA 1463
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
622-802 |
1.88e-16 |
|
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: 78.06 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGwvavselskgfglatqepwiqcatirdNILFGKTFDAQLYREvle 701
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG---------------------------EILIDGKDIAKLPLE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 702 acALNDDLSILPagdQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHRCILGVL-SHTTRL 780
Cdd:cd00267 70 --ELRRRIGYVP---Q---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVI 134
|
170 180
....*....|....*....|...
gi 24850123 781 LCTHRTEYLERA-DVVLLMEAGQ 802
Cdd:cd00267 135 IVTHDPELAELAaDRVIVLKDGK 157
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1272-1468 |
2.26e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE--PNA---GRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG-T 1345
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IRENLdPQGLH-----------EDRALWqALEQCHLSEvavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCI 1414
Cdd:PRK14247 99 IFENV-ALGLKlnrlvkskkelQERVRW-ALEKAQLWD------EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1415 DEATASVDQKTDQLLQQTICKRFANKTVLTIAH------RLntilnSDRVLVLQAGRVVE 1468
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1255-1467 |
2.44e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV---LLDNVDTSQLELAE- 1327
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1328 --------------------LRSQLAVIPQ--EPFLFSGTIRENL--DPQ--GLHEDRALWQALEQchlsevaVAMGGLD 1381
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIifGPVsmGVSKEEAKKRAAKY-------IELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1382 GELGERGQ-NLSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQqtICKRF--ANKTVLTIAHRLNTILN-SD 1456
Cdd:PRK13651 156 ESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILE--IFDNLnkQGKTIILVTHDLDNVLEwTK 233
|
250
....*....|.
gi 24850123 1457 RVLVLQAGRVV 1467
Cdd:PRK13651 234 RTIFFKDGKII 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
621-803 |
2.51e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLL-------AAITGELhrLCGWVAVSELSKGFGLATQE----PWiqcATIRDNI---L 686
Cdd:PRK11247 32 DLHIPAGQFVAVVGRSGCGKSTLLrllagleTPSAGEL--LAGTAPLAEAREDTRLMFQDarllPW---KKVIDNVglgL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FGKTFDAQLyrEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV---AN 763
Cdd:PRK11247 107 KGQWRDAAL--QALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrieMQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24850123 764 HLLHRciLGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQL 803
Cdd:PRK11247 174 DLIES--LWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1254-1479 |
2.54e-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: 80.08 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLA 1333
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1334 VIPQEPFLFSG-TIRENLdPQGLHEDRALWQALEQCHLSEVA--VAMGGLDGeLGERGQN-LSLGQRQLLCLARALLTDA 1409
Cdd:cd03296 78 FVFQHYALFRHmTVFDNV-AFGLRVKPRSERPPEAEIRAKVHelLKLVQLDW-LADRYPAqLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1410 KILCIDEATASVDQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1272-1479 |
2.72e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE------PNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG- 1344
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 TIREN----LDPQGLHEDRALWQALEQChLSEVAVAMGGLDgELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:PRK14246 106 SIYDNiaypLKSHGIKEKREIKKIVEEC-LRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1421 VDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
623-809 |
3.10e-16 |
|
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: 78.99 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 623 QVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTF 691
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALfrfleaeEGKIEidgIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 692 DAQLYrEVLEacalnddlsilpagdqteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCIL 771
Cdd:cd03369 110 DEEIY-GALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALIQKTIR 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 24850123 772 GVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPP 809
Cdd:cd03369 170 EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
567-813 |
6.60e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.84 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 567 VSLDRIQRFLDlpsySPEAYYSPDPPAEPSTALELHEALFSWDpigaSQKTFISH--LQVKKGMLVGIVGKVGCGKSSLL 644
Cdd:PRK10790 313 VAGERVFELMD----GPRQQYGNDDRPLQSGRIDIDNVSFAYR----DDNLVLQNinLSVPSRGFVALVGHTGSGKSTLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 645 AAITGELHRLCGWV-----AVSELS-----KGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPA 714
Cdd:PRK10790 385 SLLMGYYPLTEGEIrldgrPLSSLShsvlrQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 715 GDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTRLLCTHRTEYLERADV 794
Cdd:PRK10790 465 GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTIVEADT 543
|
250
....*....|....*....
gi 24850123 795 VLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10790 544 ILVLHRGQAVEQGTHQQLL 562
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
621-803 |
8.32e-16 |
|
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: 76.87 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILfgkt 690
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpNELGDHVGYLPQDDELFSGSIAENIL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 fdaqlyrevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI 770
Cdd:cd03246 98 -------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|...
gi 24850123 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03246 141 ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1272-1433 |
8.99e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTsqlELAELRSQLAVI----PQEPFLfsgTIR 1347
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLghrnAMKPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLdpqglhedrALWQALEQCHLSEVAVAMG--GLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1425
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALEavGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*...
gi 24850123 1426 DQLLQQTI 1433
Cdd:PRK13539 163 VALFAELI 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1259-1466 |
1.16e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 76.70 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1259 DVVLVYRP-GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQ-LAVIP 1336
Cdd:cd03215 2 EPVLEVRGlSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1337 QEPF---LFSG-TIRENLdpqglhedralwqALEQcHLSevavamGGldgelgergqNLslgqrQLLCLARALLTDAKIL 1412
Cdd:cd03215 82 EDRKregLVLDlSVAENI-------------ALSS-LLS------GG----------NQ-----QKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1413 CIDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLI-RELAdaGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
622-813 |
1.47e-15 |
|
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: 78.16 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCA-TIRDNILFGKT 690
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsrRELARRIAYVPQEPPAPFGlTVRELVALGRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 --------FDAQLYREVLEACAlnddlsilpagdQTEVG---EKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:COG1120 102 phlglfgrPSAEDREAVEEALE------------RTGLEhlaDRPVdELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 759 advANHLLHrcILGVLSHTTR------LLCTH------RTeylerADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1120 170 ---LAHQLE--VLELLRRLARergrtvVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
568-825 |
1.87e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.48 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 568 SLDRIQRFLDLPSYSPEAYYS--PdPPAEPST-ALELHEALFSWDP------------IGASQKtfishlqvkkgmlVGI 632
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLVIENnrP-PPGWPSSgSIKFEDVVLRYRPelppvlhglsfeISPSEK-------------VGI 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 633 VGKVGCGKSSLLAAI--TGELHRLCGWV--------AVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYrEVLE 701
Cdd:PLN03130 1271 VGRTGAGKSSMLNALfrIVELERGRILIdgcdiskfGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLW-ESLE 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 702 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTRLL 781
Cdd:PLN03130 1350 RAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFKSCTMLI 1428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 782 CTHRTEYLERADVVLLMEAGQLVRTGPPSEILP--------LVQAVPTAWAE 825
Cdd:PLN03130 1429 IAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnegsafskMVQSTGAANAQ 1480
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
621-803 |
1.87e-15 |
|
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: 77.14 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAIT-------GELhRLCGwVAVSELSKG----------------FGLatqepwIQ 677
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGgldrptsGEV-RVDG-TDISKLSEKelaafrrrhigfvfqsFNL------LP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 678 CATIRDNILFGKTF-------DAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLL 750
Cdd:cd03255 96 DLTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 751 DDPLAAVDADVANHLLHrcILGVLSH---TTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03255 165 DEPTGNLDSETGKEVME--LLRELNKeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1255-1473 |
2.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNV----DTSQLELAE 1327
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1328 LRSQLAVIPQEP--FLFSGTIRENL--DPQ--GLHEDRALWQALEQchlsevaVAMGGLDGELGERGQ-NLSLGQRQLLC 1400
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQnfGIPKEKAEKIAAEK-------LEMVGLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1401 LARALLTDAKILCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPS 1473
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
622-813 |
3.16e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.04 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELS---KGFGLATQEPwiqcA-----TIRDNILF 687
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRDLFTNLPpreRRVGFVFQHY----AlfphmTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 G----KTFDAQLYREVLEacaLnddLSIL---------PAgdQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:COG1118 99 GlrvrPPSKAEIRARVEE---L---LELVqlegladryPS--Q---------LSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 755 AAVDADVANHL------LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1118 162 GALDAKVRKELrrwlrrLHDEL-----GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1271-1468 |
3.95e-15 |
|
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: 80.11 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA----GRVLLDNVDTSQLELAELR----SQLAVIPQEPF-- 1340
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERELRrirgNRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1341 ---LFS-GT-IRENLDpqgLH--------EDRALwQALEQCHLSEVAvamggldGELGERGQNLSLGQRQLLCLARALLT 1407
Cdd:COG4172 105 lnpLHTiGKqIAEVLR---LHrglsgaaaRARAL-ELLERVGIPDPE-------RRLDAYPHQLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1408 DAKILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:COG4172 174 EPDLLIADEPTTALDvtvQA--QILDllKDLQREL-GMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
622-817 |
4.46e-15 |
|
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: 76.39 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-------------ELSKGFGLATQepwiQCA-----TIRD 683
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgedisglseaelyRLRRRMGMLFQ----SGAlfdslTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NILFG----KTFDAQLYREV----LEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:cd03261 97 NVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 756 AVD---ADVANHLLHRciLGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL----PLVQ 817
Cdd:cd03261 166 GLDpiaSGVIDDLIRS--LKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEELRasddPLVR 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1281-1467 |
5.35e-15 |
|
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: 75.41 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1281 PGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNV---DTSQ-LELAELRSQLAVIPQEPFLFSG-TIRENLDpQGL 1355
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPHlNVRENLA-FGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1356 hedRALWQALEQCHLSEVAVAMGgLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK 1435
Cdd:cd03297 101 ---KRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*
gi 24850123 1436 RFA--NKTVLTIAHRLNTI-LNSDRVLVLQAGRVV 1467
Cdd:cd03297 177 IKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1255-1467 |
5.49e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.20 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQL 1332
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEP--FLFSGTIRENLD----PQGLHEDralwqalEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALL 1406
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSfgavNLKLPED-------EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1407 TDAKILCIDEATASVDQK-TDQLLQqtICKRFANKTVLTI---AHRLNTI-LNSDRVLVLQAGRVV 1467
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMgVSEIMK--LLVEMQKELGLTIiiaTHDIDIVpLYCDNVFVMKEGRVI 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
621-807 |
5.61e-15 |
|
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: 75.41 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVK---KGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-----ELSKGFGLATQEPWI-----QCA-----TIR 682
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfDSRKKINLPPQQRKIglvfqQYAlfphlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 683 DNILFGKTF-----DAQLYREVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:cd03297 94 ENLAFGLKRkrnreDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 757 VDADVANHLLH--RCILGVLsHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03297 162 LDRALRLQLLPelKQIKKNL-NIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1255-1479 |
5.74e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQLELAELRSQ 1331
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1332 LAVIPQEP-FLFSGTIRENLDPQGLhEDRALWQALEQCHLSEVAVAMGGLDGELGERgQNLSLGQRQLLCLARALLTDAK 1410
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1411 ILCIDEATASVDQK-TDQLLQqtICKRFANK---TVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK13640 164 IIILDESTSMLDPAgKEQILK--LIRKLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1255-1467 |
5.78e-15 |
|
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: 76.28 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVY--RPglpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV--LLDNvDTSQLELAELRS 1330
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGE-RRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1331 QLAVI-P--QEPFLFSGTIRE--------------NLDPQglHEDRAlWQALEQCHLSEVAvamggldgelGERGQNLSL 1393
Cdd:COG1119 79 RIGLVsPalQLRFPRDETVLDvvlsgffdsiglyrEPTDE--QRERA-RELLELLGLAHLA----------DRPFGTLSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1394 GQRQLLCLARALLTDAKILCIDEATASVDQK-TDQLLQ--QTICKRFAnKTVLTIAHRLNTILNS-DRVLVLQAGRVV 1467
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGaRELLLAllDKLAAEGA-PTLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1262-1476 |
7.77e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.10 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1262 LVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAVIPQEPFL 1341
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 FSG-TIRENLDPQGlhedrAL----WQALEQcHLSEVAVAMGGLDGElGERGQNLSLGQRQLLCLARALLTDAKILCIDE 1416
Cdd:cd03265 85 DDElTGWENLYIHA-----RLygvpGAERRE-RIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1417 ATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTI-LNSDRVLVLQAGRVVELDSPSALR 1476
Cdd:cd03265 158 PTIGLDPQTrAHVWEyiEKLKEEF-GMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1254-1478 |
1.41e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.97 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVD----TSQLELA 1326
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1327 ELRSQLAVIPQ--EPFLFSGTI-RENL-DPQGLHEDralwqaleqchLSEVAVAMGGLDGELGERGQNLSL-------GQ 1395
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVeREIIfGPKNFKMN-----------LDEVKNYAHRLLMDLGFSRDVMSQspfqmsgGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1396 RQLLCLARALLTDAKILCIDEATASVDQKT-DQLLqqTICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 1470
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSkRQVM--RLLKSLQtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQT 228
|
....*...
gi 24850123 1471 SPSALRNQ 1478
Cdd:PRK13646 229 SPKELFKD 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
621-813 |
1.43e-14 |
|
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: 74.89 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELSK----------GFGLatqePWIQcaTIRDN 684
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVRKEPREarrqigvlpdERGL----YDRL--TVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFgktFdAQLYREVLEACALNDDlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvAN 763
Cdd:COG4555 95 IRY---F-AELYGLFDEELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM-AR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 764 HLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4555 169 RLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1266-1479 |
1.85e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1266 PGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDT---SQLELAELRSQLAVIPQEPFlf 1342
Cdd:PRK11308 25 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1343 sgtirENLDP-----QGLHEDRALWQALEQCHLSEVAVAMG---GLDGELGERGQNL-SLGQRQLLCLARALLTDAKILC 1413
Cdd:PRK11308 103 -----GSLNPrkkvgQILEEPLLINTSLSAAERREKALAMMakvGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1414 IDEATASVD-----QKTDQL--LQQTIckrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK11308 178 ADEPVSALDvsvqaQVLNLMmdLQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1236-1479 |
2.25e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1236 SQPLQSPHQQRISWLTQGSVefQDVVlvyrpglpnalDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePN------ 1309
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTV--RTVV-----------NDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvyp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1310 ------AGRVLLDnvdTSQLELAELR-SQLAVIPQEPfLFSGTIRENLDPQgLHEDRALWQALEQchlsEVAVA--MGGL 1380
Cdd:PRK15134 68 sgdirfHGESLLH---ASEQTLRGVRgNKIAMIFQEP-MVSLNPLHTLEKQ-LYEVLSLHRGMRR----EAARGeiLNCL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1381 D--------GELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD----QLLQQTicKRFANKTVLTIAHR 1448
Cdd:PRK15134 139 DrvgirqaaKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLREL--QQELNMGLLFITHN 216
|
250 260 270
....*....|....*....|....*....|..
gi 24850123 1449 LNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK15134 217 LSIVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1272-1468 |
3.48e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRS-----QL-------AVIPQEp 1339
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMvfqdsisAVNPRK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1340 flfsgTIRENLDpQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:PRK10419 107 -----TVREIIR-EPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1420 SVD-----QKTDQL--LQQ---TICkrfanktvLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:PRK10419 181 NLDlvlqaGVIRLLkkLQQqfgTAC--------LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1271-1479 |
3.94e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL---DNVDTSQLELAELRSQLAVIPQEPfLFSgtir 1347
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDP-LAS---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 enLDPQGLHED------RALWQALEQCHLSEVAVAM----GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEA 1417
Cdd:PRK15079 111 --LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkvGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1418 TASVD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK15079 189 VSALDvsiqAQVVNLLQQL--QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1262-1431 |
4.00e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1262 LVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDnvdtsQLELAELRSQlaviPQEPFL 1341
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN-----GTPLAEQRDE----PHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 FSG---------TIRENLD---PQGLHEDRALWQALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLTDA 1409
Cdd:TIGR01189 77 YLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAV----------GLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180
....*....|....*....|..
gi 24850123 1410 KILCIDEATASVDQKTDQLLQQ 1431
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAG 168
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1271-1472 |
4.49e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.35 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLE-LAELRSQLAVIPQEP-FLFSGTIRE 1348
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 N---LDPQGL----HEDRA-LWQALEQCHLSEVAVAMGGLdgelgergqnLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:PRK13633 105 EdvaFGPENLgippEEIRErVDESLKKVGMYEYRRHAPHL----------LSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1421 VDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1472
Cdd:PRK13633 175 LDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1271-1465 |
4.76e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNA---GRVLLD-------NV-DTSQLELAELRSQLAVIPQEp 1339
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEgeelqasNIrDTERAGIAIIHQELALVKEL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1340 flfsgTIREN------LDPQGLHEDRALWQALEQChLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILC 1413
Cdd:PRK13549 98 -----SVLENiflgneITPGGIMDYDAMYLRAQKL-LAQL-----KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1414 IDEATASV-DQKTDQLLqqTICKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGR 1465
Cdd:PRK13549 167 LDEPTASLtESETAVLL--DIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
622-813 |
6.51e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 6.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAIT-------GEL----HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILFGKT 690
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEIlldgHDLRDY-TLASLRNQVALVSQNVHLFNDTIANNIAYART 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 fdAQLYREVLE-----ACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVanhl 765
Cdd:PRK11176 443 --EQYSREQIEeaarmAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES---- 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 766 lHRCILGVLS----HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK11176 516 -ERAIQAALDelqkNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
622-813 |
8.22e-14 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGLATQEPWIQCA--------------TIRDNILF 687
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL------FGKPPRRARRRIGyvpqraevdwdfpiTVRDVVLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 G--------KTFDAQLYREVLEACALnddLSILPAGDQTeVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:COG1121 101 GrygrrglfRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 760 DVANHLLHrcILGVLSH--TTRLLCTHRTEYLER-ADVVLLMeAGQLVRTGPPSEIL 813
Cdd:COG1121 173 ATEEALYE--LLRELRRegKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1271-1479 |
8.52e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVdtsqlELAELRSQ----LAVIP--QEPFLF-S 1343
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-----HIEGLPGHqiarMGVVRtfQHVRLFrE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 GTIRENL-DPQGLH------------------EDRALWQA---LEQCHLSEVAVAMGGldgelgergqNLSLGQRQLLCL 1401
Cdd:PRK11300 95 MTVIENLlVAQHQQlktglfsgllktpafrraESEALDRAatwLERVGLLEHANRQAG----------NLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1402 ARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 244
|
.
gi 24850123 1479 P 1479
Cdd:PRK11300 245 P 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1271-1468 |
9.18e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFlfsgtir 1347
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPN------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLDPQgLHEDRALWQALE--QCHLS------EVAVAMG--GLDGELGER-GQNLSLGQRQLLCLARALLTDAKILCIDE 1416
Cdd:PRK15134 373 SSLNPR-LNVLQIIEEGLRvhQPTLSaaqreqQVIAVMEevGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1417 ATASVDqKTDQLLQQTICKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:PRK15134 452 PTSSLD-KTVQAQILALLKSLQQKHQLAylfISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1271-1472 |
9.78e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAelrsqLAVIPQepflFSGtiREN- 1349
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELG-----AGFHPE----LTG--RENi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 --------LDPQglhEDRALwqaLEQChlseVAVAmggldgELGE------RgqNLSLGQRQLLCLARALLTDAKILCID 1415
Cdd:COG1134 110 ylngrllgLSRK---EIDEK---FDEI----VEFA------ELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1416 EATASVD----QKTDQLLQQticKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:COG1134 172 EVLAVGDaafqKKCLARIRE---LRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1272-1480 |
1.13e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL-AELRSQLAVIPQEPFLFSG------ 1344
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlsvydn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 -----TIRENLDPQGlHEDRALwQALEQCHLSEVAVAMggldgelgerGQNLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:PRK10895 99 lmavlQIRDDLSAEQ-REDRAN-ELMEEFHIEHLRDSM----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1420 SVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQPH 1480
Cdd:PRK10895 167 GVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1271-1470 |
1.24e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 71.79 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL-AELRSQLAVIpqEPFLFSGTIReN 1349
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPELTGR--ENIYLNGRLL-G 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 LDPQglhEDRALWQALEQchLSevavamggldgELGERGQ----NLSLGQRQLLCLARALLTDAKILCIDEATASVD--- 1422
Cdd:cd03220 114 LSRK---EIDEKIDEIIE--FS-----------ELGDFIDlpvkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaaf 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 1423 -QKTDQLLQQTICKrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 1470
Cdd:cd03220 178 qEKCQRRLRELLKQ---GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
962-1196 |
1.43e-13 |
|
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: 72.68 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 962 ASNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVD 1041
Cdd:pfam00664 33 GDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1042 DSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPV 1121
Cdd:pfam00664 113 DGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRT 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1122 LRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLVLSYA 1196
Cdd:pfam00664 193 VKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
287-572 |
1.59e-13 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 72.97 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 287 LALGLLKM-VGTMLGFSGPLLLSLLVGFLEeGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLY 365
Cdd:cd07346 1 LLLALLLLlLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 366 RKALKLGPS---RPPTGEVLNLLGTDSERLLNFAGS-FHEAWGLPLQLAITL-YLLYQQVGMAFLAGLVLALLLVPvNKV 440
Cdd:cd07346 80 RHLQRLSLSffdRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALvILFYLNWKLTLVALLLLPLYVLI-LRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 441 IATRIMASNQEmLRHKDARV-KLMTELLSGIRVIKFFRWEQALGDRVKAcRTKELGRLRVIKYLDAACVYLWAALPVVIC 519
Cdd:cd07346 159 FRRRIRKASRE-VRESLAELsAFLQESLSGIRVVKAFAAEEREIERFRE-ANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 520 ITIFITY----VLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd07346 237 TALVLLYggylVLQG-SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
622-803 |
1.92e-13 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 69.73 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGlatQEPWIQCATIRDNILFgktfdaqlyreVLE 701
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV------LG---KDIKKEPEEVKRRIGY-----------LPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 702 ACALNDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS--HTTR 779
Cdd:cd03230 81 EPSLYENLT----------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKkeGKTI 148
|
170 180
....*....|....*....|....*
gi 24850123 780 LLCTHRTEYLER-ADVVLLMEAGQL 803
Cdd:cd03230 149 LLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1254-1475 |
2.01e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.33 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-LLDNVDTSQLELAelRSQL 1332
Cdd:PRK13536 41 AIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLA--RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFL-FSGTIRENLDPQGLH---EDRALWQALEQchLSEVAvamgGLDGELGERGQNLSLGQRQLLCLARALLTD 1408
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLLVFGRYfgmSTREIEAVIPS--LLEFA----RLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1409 AKILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
614-807 |
2.57e-13 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 70.64 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 614 SQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV-----SELSKGFGLATQE---PWIQCATIRD 683
Cdd:cd03235 10 GGHPVLEDvsFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplEKERKRIGYVPQRrsiDRDFPISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NIL--------FGKTFDAQLYREVLEAcalnddlsiLPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:cd03235 90 VVLmglyghkgLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 755 AAVDADVANHLLHrcILGVLSHTTR--LLCTH-RTEYLERADVVLLMeAGQLVRTG 807
Cdd:cd03235 161 AGVDPKTQEDIYE--LLRELRREGMtiLVVTHdLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1271-1471 |
2.60e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPN---AGRVLLD--NVDTSQLELAELRSQLAVIPQEPFLFS 1343
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNghNIYSPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 GTIREN----LDPQGLHEDRALWQALEQChLSEVAVAMGGLDgELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:PRK14239 100 MSIYENvvygLRLKGIKDKQVLDEAVEKS-LKGASIWDEVKD-RLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1420 SVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 1471
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
616-813 |
3.04e-13 |
|
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: 71.48 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 616 KTFISHLQ--VKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQCATIRD 683
Cdd:cd03288 34 KPVLKHVKayIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDgidisklplhTLRSRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NI-LFGKTFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03288 114 NLdPECKCTDDRLW-EALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 763 NhLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03288 193 N-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
621-807 |
3.28e-13 |
|
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: 69.39 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELhrlcgwvavsELSKGfglatqepwiqcaTIRdniLFGKTFDAQLYREVL 700
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLL----------KPSSG-------------EIL---LDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 701 EACAlnddlsILP-AGDQTEVG---EKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS 775
Cdd:cd03214 73 RKIA------YVPqALELLGLAhlaDRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 24850123 776 H---TTRLLCTHrteYLERA----DVVLLMEAGQLVRTG 807
Cdd:cd03214 145 RergKTVVMVLH---DLNLAaryaDRVILLKDGRIVAQG 180
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1270-1472 |
3.69e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1270 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAEL---------RSQLAVIPQEP- 1339
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1340 ------FLFSGTIRENLDPQGL-HEDRALWQALEQchLSEVAVAMGGLDgelgERGQNLSLGQRQLLCLARALLTDAKIL 1412
Cdd:PRK11701 100 dglrmqVSAGGNIGERLMAVGArHYGDIRATAGDW--LERVEIDAARID----DLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1413 CIDEATA----SVDQKTDQLLQQTIckRFANKTVLTIAHRLNTI-LNSDRVLVLQAGRVVE-------LDSP 1472
Cdd:PRK11701 174 FMDEPTGgldvSVQARLLDLLRGLV--RELGLAVVIVTHDLAVArLLAHRLLVMKQGRVVEsgltdqvLDDP 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1255-1472 |
3.89e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.59 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN----VDTSQLELAE 1327
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1328 LRSQLAVIPQ--EPFLFSGTIRENL--DPQ--GLHEDRALWQALEqchlsevAVAMGGLDGELGERGQ-NLSLGQRQLLC 1400
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMnfGVSEEDAKQKARE-------MIELVGLPEELLARSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1401 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
622-807 |
4.48e-13 |
|
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: 70.23 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV-------------SELSKGFGLATQE------PWIqcaTIR 682
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsrrlrKIRRKEIQMVFQDpmsslnPRM---TIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 683 DNI-----LFGKTFDAQLYREV--LEACALNDDLSIL---PAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDD 752
Cdd:cd03257 103 EQIaeplrIHGKLSKKEARKEAvlLLLVGVGLPEEVLnryPH-----------ELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 753 PLAAVDADVAnhllhRCILGVLSH------TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03257 172 PTSALDVSVQ-----AQILDLLKKlqeelgLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
622-812 |
4.58e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.44 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQEPwiqcA-----TIRDNILFG 688
Cdd:COG3842 26 LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgrdVTGLPpekRNVGMVFQDY----AlfphlTVAENVAFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 -------KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARA-VYQEKALyLLDDPLAAVDAD 760
Cdd:COG3842 102 lrmrgvpKAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRVALARAlAPEPRVL-LLDEPLSALDAK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 761 VANHL------LHRcILGVlshTTrLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:COG3842 170 LREEMreelrrLQR-ELGI---TF-IYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1255-1473 |
5.11e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.26 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQL 1332
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEP--FLFSGTIRE-------NLdpqGLHED---RALWQALEqchlsevAVAMGGLDgelGERGQNLSLGQRQLLC 1400
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEdvafgplNL---GLSKEeveKRVKEALK-------AVGMEGFE---NKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1401 LARALLTDAKILCIDEATASVD----QKTDQLLQQTickrfaNKTVLTI---AHRLNTI-LNSDRVLVLQAGRVVELDSP 1472
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDL------NKEGITIiisTHDVDLVpVYADKVYVMSDGKIIKEGTP 221
|
.
gi 24850123 1473 S 1473
Cdd:PRK13639 222 K 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1271-1475 |
5.19e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQEPFLFSG-TIRE 1348
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NLDPQGLHEDRALWQAleqcHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1428
Cdd:PRK11614 100 NLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24850123 1429 LQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK11614 176 IFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
569-822 |
5.29e-13 |
|
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: 73.40 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 569 LDRIQRFLDLPSYSPEAYYSPDPPAEPSTALELHEALFSWDPIGASQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAA 646
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAVDDvsLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 647 ITG--------------ELHRLCGwVAVSELSKGFGLATQEPWIQ---CATIRDNI-----LFGKTFDAQLY---REVLE 701
Cdd:COG1123 311 LLGllrptsgsilfdgkDLTKLSR-RSLRELRRRVQMVFQDPYSSlnpRMTVGDIIaeplrLHGLLSRAERRervAELLE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 702 ACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVANHLLH-RCILGVls 775
Cdd:COG1123 390 RVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqAQILNLLRDlQRELGL-- 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 776 htTRLLCTH---RTEYLerADVVLLMEAGQLVRTGPPSEIL--P-------LVQAVPTA 822
Cdd:COG1123 457 --TYLFISHdlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFanPqhpytraLLAAVPSL 511
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1255-1470 |
5.54e-13 |
|
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: 69.59 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLAV 1334
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEPFLFSG-TIRENLdPQGLHEDRALWQALEQcHLSEVAvAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILC 1413
Cdd:cd03301 77 VFQNYALYPHmTVYDNI-AFGLKLRKVPKDEIDE-RVREVA-ELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1414 IDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 1470
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1264-1468 |
5.90e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1264 YRPGL-----PNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtSQLELAE--LRSQ-LAVI 1335
Cdd:PRK15112 16 YRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGDysYRSQrIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1336 PQEPF-----------LFSGTIRENLDPQGLHEDRALWQALEQchlsevavaMGGLDGELGERGQNLSLGQRQLLCLARA 1404
Cdd:PRK15112 93 FQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQ---------VGLLPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1405 LLTDAKILCIDEATASVD-----QKTDQLLQ----QTICKRFANKTVLTIAHRlntilnSDRVLVLQAGRVVE 1468
Cdd:PRK15112 164 LILRPKVIIADEALASLDmsmrsQLINLMLElqekQGISYIYVTQHLGMMKHI------SDQVLVMHQGEVVE 230
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
287-552 |
6.75e-13 |
|
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: 70.75 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 287 LALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEP----LSHGLLYVLGLAGGTVISAVLQNqygYEVRKVTLQARVAVLS 362
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetqaLNVYSLALLLLGLAQFILSFLQS---YLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 363 TLYRKALKLGPS---RPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLAL-LLVPVN 438
Cdd:pfam00664 79 KLFKKILRQPMSffdTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLpLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 439 KVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLR---VIKYLDAACVYLWAALp 515
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIkkaVANGLSFGITQFIGYL- 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 24850123 516 VVICITIFITYVLMGHQLTATKVFTALALVRMLILPL 552
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
622-807 |
7.03e-13 |
|
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: 69.21 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELS---KGFGLATQE----PWIqcaTIRDNILFG 688
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAG-LEEptsgriYIGGRDVTDLPpkdRDIAMVFQNyalyPHM---TVYDNIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ----KTFDAQLYREVLEACALnddLSIlpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:cd03301 97 lklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 765 L------LHRcILGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03301 169 MraelkrLQQ-RLG----TTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1234-1471 |
7.48e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1234 PHSQPLQSPHQQRISWLtqgSVEFQDvvlvYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV 1313
Cdd:PRK10261 2 PHSDELDARDVLAVENL---NIAFMQ----EQQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1314 LLDN----------VDTSQLELAELR----SQLAVIPQEP-------FLFSGTIRENLD-PQGLHEDRALWQA---LEQC 1368
Cdd:PRK10261 74 QCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQEPmtslnpvFTVGEQIAESIRlHQGASREEAMVEAkrmLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1369 HLSEvAVAMggldgeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD-QLLQQ-TICKRFANKTVLTIA 1446
Cdd:PRK10261 154 RIPE-AQTI------LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLiKVLQKEMSMGVIFIT 226
|
250 260
....*....|....*....|....*.
gi 24850123 1447 HRLNTILN-SDRVLVLQAGRVVELDS 1471
Cdd:PRK10261 227 HDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1271-1467 |
7.83e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 69.67 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-LLDNVDTSQLElaELRSQLAVI------------PQ 1337
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRK--KFLRRIGVVfgqktqlwwdlpVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1338 EPFLFSGTIReNLDPQGLHEDRAlwqaleqcHLSEvavaMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEA 1417
Cdd:cd03267 114 DSFYLLAAIY-DLPPARFKKRLD--------ELSE----LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1418 TASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:cd03267 181 TIGLDVVAQENIRNFL--KEYNRergtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1271-1479 |
7.90e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 71.72 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVD-TSQLELAELRsqLAVIPQEPFLFSG-TIRE 1348
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERR--VGFVFQHYALFPHmTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 N----LDPQGLHEDRALWQALEQchLSEVavamgGLDGeLGER--GQnLSLGQRQLLCLARALLTDAKILCIDEATASVD 1422
Cdd:COG1118 95 NiafgLRVRPPSKAEIRARVEEL--LELV-----QLEG-LADRypSQ-LSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1423 QK-TDQL---LQQTIcKRFaNKTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:COG1118 166 AKvRKELrrwLRRLH-DEL-GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
660-797 |
7.99e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 660 VSELSKGFGLATQEPWIQCATIRDNILFGKTfDAQLyREVLEAC---ALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 736
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 737 LARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTRLLCT--HRTEYLERADVVLL 797
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVV 1430
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1218-1476 |
8.48e-13 |
|
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: 72.91 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1218 VSVERLEEYSCDVPQEPHSQPLQSPHQQRISWltqGSVEFQDVVLVYrpglPNALDGVTFRV-------EPGEKLGIVGR 1290
Cdd:COG4615 294 VALRKIEELELALAAAEPAAADAAAPPAPADF---QTLELRGVTYRY----PGEDGDEGFTLgpidltiRRGELVFIVGG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1291 TGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFsgtiRENLDPQGLHEDRALWQALEQCHL 1370
Cdd:COG4615 367 NGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1371 SE-VAVAmgglDGELGERgqNLSLGQRQLLCLARALLTDAKILCIDEATAsvDQktD---------QLLQQTicKRfANK 1440
Cdd:COG4615 443 DHkVSVE----DGRFSTT--DLSQGQRKRLALLVALLEDRPILVFDEWAA--DQ--DpefrrvfytELLPEL--KA-RGK 509
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24850123 1441 TVLTIAH-----RLntilnSDRVLVLQAGRVVELDSPSALR 1476
Cdd:COG4615 510 TVIAISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
622-807 |
9.72e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 69.22 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH---RLCGWVAV--SELSKG-----FGLATQ-EPWIQCATIRDNILFGKT 690
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFngQPRKPDqfqkcVAYVRQdDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 F-----DAQLYREVLEACALNDDLSILPAGDQTEVGekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL 765
Cdd:cd03234 108 LrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24850123 766 LHrcILGVLSHTTRL-LCT-H--RTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03234 183 VS--TLSQLARRNRIvILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1267-1472 |
9.98e-13 |
|
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: 72.53 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1267 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-------LLDNVDTSQLELAELRSQLAVIPQEP 1339
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1340 FLFS-GTIRENL-DPQGLH--EDRALWQALeqchlseVAVAMGGLDGE-----LGERGQNLSLGQRQLLCLARALLTDAK 1410
Cdd:TIGR03269 375 DLYPhRTVLDNLtEAIGLElpDELARMKAV-------ITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1411 ILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1276-1478 |
1.22e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1276 TFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAelRSQLAVIPQEPFLFSG-TIREN----L 1350
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNiglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 DPqGLHEDRAlwqalEQCHLSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD----QKTD 1426
Cdd:PRK10771 97 NP-GLKLNAA-----QREKLHAIARQM-GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1427 QLLQQtICKRfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:PRK10771 170 TLVSQ-VCQE-RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSG 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1267-1468 |
1.24e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.91 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1267 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---------GRVLLdnvDTSQLELAELRS-QLAVIP 1336
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGriggsatfnGREIL---NLPEKELNKLRAeQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1337 QEPFlfsgtirENLDPQ-----------GLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARAL 1405
Cdd:PRK09473 104 QDPM-------TSLNPYmrvgeqlmevlMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1406 LTDAKILCIDEATASVDQkTDQ-----LLQQTicKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVVE 1468
Cdd:PRK09473 177 LCRPKLLIADEPTTALDV-TVQaqimtLLNEL--KREFNTAIIMITHDLGVVAGIcDKVLVMYAGRTME 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1258-1477 |
1.33e-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: 73.12 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1258 QDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTsQLELAELRSQLAVIPQ 1337
Cdd:TIGR01257 932 KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1338 EPFLFSG-TIRENLdpqgLHEDRALWQALEQCHLS-EVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 1415
Cdd:TIGR01257 1011 HNILFHHlTVAEHI----LFYAQLKGRSWEEAQLEmEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1416 EATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTI-LNSDRVLVLQAGRVVELDSPSALRN 1477
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
621-813 |
1.34e-12 |
|
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: 69.45 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV--SELSKGFGLAT--------QEP-------WiqcaTIRD 683
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgRPVTRRRRKAFrrrvqmvfQDPyaslhprH----TVDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NI-----LFGKTFDAQLYREVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:COG1124 101 ILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 758 D----ADVANhLLHRciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1124 170 DvsvqAEILN-LLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1272-1425 |
1.41e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL---AELRSQ-LAVIPQEPFLFSG-TI 1346
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1347 RENLDPQGLHEDRALWQALEQCHLSEVAVamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1425
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAV---GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
622-807 |
1.98e-12 |
|
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: 67.90 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFGLATQEPwiQCATIRDNILFgktfdAQLYREVLE 701
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLF-----AHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 702 ACALNDDLSiLPAGDQTEV----GEKGV---------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhR 768
Cdd:cd03298 92 GLGLSPGLK-LTAEDRQAIevalARVGLaglekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-D 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24850123 769 CILGVLSHT--TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03298 170 LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
631-825 |
2.06e-12 |
|
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: 70.51 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 631 GIVGKVGCGKSSLLAAITGELHRLCGWVAVSElskgfglatqEPWIQCA-------------------------TIRDNI 685
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG----------EVLQDSArgiflpphrrrigyvfqearlfphlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 686 LFG-----KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:COG4148 99 LYGrkrapRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 761 VANHLLHrcILGVLSHTTR---LLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEILPLVQAVPTAWAE 825
Cdd:COG4148 168 RKAEILP--YLERLRDELDipiLYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGE 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
622-812 |
2.28e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.10 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSElsKGFGLATQEPwiqcA-----TIRDNIL 686
Cdd:COG3839 24 LDIEDGEFLVLLGPSGCGKSTLLRMIagledptSGEILiggRDVTDLPPKD--RNIAMVFQSY----AlyphmTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FG----KTFDAQLYREVLEACALnddLSI------LPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:COG3839 98 FPlklrKVPKAEIDRRVREAAEL---LGLedlldrKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 757 VDADVANHL------LHRcilgVLSHTTrLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:COG3839 164 LDAKLRVEMraeikrLHR----RLGTTT-IYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1272-1467 |
3.62e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAeLRSQLAV--IPQEPFLFSG-TIRE 1348
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NL-----DPQGLHED-RALWQALeQCHLSeVAVAMGGLDgelgergqnlsLGQRQLLCLARALLTDAKILCIDEATASVD 1422
Cdd:PRK15439 106 NIlfglpKRQASMQKmKQLLAAL-GCQLD-LDSSAGSLE-----------VADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24850123 1423 Q-KTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:PRK15439 173 PaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1267-1480 |
3.67e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1267 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLfRLLE-PNAGRVLLDN------VDTSQLELAELRSQLAVIPQE- 1338
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1339 ---PFLfsgTIRENL--DP---QGLHEDRALWQA---LEQCHLSEVAvamggldgelgER-GQNLSLGQRQLLCLARALL 1406
Cdd:PRK11124 92 nlwPHL---TVQQNLieAPcrvLGLSKDQALARAeklLERLRLKPYA-----------DRfPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1407 TDAKILCIDEATASVDQK-TDQL------LQQTickrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALrNQ 1478
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEiTAQIvsiireLAET------GITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASCF-TQ 230
|
..
gi 24850123 1479 PH 1480
Cdd:PRK11124 231 PQ 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
627-803 |
3.81e-12 |
|
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: 68.34 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 627 GMLVGIVGKVGCGKSSLLAA------ITGELH-RLCGW--VAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLY 696
Cdd:cd03289 30 GQRVGLLGRTGSGKSTLLSAflrllnTEGDIQiDGVSWnsVPLQKWRKAFGVIPQKVFIFSGTFRKNLdPYGKWSDEEIW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 697 ReVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSH 776
Cdd:cd03289 110 K-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFAD 187
|
170 180
....*....|....*....|....*..
gi 24850123 777 TTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03289 188 CTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1272-1472 |
4.14e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQLAVIPQEP--FLFSGTIR 1347
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 EN----LDPQGLHEDralwqalEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 1423
Cdd:PRK13638 97 SDiafsLRNLGVPEA-------EITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1424 K-TDQLLqqTICKRFA---NKTVLTiAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:PRK13638 170 AgRTQMI--AIIRRIVaqgNHVIIS-SHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
622-812 |
4.98e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 67.26 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSEL---SKGFGLATQE----PWIqcaTIRDNILF 687
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIagfetptSGEI--LLDGKDITNLpphKRPVNTVFQNyalfPHL---TVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 G----KTFDAQLYREVLEACalndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:cd03300 96 GlrlkKLPKAEIKERVAEAL----DLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 764 HL------LHRcILGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03300 168 DMqlelkrLQK-ELG----ITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1255-1475 |
6.41e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.29 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-LLDNVDTSQLELAelRSQLA 1333
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHA--RQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1334 VIPQ----EPFLfsgTIRENLDPQGLHEDRALWQALEQC-HLSEVAVAMGGLDGELGErgqnLSLGQRQLLCLARALLTD 1408
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVpPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1409 AKILCIDEATASVDQKTDQLLQQTICKRFAN-KTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1218-1470 |
6.84e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1218 VSVERLEEYSCDVPQEPHSQPLQSPHQQRIswltqgsvEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSS 1297
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPRPQAFPDWQTL--------ELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKST 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1298 LFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTirenLDPQGLHEDRALWQA-LEQCHLSE-VAV 1375
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHkLEL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1376 AmgglDGELgeRGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD--------QKTDQLLQQtickrfANKTVLTIAH 1447
Cdd:PRK10522 441 E----DGRI--SNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQE------MGKTIFAISH 508
|
250 260
....*....|....*....|...
gi 24850123 1448 RLNTILNSDRVLVLQAGRVVELD 1470
Cdd:PRK10522 509 DDHYFIHADRLLEMRNGQLSELT 531
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1255-1479 |
7.54e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 1334
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1335 IPQEP--FLFSGTIRENL--DPQGLHEDRALWQaleqcHLSEVAVAMGGLDgELGERG-QNLSLGQRQLLCLARALLTDA 1409
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEETVA-----HRVSSALHMLGLE-ELRDRVpHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1410 KILCIDEATASVD-QKTDQLLqqtickRFANK-------TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK13652 157 QVLVLDEPTAGLDpQGVKELI------DFLNDlpetygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1272-1479 |
7.58e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEP-----NAGRVLLDNVDT-SQLELAELRSQLAVIPQEPFLFSGT 1345
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IREN-LDPQGLHE--DRALWQALEQCHLSEVAVaMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 1422
Cdd:PRK14271 117 IMDNvLAGVRAHKlvPRKEFRGVAQARLTEVGL-WDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1423 QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
613-833 |
8.35e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 613 ASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSEL--------------SKGFGLATQEPWIQC 678
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeikpvRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 679 --ATIRDNILFGKTfDAQLYREVLEACALnDDLSILpaGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:PRK13643 98 feETVLKDVAFGPQ-NFGIPKEKAEKIAA-EKLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 756 AVDADVANHLLHrcILGVLSHT--TRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEILPLVQ-------AVPTAWAE 825
Cdd:PRK13643 174 GLDPKARIEMMQ--LFESIHQSgqTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDflkahelGVPKATHF 251
|
....*...
gi 24850123 826 KEQVATSG 833
Cdd:PRK13643 252 ADQLQKTG 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1213-1479 |
8.54e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1213 TEAMMVSVERLEEYS-CDVPQE------PHSQPLQSPHQQRISWLTQGSVEFQDVVLVY--RPGLPN-------ALDGVT 1276
Cdd:PRK10261 265 TRALLAAVPQLGAMKgLDYPRRfplislEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFplRSGLLNrvtrevhAVEKVS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1277 FRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDT-SQLELAELRSQLAVIPQEPF-------LFSGTI 1346
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQDPYasldprqTVGDSI 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1347 RENLDPQGLHEDRALWQALEQChLSEVavamgGLDGELGER-GQNLSLGQRQLLCLARALLTDAKILCIDEATASVD--- 1422
Cdd:PRK10261 425 MEPLRVHGLLPGKAAAARVAWL-LERV-----GLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvsi 498
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1423 --QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK10261 499 rgQIINLLLD---LQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
622-802 |
1.02e-11 |
|
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: 64.90 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGLATQEPWIQCATIRDNIlfGKTF-DAQLYR--E 698
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI------DGEDLTDLEDELPPLRRRI--GMVFqDFALFPhlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 699 VLEACALnddlsilpagdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL------LHRcILG 772
Cdd:cd03229 93 VLENIAL--------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVrallksLQA-QLG 151
|
170 180 190
....*....|....*....|....*....|.
gi 24850123 773 VlshtTRLLCTHRTEYLER-ADVVLLMEAGQ 802
Cdd:cd03229 152 I----TVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
589-812 |
1.04e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 589 PDPPAEPSTA----LELHEALFSWDPIGASQKTfisHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSels 664
Cdd:PRK11607 6 PRPQAKTRKAltplLEIRNLTKSFDGQHAVDDV---SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 665 kGFGLATQEPWIQC-------------ATIRDNILFGKTFDAQLYREVleACALNDDLSILPAgdQTEVGEKGVTLSGGQ 731
Cdd:PRK11607 80 -GVDLSHVPPYQRPinmmfqsyalfphMTVEQNIAFGLKQDKLPKAEI--ASRVNEMLGLVHM--QEFAKRKPHQLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 732 RARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSH--TTRLLCTH-RTEYLERADVVLLMEAGQLVRTGP 808
Cdd:PRK11607 155 RQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE-VVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
....
gi 24850123 809 PSEI 812
Cdd:PRK11607 234 PEEI 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1265-1479 |
1.14e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1265 RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN---------------VDTSQLELaeLR 1329
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvADKNQLRL--LR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1330 SQLAVIPQEPFLFSG-TIREN-----LDPQGLHEDRALWQALEqcHLSEVavamgGLDgelgERGQ-----NLSLGQRQL 1398
Cdd:PRK10619 92 TRLTMVFQHFNLWSHmTVLENvmeapIQVLGLSKQEARERAVK--YLAKV-----GID----ERAQgkypvHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1399 LCLARALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSA 1474
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPElVGEVLR--IMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQ 238
|
....*
gi 24850123 1475 LRNQP 1479
Cdd:PRK10619 239 LFGNP 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
622-805 |
1.34e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 65.84 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhRLCGwVAVSELSKG----------------FGLatqepwIQC 678
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILggldrptSGEV-LIDG-QDISSLSERelarlrrrhigfvfqfFNL------LPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 679 ATIRDNILF-------GKTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:COG1136 101 LTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 752 DPLAAVDADVANHllhrcILGVL------SHTTRLLCTHRTEYLERADVVLLMEAGQLVR 805
Cdd:COG1136 170 EPTGNLDSKTGEE-----VLELLrelnreLGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1270-1479 |
1.64e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.94 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1270 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLelAELRSQLAVIPQEPFLFSG-TIRE 1348
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NLdPQGLHEDRA--------LWQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:PRK11607 111 NI-AFGLKQDKLpkaeiasrVNEMLGLVHMQEFA----------KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1421 VDQKTDQLLQQT---ICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK11607 180 LDKKLRDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
621-813 |
1.65e-11 |
|
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: 65.68 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELSK---------------GFGLATQEpwiqca 679
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCING-LERptsgsvLVDGTDLTLLSGkelrkarrrigmifqHFNLLSSR------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 680 TIRDNILF-------GKTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDD 752
Cdd:cd03258 98 TVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 753 PLAAVDADVANH---LLHR--CILGVlshtTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03258 167 ATSALDPETTQSilaLLRDinRELGL----TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1272-1474 |
1.92e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.20 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQLElAELRsQLAVIPQEPFLFSG-TIR 1347
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALP-AEQR-RIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLD---PQGLHedRALWQALEQCHLSEVavamgGLDGeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 1423
Cdd:COG4136 95 ENLAfalPPTIG--RAQRRARVEQALEEA-----GLAG-FADRDpATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1424 K-TDQLLQQtickrfanktVLTIAHRLN--TILNS-DRVLVLQAGRVVELDSPSA 1474
Cdd:COG4136 167 AlRAQFREF----------VFEQIRQRGipALLVThDEEDAPAAGRVLDLGNWQH 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1272-1431 |
1.95e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.82 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLD 1351
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1352 -PQGLHEDRALWQALEQCHLSEVAVAMGGldgelgergqNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQ 1430
Cdd:cd03231 96 fWHADHSDEQVEEALARVGLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
.
gi 24850123 1431 Q 1431
Cdd:cd03231 166 E 166
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
621-813 |
2.25e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQCA-TIRDNILFGK 689
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsarAASRRVASVPQDTSLSFEfDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 TfdaqLYREVLEACALNDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKALYLLDDPLAAVDadvANHL 765
Cdd:PRK09536 103 T----PHRSRFDTWTETDRAAVERAMERTGVaqfADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD---INHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 766 LHrcilgVLSHTTRLLCTHRTEY-----LERA----DVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK09536 176 VR-----TLELVRRLVDDGKTAVaaihdLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1270-1478 |
3.26e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1270 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAVI------------PQ 1337
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIGVVfgqrsqlwwdlpAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1338 EPFLFSGTI--------RENLDpqglhedralwqaleqcHLSEvavaMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 1409
Cdd:COG4586 115 DSFRLLKAIyripdaeyKKRLD-----------------ELVE----LLDLGELLDTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1410 KILCIDEATASVD----QKTDQLLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:COG4586 174 KILFLDEPTIGLDvvskEAIREFLKE-YNRER-GTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1272-1479 |
3.67e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ-LAVIPQEPFLFSG-TI 1346
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1347 RENLdpqglhEDRALWQALEQCHLSEVAVAMGGLDGeLGER-----GQnLSLGQRQLLCLARALLTDAKILCIDEATASV 1421
Cdd:PRK10535 104 AQNV------EVPAVYAGLERKQRLLRAQELLQRLG-LEDRveyqpSQ-LSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1422 DQKTdqllqqtickrfaNKTVLTIAHRLN------TILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK10535 176 DSHS-------------GEEVMAILHQLRdrghtvIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1272-1479 |
4.44e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.77 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNV--DTS------QLELAELRSQLAVIPQEPFLFS 1343
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTArslsqqKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 G-TIRENLDPQGL---HEDRALWQALEQCHLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:PRK11264 99 HrTVLENIIEGPVivkGEPKEEATARARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1420 SVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK11264 174 ALDPELVGEVLNTI-RQLAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1272-1476 |
5.41e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.74 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPG-----EKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTS-QLELAELRSQLAVipqEPFLFSGT 1345
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTV---RDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IRENLDPQglhedralWQaleqchlSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKt 1425
Cdd:cd03237 87 KDFYTHPY--------FK-------TEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1426 DQLLQQTICKRFA---NKTVLTIAHRLNTI-LNSDRVLVL--QAGRVVELDSPSALR 1476
Cdd:cd03237 150 QRLMASKVIRRFAennEKTAFVVEHDIIMIdYLADRLIVFegEPSVNGVANPPQSLR 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1254-1472 |
5.78e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.64 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1254 SVEFQDVVLVYRPGLPN---ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL------DNVDTSQLE 1324
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1325 LA----------ELRSQLAVIPQEP--FLFSGTIRENLdpqgLHEDRALWQALEQCH-LSEVAVAMGGLDGELGERGQ-N 1390
Cdd:PRK13631 101 TNpyskkiknfkELRRRVSMVFQFPeyQLFKDTIEKDI----MFGPVALGVKKSEAKkLAKFYLNKMGLDDSYLERSPfG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1391 LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1468
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEvADEVIVMDKGKILK 256
|
....
gi 24850123 1469 LDSP 1472
Cdd:PRK13631 257 TGTP 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1255-1467 |
8.91e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE---LRSQ 1331
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1332 LAVIPQE-PFLFSGTIREN----LDPQGLHED---RALWQALEQchlsevavaMGGLDgelgeRGQN----LSLGQRQLL 1399
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNvaipLIIAGASGDdirRRVSAALDK---------VGLLD-----KAKNfpiqLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1400 CLARALLTDAKILCIDEATASVDQKtdqlLQQTICKRFA--NK---TVLTIAHRLNTILNSD-RVLVLQAGRVV 1467
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefNRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
622-813 |
1.12e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 63.57 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------------RLCGWVaVSELSKGFGLAT---QEPWIQCATIRDNIL 686
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfgeRRGGED-VWELRKRIGLVSpalQLRFPRDETVLDVVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FGKtFDA-QLYREVLE-----ACALNDDLSILPAGDQTeVGekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaD 760
Cdd:COG1119 103 SGF-FDSiGLYREPTDeqrerARELLELLGLAHLADRP-FG----TLSQGEQRRVLIARALVKDPELLILDEPTAGLD-L 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 761 VANHLLHRCI--LGVLSHTTRLLCTHRTEYL----ERadvVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1119 176 GARELLLALLdkLAAEGAPTLVLVTHHVEEIppgiTH---VLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
622-812 |
1.16e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 65.11 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQE-PWIQCATIRDNILFGKTFD 692
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdVSRLHardRKVGFVFQHyALFRHMTVFDNIAFGLTVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 693 AQlyREVLEACALNDDLSILPAGDQTE--VGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL----- 765
Cdd:PRK10851 103 PR--RERPNAAAIKAKVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELrrwlr 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24850123 766 -LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK10851 181 qLHEEL-----KFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1271-1478 |
1.24e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.36 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelrsqlavipqEPflFSGTIRENL 1350
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG--------------------EP--LDPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 dpqG-LHEDRAL---WQALEQchlsevAVAMGGLDG-----------------ELGERG----QNLSLGQRQLLCLARAL 1405
Cdd:COG4152 74 ---GyLPEERGLypkMKVGEQ------LVYLARLKGlskaeakrradewlerlGLGDRAnkkvEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1406 LTDAKILCIDEATASVDQKTDQLLQQTIcKRFANK--TVLTIAHRLNTI--LnSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVI-RELAAKgtTVIFSSHQMELVeeL-CDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1272-1470 |
1.29e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVdtsqlelaelrsQLAVIPQEpflfsgtiRENL 1350
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETV------------KIGYFDQH--------QEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 DPqglheDRALWQALEQchlsevaVAMGGLDGEL----------GERGQ----NLSLGQRQLLCLARALLTDAKILCIDE 1416
Cdd:COG0488 391 DP-----DKTVLDELRD-------GAPGGTEQEVrgylgrflfsGDDAFkpvgVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1417 ATASVDQKTDQLLQQTIcKRFANkTVLTIAH-R--LNTIlnSDRVLVLQAGRVVELD 1470
Cdd:COG0488 459 PTNHLDIETLEALEEAL-DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1017-1227 |
1.62e-10 |
|
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: 63.77 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1017 PVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLAnSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRE 1096
Cdd:cd18559 85 PISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMG-PLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1097 LRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQrLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIAL 1176
Cdd:cd18559 164 LKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVD-AKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAY 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1177 VQHQQglaNPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYS 1227
Cdd:cd18559 243 VSRHS---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
622-812 |
1.64e-10 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 62.97 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS--ELSKGFGLATQEPWIQCATI--------R----DNILF 687
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtDINKLKGKALRQLRRQIGMIfqqfnlieRlsvlENVLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 GKTFDAQLYR---------EVLEACALNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:cd03256 102 GRLGRRSTWRslfglfpkeEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 759 ADVANHLLHrcILGVLSHT---TRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03256 177 PASSRQVMD--LLKRINREegiTVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1272-1469 |
1.87e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA-----GRVLL--DNVDTSQLELAELRSQLAVIPQEPFLFSG 1344
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLfgRNIYSPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 -TIREN----------LDPQGLHEDRALWqALEQCHLSEvavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILC 1413
Cdd:PRK14267 100 lTIYDNvaigvklnglVKSKKELDERVEW-ALKKAALWD------EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1414 IDEATASVDQKTDQLLQQTICKRFANKTVLTIAHR-LNTILNSDRVLVLQAGRVVEL 1469
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
622-797 |
2.16e-10 |
|
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: 61.73 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSElsKGFGLATQEPWIQCA------------TIRDNILF-- 687
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG--EPIRDAREDYRRRLAylghadglkpelTVRENLRFwa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 ---GKTFDAQLYREVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANH 764
Cdd:COG4133 101 alyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 24850123 765 LLHRCIlgvLSHTTR----LLCTHRTEYLERADVVLL 797
Cdd:COG4133 169 LLAELI---AAHLARggavLLTTHQPLELAAARVLDL 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
621-760 |
2.60e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 61.73 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELH---RLCGWV--------AVSELSKGFGLATQEP-----WiqcaTIRDN 684
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVllngrrltALPAEQRRIGILFQDDllfphL----SVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFG--KTFDAQLYREVLEAcALnddlsilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:COG4136 97 LAFAlpPTIGRAQRRARVEQ-AL------------EEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
....
gi 24850123 757 VDAD 760
Cdd:COG4136 164 LDAA 167
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1272-1473 |
3.24e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.68 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN---AGRVLLDNVdtsQLELAELRSQLAVIPQ-EPFLFSGTIR 1347
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQdDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLDPQG-LHEDRALWQALEQCHLSEVAVAMGGLD------GELGeRGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:TIGR00955 118 EHLMFQAhLRMPRRVTKKEKRERVDEVLQALGLRKcantriGVPG-RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 1421 VDQKTDQLLQQTIcKRFANK--TVLTIAHRLNTIL--NSDRVLVLQAGRVVELDSPS 1473
Cdd:TIGR00955 197 LDSFMAYSVVQVL-KGLAQKgkTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSPD 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1270-1471 |
3.55e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1270 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE--PNAGRVlldnvdtsqlelaelrsqlaVIPQEPFLFSGTIR 1347
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV--------------------DVPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLDPQGLHEDRAlwQALEQCHLSEVAVamggldgeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 1427
Cdd:COG2401 104 DAIGRKGDFKDAV--ELLNAVGLSDAVL--------WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24850123 1428 LLQ---QTICKRfANKTVLTIAHRLNTI--LNSDRVLVLQAGRVVELDS 1471
Cdd:COG2401 174 RVArnlQKLARR-AGITLVVATHHYDVIddLQPDLLIFVGYGGVPEEKR 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1272-1472 |
3.95e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.00 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVdtsqlELAELRSQLAVIPQEPFLFS-GTIREN- 1349
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMFQDARLLPwKKVIDNv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 -LDPQGLHEDRALwQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1428
Cdd:PRK11247 103 gLGLKGQWRDAAL-QALAAVGLADRA----------NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1429 LQQTICKRFANK--TVLTIAHRLN-TILNSDRVLVLQAGRV-----VELDSP 1472
Cdd:PRK11247 172 MQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1271-1472 |
4.42e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.43 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRsQLAVIPQEPFLFSG-TIREN 1349
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVNTVFQSYALFPHmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 ----LDPQGLHED----RALwQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASV 1421
Cdd:PRK09452 107 vafgLRMQKTPAAeitpRVM-EALRMVQLEEFA----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1422 DQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:PRK09452 176 DYKLRKQMQNEL-KALQRKLGITfvfVTHDQEEALTmSDRIVVMRDGRIEQDGTP 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1271-1467 |
4.42e-10 |
|
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: 64.08 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRlLEPNA---GRVLLDNVDTSQLELAEL-RSQLAVIPQEPFLFSG-T 1345
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IRENL-------DPQGLHEDRALWQaleQCH--LSEVAVAMGGLDGELGERGqnlsLGQRQLLCLARALLTDAKILCIDE 1416
Cdd:TIGR02633 95 VAENIflgneitLPGGRMAYNAMYL---RAKnlLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1417 ATASVDQKTDQLLQQTIcKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:TIGR02633 168 PSSSLTEKETEILLDII-RDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
621-813 |
4.91e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 61.40 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS-----------KGFGLATQEPWI-QCATIRDNIL-- 686
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarLGIGYLPQEASIfRKLTVEENILav 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 ---FGKTFDAQlyREVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----A 759
Cdd:cd03218 100 leiRGLSKKER--EEKLEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 760 DVAN---HLLHRCIlGVL--SHTTRllcthrtEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03218 171 DIQKiikILKDRGI-GVLitDHNVR-------ETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1267-1470 |
5.41e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1267 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIP----QEPFL 1341
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 FSGTIREN--------------LDPQGlhEDRALWQALEQchlseVAVAMGGLDGELGergqNLSLGQRQLLCLARALLT 1407
Cdd:COG1129 343 LDLSIRENitlasldrlsrgglLDRRR--ERALAEEYIKR-----LRIKTPSPEQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1408 DAKILCIDEATASVD--QKTD--QLLQQtickrFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV-ELD 1470
Cdd:COG1129 412 DPKVLILDEPTRGIDvgAKAEiyRLIRE-----LAAegKAVIVISSELPELLgLSDRILVMREGRIVgELD 477
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
543-807 |
5.88e-10 |
|
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: 63.69 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 543 ALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLDLPsysPEAYYSPDPPAEPSTALELH-EAL-FSWDPigASQktfIS 620
Cdd:COG5265 303 AYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQP---PEVADAPDAPPLVVGGGEVRfENVsFGYDP--ERP---IL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 H---LQVKKGMLVGIVGKVGCGKSSL---------------------LAAITGE-LHRLCGWVAvselskgfglatQEPW 675
Cdd:COG5265 375 KgvsFEVPAGKTVAIVGPSGAGKSTLarllfrfydvtsgrilidgqdIRDVTQAsLRAAIGIVP------------QDTV 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 676 IQCATIRDNILFGKT--FDAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:COG5265 443 LFNDTIAYNIAYGRPdaSEEEV-EAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 754 LAAVDAdvanhllH--RCILGVL-----SHTTrLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:COG5265 522 TSALDS-------RteRAIQAALrevarGRTT-LVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1271-1473 |
5.91e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.67 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPNAGRVL---------------------------------L 1315
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1316 DNVDTSQLELAELRSQLAVIPQEPFLFSG--TIREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQ 1389
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAVD-------LIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1390 NLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
....*..
gi 24850123 1467 VELDSPS 1473
Cdd:TIGR03269 248 KEEGTPD 254
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
622-813 |
6.23e-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: 61.20 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS---KGFGLATQE----PWIqcaTIRDNILFG 688
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKpdsgkiLLNG-KDITNLPpekRDISYVPQNyalfPHM---TVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ----KTFDAQLYREVLEacaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:cd03299 96 lkkrKVDKKEIERKVLE---IAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24850123 765 LlhRCILGVLSH---TTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03299 168 L--REELKKIRKefgVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
621-813 |
6.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-----------ELSKGFGLATQEPWIQCA--TIRDNILF 687
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklqGIRKLVGIVFQNPETQFVgrTVEEDLAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 GKTFDAQLYREVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLH 767
Cdd:PRK13644 102 GPENLCLPPIEIRKRV----DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24850123 768 RCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13644 178 RIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1273-1461 |
7.15e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1273 DGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAVI-----------PQEPFL 1341
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLghqpgikteltALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 FSGTIRENLDpqglheDRALWQALEQCHLS---EVAVAmggldgelgergqNLSLGQRQLLCLARALLTDAKILCIDEAT 1418
Cdd:PRK13538 97 FYQRLHGPGD------DEALWEALAQVGLAgfeDVPVR-------------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24850123 1419 ASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVL 1461
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGgmVILTTHQDLPVASDKVRKLRL 202
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
622-818 |
8.05e-10 |
|
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: 60.76 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCG--WVA---VSELS--------KGFGLATQepwiQCA-----TIRD 683
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGeiLVDgqdITGLSekelyelrRRIGMLFQ----GGAlfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NILFG----KTFDAQLYRE----VLEACALNDDLSILPAgdqtevgEkgvtLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:COG1127 102 NVAFPlrehTDLSEAEIRElvleKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 756 AVD---ADVANHLLHRC--ILGvlshTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL----PLVQA 818
Cdd:COG1127 171 GLDpitSAVIDELIRELrdELG----LTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLasddPWVRQ 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
622-812 |
8.27e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.55 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSL------LAAIT-GELHrLCGWVaVSELskgfglatqEPWIQ-CA------------TI 681
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLlrmvagLERITsGEIW-IGGRV-VNEL---------EPADRdIAmvfqnyalyphmSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 682 RDNILFG----KTFDAQLYREVLEACALnddLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK11650 94 RENMAYGlkirGMPKAEIEERVAEAARI---LELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 758 DADVANHL------LHRCiLGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11650 166 DAKLRVQMrleiqrLHRR-LK----TTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
595-813 |
8.37e-10 |
|
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: 61.51 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 595 PSTALELHEALFSWDPIGASQKTFIS----HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELSK 665
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILKKTGQTVGvndvSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 666 G----------------FGLATQEpwiqcaTIRDNILFG-------KTFDAQLYREVLEACALNDDLSILPagDQtevge 722
Cdd:cd03294 94 KelrelrrkkismvfqsFALLPHR------TVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP--DE----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 723 kgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVANHLLHrciLGVLSHTTRLLCTHR-TEYLERADVVLL 797
Cdd:cd03294 161 ----LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLR---LQAELQKTIVFITHDlDEALRLGDRIAI 233
|
250
....*....|....*.
gi 24850123 798 MEAGQLVRTGPPSEIL 813
Cdd:cd03294 234 MKDGRLVQVGTPEEIL 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1266-1468 |
9.13e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1266 PGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQLAVIPQEPFLfs 1343
Cdd:PRK11248 12 GGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAERGVVFQNEGLLPWRNVQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 GTIRENLDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 1423
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQ-------MLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 1424 KTDQLLQQTICKRFAN--KTVLTIAHRLNTILNSDRVLVLQA---GRVVE 1468
Cdd:PRK11248 162 FTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSpgpGRVVE 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
622-813 |
1.08e-09 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 60.78 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQE----PWIqcaTIRDNI-- 685
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgedireqdpVELRRKIGYVIQQiglfPHM---TVEENIal 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 686 ---LFGKTfDAQLYREVLEACALNDdlsiLPagDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03295 99 vpkLLKWP-KEKIRERADELLALVG----LD--PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 763 NHL------LHRcilgvLSHTTRLLCTHRT-EYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03295 172 DQLqeefkrLQQ-----ELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
621-812 |
1.11e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.19 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE--------------LSKGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkknkklkpLRKKVGIVFQFPEHQLfeETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFG-KTF-----DA-QLYREVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK13634 107 ICFGpMNFgvseeDAkQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 758 DADVANHL------LHRcilgvLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13634 177 DPKGRKEMmemfykLHK-----EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
622-813 |
1.35e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE-----------LSKGFGLATQEPWI-QCATIRDNILFGK 689
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplharARRGIGYLPQEASIfRRLSVYDNLMAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 TFDAQLYREVLE--ACALNDDLSILPAGDQTevgekGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD-------AD 760
Cdd:PRK10895 104 QIRDDLSAEQREdrANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvidiKR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 761 VANHLLHRCiLGVL--SHTTRllctHRTEYLERADVVllmEAGQLVRTGPPSEIL 813
Cdd:PRK10895 179 IIEHLRDSG-LGVLitDHNVR----ETLAVCERAYIV---SQGHLIAHGTPTEIL 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1271-1478 |
1.45e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQ-LAVIPQEPF---LFSG-T 1345
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLgrgLVPDmS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IRENL------DPQ---GLHEDRALWQALEQCHLSEVAVAMGGLDGELGergqNLSLGQRQLLCLARALLTDAKILCIDE 1416
Cdd:COG3845 353 VAENLilgryrRPPfsrGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1417 ATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV-ELDSPSALRNQ 1478
Cdd:COG3845 429 PTRGLDVGaIEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREE 493
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
622-813 |
1.59e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.13 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSL---LAAIT----GELHRLCG--WVAVSELS-KGFGLATqePWIqcatirdNILFgKTF 691
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLskiIAGVLeptsGEVNVRVGdeWVDMTKPGpDGRGRAK--RYI-------GILH-QEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 692 DAQLYREVLE------ACALNDDLSILPA-------GDQTEVGEKGV-----TLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:TIGR03269 375 DLYPHRTVLDnlteaiGLELPDELARMKAvitlkmvGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 754 LAAVD----ADVANHLLH-RCILGvlshTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:TIGR03269 455 TGTMDpitkVDVTHSILKaREEME----QTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1272-1468 |
1.60e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.08 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVL--FRLLEPNAGRVLLDNVDTSQLELAElRSQLAVI--PQEPFLFSGTIR 1347
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENLdpqglhedralwqaleqchLSEVAVamgGLDGelGERGQNLSLgqrQLLCLaralltDAKILCIDEATASVDQKTDQ 1427
Cdd:cd03217 95 ADF-------------------LRYVNE---GFSG--GEKKRNEIL---QLLLL------EPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24850123 1428 LLQQTICK-RFANKTVLTIAHRLNtILN---SDRVLVLQAGRVVE 1468
Cdd:cd03217 142 LVAEVINKlREEGKSVLIITHYQR-LLDyikPDRVHVLYDGRIVK 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
622-811 |
1.63e-09 |
|
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: 59.75 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITG--------------ELHRL------------CGWVAVSelskgFGLatqepw 675
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGldrptsgtvrlagqDLFALdedararlrarhVGFVFQS-----FQL------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 676 IQCATIRDNI-----LFGKTFDAQLYREVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALYLL 750
Cdd:COG4181 102 LPTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 751 DDPLAAVDADVANHllhrcILGVL------SHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSE 811
Cdd:COG4181 171 DEPTGNLDAATGEQ-----IIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
599-813 |
1.69e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.49 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 599 LELHEALFSWDPIGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFG 668
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgelltaenvwNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 669 LATQEPWIQC--ATIRDNILFGKTFDAQLYREVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKA 746
Cdd:PRK13642 85 MVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 747 LYLLDDPLAAVDADVANHLLhRCILGVLS--HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIM-RVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1255-1479 |
1.70e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1255 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD--NVDTSQLELAELRSQL 1332
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1333 AVIPQEPFLFSG-TIREN-----LDPQGLHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALL 1406
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENvmfgpLRVRGASKEEAEKQAREL--LAKV-----GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1407 TDAKILCIDEATASVDQktdQLLQQ--TICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK09493 153 VKPKLMLFDEPTSALDP---ELRHEvlKVMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1215-1466 |
1.95e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1215 AMMVSVERLEEYscdvPQEPHsqplqsphqqriswlTQGSVEFQ-DVVLVYRPGLPNA--LDGVTFRVEPGEKLGIVGRT 1291
Cdd:PRK13549 237 TMMVGRELTALY----PREPH---------------TIGEVILEvRNLTAWDPVNPHIkrVDDVSFSLRRGEILGIAGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1292 GSGKSSLFLVLFRLLE-PNAGRVLLDN--VDTSQLELA---------ELRSQLAVIPQ------------EPFLFSGTIR 1347
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQAiaqgiamvpEDRKRDGIVPVmgvgknitlaalDRFTGGSRID 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 ENldpqglHEDRALWQALEQCHL----SEVAVAmggldgelgergqNLSLGQRQLLCLARALLTDAKILCIDEATASVD- 1422
Cdd:PRK13549 378 DA------AELKTILESIQRLKVktasPELAIA-------------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDv 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1423 -------QKTDQLLQQTICkrfanktVLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:PRK13549 439 gakyeiyKLINQLVQQGVA-------IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
616-812 |
2.06e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.12 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 616 KTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELHrLCGwVAVSELSkgfglATQEP----WIQCA--- 679
Cdd:PRK09452 27 KEVISNldLTINNGEFLTLLGPSGCGKTTVLRLIagfetpdSGRIM-LDG-QDITHVP-----AENRHvntvFQSYAlfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 680 --TIRDNILFG----KTFDAQLYREVLEACALN--DDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:PRK09452 100 hmTVFENVAFGlrmqKTPAAEITPRVMEALRMVqlEEFA----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 752 DPLAAVDA----DVANHL--LHRcILGVlshtTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK09452 170 ESLSALDYklrkQMQNELkaLQR-KLGI----TFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
622-813 |
2.31e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.38 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQEPwiqcA-----------------TIRDN 684
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI----LWNGQDLTALPP----AerpvsmlfqennlfphlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFG-------KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:COG3840 92 IGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 758 D-------ADVANHLLHRcilgvlSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG3840 161 DpalrqemLDLVDELCRE------RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1272-1480 |
2.46e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA-----GRVLL--DNVDTSQLELAELRSQLAVIPQEPFLFSG 1344
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfnQNIYERRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 TIRENL---------DPQgLHEDRALWQALEQCHLSEvavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 1415
Cdd:PRK14258 103 SVYDNVaygvkivgwRPK-LEIDDIVESALKDADLWD------EIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1416 EATASVD----QKTDQLLQQTICKrfANKTVLTIAHRLNTILN-SDRVLVLQA-----GRVVELDSPSALRNQPH 1480
Cdd:PRK14258 176 EPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
625-812 |
2.92e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 625 KKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV--------------------------SELSKGFGLATQEPWIQC 678
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpyskkiknfKELRRRVSMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 679 --ATIRDNILFG-------KTFDAQLYREVLEACALNDD-LSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALY 748
Cdd:PRK13631 130 fkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 749 LLDDPLAAVDADvANHLLHRCILGV-LSHTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13631 199 IFDEPTAGLDPK-GEHEMMQLILDAkANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1276-1448 |
3.18e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.69 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1276 TFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelRSQLAVIPQEPFLFSGTIREN-LDPQG 1354
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQiIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1355 LHE-------DRALWQALEQCHLSEVAVAMGGLDGeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 1427
Cdd:TIGR00954 541 SEDmkrrglsDKDLEQILDNVQLTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|.
gi 24850123 1428 LLQQtICKRFaNKTVLTIAHR 1448
Cdd:TIGR00954 620 YMYR-LCREF-GITLFSVSHR 638
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1275-1466 |
3.73e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1275 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIP---QEPFLF-SGTIREN 1349
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYlDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 LDPQgLHEDRALWQ--ALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 1427
Cdd:PRK15439 362 VCAL-THNRRGFWIkpARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24850123 1428 LLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:PRK15439 441 DIYQLI-RSIAaqNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1270-1468 |
3.73e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.64 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1270 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFLFSGTI 1346
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1347 --RENLDPQGLHEDRALWQALEQchlsevAVAMGGLDGeLGER----GQNLSLGQRQLLCLARALLTDAKILCIDEATAS 1420
Cdd:PRK10584 104 naLENVELPALLRGESSRQSRNG------AKALLEQLG-LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1421 VDQKT-DQL--LQQTICKRFANkTVLTIAHRLNTILNSDRVLVLQAGRVVE 1468
Cdd:PRK10584 177 LDRQTgDKIadLLFSLNREHGT-TLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
622-812 |
4.21e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSEL---SKGFGLATQE----PWIQCAtirDNILF 687
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIagleditSGDL--FIGEKRMNDVppaERGVGMVFQSyalyPHLSVA---ENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 G----KTFDAQLYREVLEACAlnddlsILPAGDQTEVGEKgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:PRK11000 99 GlklaGAKKEEINQRVNQVAE------VLQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 764 HL------LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11000 171 QMrieisrLHKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1275-1467 |
4.23e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1275 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRVLLDNVDTSQLELAEL---RSQLAviPQEPFLFSGTIRENLD 1351
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1352 ---PQGLHEDRAlwqaleQCHLSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLT-------DAKILCIDEATASV 1421
Cdd:PRK03695 92 lhqPDKTRTEAV------ASALNEVAEAL-GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 1422 D--QKT--DQLLQQtICKrfANKTVLTIAHRLN-TILNSDRVLVLQAGRVV 1467
Cdd:PRK03695 165 DvaQQAalDRLLSE-LCQ--QGIAVVMSSHDLNhTLRHADRVWLLKQGKLL 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
621-810 |
4.47e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELHRLCGWVAVselskgfgLATQEPWIQCATIRDNILFGKT--- 690
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIaglwpygSGRIARPAGARVL--------FLPQRPYLPLGTLREALLYPATaea 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 691 FDAQLYREVLEACALnDDLsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcI 770
Cdd:COG4178 455 FSDAELREALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-L 528
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24850123 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPS 810
Cdd:COG4178 529 REELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1271-1475 |
5.13e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVePGEKL--------------GIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIP 1336
Cdd:PRK10575 13 ALRNVSFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1337 QE-PFLFSGTIREnLDPQGlhedRALWQ-AL-----EQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 1409
Cdd:PRK10575 92 QQlPAAEGMTVRE-LVAIG----RYPWHgALgrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 1410 KILCIDEATASVD--QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 1475
Cdd:PRK10575 167 RCLLLDEPTSALDiaHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
622-798 |
6.05e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 57.24 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSeLSKGFGLATQ---EPWIQCATIRDNILFGKTFDAQLYR- 697
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-GGARVAYVPQrseVPDSLPLTVRDLVAMGRWARRGLWRr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 698 ----------EVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLlh 767
Cdd:NF040873 92 ltrddraavdDALERVGL-ADLAGRQLG----------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI-- 158
|
170 180 190
....*....|....*....|....*....|...
gi 24850123 768 RCILGVLSHTTR--LLCTHRTEYLERADVVLLM 798
Cdd:NF040873 159 IALLAEEHARGAtvVVVTHDLELVRRADPCVLL 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
622-812 |
7.02e-09 |
|
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: 57.90 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelskGFGLATQEPWIQ-----CAtiRDNILFGK------- 689
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN----GYSIRTDRKAARqslgyCP--QFDALFDEltvrehl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 TFDAQLYREVLEACALNDDLsILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHR 768
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVEL-LLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-ASRRAIWD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24850123 769 CILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03263 175 LILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1271-1478 |
8.87e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL--DNVDTSQLELaelRSQLAVIPQEpflFS--G-- 1344
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgQPVDAGDIAT---RRRVGYMSQA---FSlyGel 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 TIRENLDpqgLH-------EDRA---LWQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCI 1414
Cdd:NF033858 355 TVRQNLE---LHarlfhlpAAEIaarVAEMLERFDLADVA----------DALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1415 DEATASVD-QKTDQLLQQTIckRFANKTVLTI---AHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 1478
Cdd:NF033858 422 DEPTSGVDpVARDMFWRLLI--ELSREDGVTIfisTHFMNEAERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
622-812 |
9.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.52 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV------------SELSKGFGLATQEPWIQC--ATIRDNILF 687
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkkvklSDIRKKVGLVFQYPEYQLfeETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 GKT----FDAQLYREVLEACALnddlsilpAG-DQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-- 759
Cdd:PRK13637 108 GPInlglSEEEIENRVKRAMNI--------VGlDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkg 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 760 --DVANHL--LHRcilgvLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13637 180 rdEILNKIkeLHK-----EYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1253-1472 |
9.76e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1253 GSVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQ-----LE 1324
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1325 LAELRSQLAVIPQEP--FLFSGTIRENL--DPQGLHEDRAlwQALEQchLSEVaVAMGGLDGELGERGQ-NLSLGQRQLL 1399
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKK--VPEL-LKLVQLPEDYVKRSPfELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1400 CLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
622-812 |
1.05e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGE----------LHRL-----CGWVAVSELSK------GFGLATQEP--WIQC 678
Cdd:TIGR03269 21 FTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriIYHValcekCGYVERPSKVGepcpvcGGTLEPEEVdfWNLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 679 ATIRDN------ILFGKTFdaQLYRE--VLEAC--ALND-----DLSILPAGD---QTEVGEK----GVTLSGGQRARIA 736
Cdd:TIGR03269 101 DKLRRRirkriaIMLQRTF--ALYGDdtVLDNVleALEEigyegKEAVGRAVDlieMVQLSHRithiARDLSGGEKQRVV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 737 LARAVYQEKALYLLDDPLAAVDADVANhLLHRCIL-GVL-SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:TIGR03269 179 LARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEeAVKaSGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
622-807 |
1.08e-08 |
|
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: 57.16 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH-------RLCGWVAVSELSKGFGLAtqepwiqcATIRDNILFG------ 688
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgtvtVRGRVSSLLGLGGGFNPE--------LTGRENIYLNgrllgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 -KTFDAQLYREVLEACALNDDLSiLPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-------D 760
Cdd:cd03220 115 sRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAafqekcqR 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24850123 761 VANHLLHRC-ILGVLSH---TTRLLCthrteyleraDVVLLMEAGQLVRTG 807
Cdd:cd03220 184 RLRELLKQGkTVILVSHdpsSIKRLC----------DRALVLEKGKIRFDG 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
622-813 |
1.17e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGEL-----HRLCGWVAVSELSKGFGLATQE----PWIqcaTIRDNI 685
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglKVNDPKVDERLIRQEAGMVFQQfylfPHL---TALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 686 LFG-------KTFDA-QLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK09493 99 MFGplrvrgaSKEEAeKQARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 758 DADvanhLLHRcILGVLSH-----TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK09493 168 DPE----LRHE-VLKVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
622-765 |
1.32e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselSKGFGLA--TQEPWI-QCATIRDNILFGKTFDAQL--- 695
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---PKGLRIGylPQEPPLdDDLTVLDTVLDGDAELRALeae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 696 YREVLEACALNDDLSILPAGDQTEVGEKGV--------------------------TLSGGQRARIALARAVYQEKALYL 749
Cdd:COG0488 96 LEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLLL 175
|
170
....*....|....*.
gi 24850123 750 LDDPlaavdadvANHL 765
Cdd:COG0488 176 LDEP--------TNHL 183
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1272-1465 |
1.35e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.15 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTsqlelaelrsqLAVIPQepflfsgtirenld 1351
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1352 pqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ 1431
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|....*..
gi 24850123 1432 TIcKRFaNKTVLTIAH-R--LNTIlnSDRVLVLQAGR 1465
Cdd:cd03221 112 AL-KEY-PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1215-1466 |
1.39e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.07 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1215 AMMVSVERLEEYscdvPQEPHsqplqsphqqriswltqgsvEFQDVVL------VYRPGLPNA--LDGVTFRVEPGEKLG 1286
Cdd:TIGR02633 235 TMMVGREITSLY----PHEPH--------------------EIGDVILearnltCWDVINPHRkrVDDVSFSLRRGEILG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1287 IVGRTGSGKSSLFLVLFRLLEPN-AGRVLLDN--VDTSQLELAeLRSQLAVIPQE-------PFLFSG-----------T 1345
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-IRAGIAMVPEDrkrhgivPILGVGknitlsvlksfC 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1346 IRENLDPQGlhEDRALWQALEQCHLSEVA--VAMGGLDGelgergqnlslGQRQLLCLARALLTDAKILCIDEATASVD- 1422
Cdd:TIGR02633 370 FKMRIDAAA--ELQIIGSAIQRLKVKTASpfLPIGRLSG-----------GNQQKAVLAKMLLTNPRVLILDEPTRGVDv 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24850123 1423 -------QKTDQLLQQTIckrfankTVLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:TIGR02633 437 gakyeiyKLINQLAQEGV-------AIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
622-811 |
1.47e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 56.98 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKG--------FGLATQEPW-IQCATIRDNIL 686
Cdd:COG2884 23 LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERptsgqvLVNG-QDLSRLKRReipylrrrIGVVFQDFRlLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 F-----GKTfDAQLYREVLEACALnddlsilpagdqteVG--EKG----VTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:COG2884 102 LplrvtGKS-RKEIRRRVREVLDL--------------VGlsDKAkalpHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 756 AVDADVAN---HLLHR-CILGvlshTTRLLCTHRTEYLERADV-VLLMEAGQLVRTGPPSE 811
Cdd:COG2884 167 NLDPETSWeimELLEEiNRRG----TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1266-1470 |
1.62e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1266 PGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVL--------FrllepnAGRVLLDNvdtsqlELAELRS------- 1330
Cdd:NF040905 12 PGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsY------EGEILFDG------EVCRFKDirdseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1331 QLAVIPQE----PFLfsgTIRENL---DPQG----LHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQLL 1399
Cdd:NF040905 79 GIVIIHQElaliPYL---SIAENIflgNERAkrgvIDWNETNRRAREL--LAKV-----GLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 1400 CLARALLTDAKILCIDEATASV-DQKTDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVE-LD 1470
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALnEEDSAALLD--LLLELKAQgiTSIIISHKLNEIRRvADSITVLRDGRTIEtLD 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1271-1466 |
1.94e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE----PNAGRVLLDNVDTSQLELA----ELRSQLAVIPQEPFLF 1342
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTVQREGRLArdirKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1343 SG-TIREN-----LDPQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDE 1416
Cdd:PRK09984 99 NRlSVLENvligaLGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1417 ATASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRV 1466
Cdd:PRK09984 179 PIASLDPESARIVMDTL--RDINQndgiTVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1266-1467 |
2.10e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1266 PGLpNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD----NVDTSQlelAELRSQLAVIPQEPFL 1341
Cdd:PRK10982 9 PGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeiDFKSSK---EALENGISMVHQELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 F-SGTIRENL------------DPQGLHED-RALWQALeqchlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLT 1407
Cdd:PRK10982 85 VlQRSVMDNMwlgryptkgmfvDQDKMYRDtKAIFDEL-------------DIDIDPRAKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 1408 DAKILCIDEATASVDQK-TDQLLqqTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKeVNHLF--TIIRKLKERgcGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
622-819 |
2.40e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS-----------KGFGLATQEPWIQ-CATI-RDNILFG 688
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirNKAGMVFQNPDNQiVATIvEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 KtfdaqlyrevleacalnDDLSILPAGDQTEVGE--KGVT-----------LSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:PRK13633 111 P-----------------ENLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 756 AVDA----DVANHLLHrciLGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAV 819
Cdd:PRK13633 174 MLDPsgrrEVVNTIKE---LNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMM 238
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
612-807 |
2.44e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 612 GASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---------RLCGWVAVSELSKGFGLATQE-- 673
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiagnhfdfsKTPSDKAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 674 --PWIqcaTIRDNIL--------FGKTFDAQLYREVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQ 743
Cdd:PRK11124 93 lwPHL---TVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 744 EKALYLLDDPLAAVDADVANHLLHrcILGVLSHT--TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
622-759 |
2.50e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.79 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWIqcaTIRDNILFGKTF 691
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLApssgeiTLDG-VPVTGPGADRGVVFQKdallPWL---NVLDNVAFGLRL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 692 D----AQLYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:COG4525 104 RgvpkAERRARAEELLAL--------------VGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
622-813 |
2.84e-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: 56.29 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSK-GFGLATQEPWI-QCATIRDNILFG 688
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptsgsvlfdgEDITGL-PPHEIARlGIGRTFQIPRLfPELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 KTFDAQLY-----------------REVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:cd03219 100 AQARTGSGlllararreereareraEELLERVGL-ADLADRPAG----------ELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 752 DPLAAVDADVANHLLHRcILGV-LSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03219 169 EPAAGLNPEETEELAEL-IRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1271-1480 |
3.36e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.22 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN----AGRVLLDNVDTSQLELAELR----SQLAVIPQEPflf 1342
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRkiigREIAMIFQEP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1343 sgtiRENLDP-----QGLHE------------DRALW---QALEQCHlsEVAV-----AMGGLDGELGErgqnlslGQRQ 1397
Cdd:COG4170 99 ----SSCLDPsakigDQLIEaipswtfkgkwwQRFKWrkkRAIELLH--RVGIkdhkdIMNSYPHELTE-------GECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1398 LLCLARALLTDAKILCIDEATASVDQKTD----QLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQaqifRLLARL--NQLQGTSILLISHDLESISQwADTITVLYCGQTVESGPT 243
|
....*...
gi 24850123 1473 SALRNQPH 1480
Cdd:COG4170 244 EQILKSPH 251
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
621-815 |
3.40e-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: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITG-------ELHRLCGWVAVSELS------KGFGLATQEPW-IQCATIRDnil 686
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyevtEGEILFKGEDITDLPpeerarLGIFLAFQYPPeIPGVKNAD--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 fgktfdaqLYREVleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD-------A 759
Cdd:cd03217 97 --------FLRYV------------------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalrlvA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 760 DVANHLL--HRCILgVLSHTTRLLcthrtEYLeRADVVLLMEAGQLVRTGPPSEILPL 815
Cdd:cd03217 145 EVINKLReeGKSVL-IITHYQRLL-----DYI-KPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
616-762 |
3.76e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.17 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 616 KTFISH-------LQVKKGMLVGIVGKVGCGKSSLLAAITG--------ELH------------RLCGWVAVSELSKGFg 668
Cdd:PRK09984 12 KTFNQHqalhavdLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHiellgrtvqregRLARDIRKSRANTGY- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 669 LATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAgdQTEVG------EKGVTLSGGQRARIALARAVY 742
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALM 168
|
170 180
....*....|....*....|
gi 24850123 743 QEKALYLLDDPLAAVDADVA 762
Cdd:PRK09984 169 QQAKVILADEPIASLDPESA 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1281-1472 |
4.75e-08 |
|
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: 53.92 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1281 PGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGtirenldpqglhedra 1360
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1361 lwqaleqchlsevavamggldgelgergqnlsLGQRQLlcLARALLTDAKILCIDEATASVDQKTDQLLQQTIC------ 1434
Cdd:smart00382 65 --------------------------------LRLRLA--LALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 24850123 1435 -KRFANKTVLTIAHRLNTILnsDRVLVLQAGRVVELDSP 1472
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
621-813 |
5.17e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCG--WVA-------------VSELSKGFGLATQepwiqcATIRDNI 685
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGslTLNgqdhtttppsrrpVSMLFQENNLFSH------LTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 686 LFG-----KTFDAQlyREVLEACA----LNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:PRK10771 93 GLGlnpglKLNAAQ--REKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 757 VDADVANHllhrcILGVLS------HTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10771 160 LDPALRQE-----MLTLVSqvcqerQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
615-813 |
5.21e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.93 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 615 QKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCG-----WvAVSELSKGFGLATQE-----PWi 676
Cdd:PRK13548 14 GRTLLDDvsLTLRPGEVVAILGPNGAGKSTLLRALSGELSpdsgevRLNGrpladW-SPAELARRRAVLPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 677 qcaTIRDNILFG-------KTFDAQLYREVLEACALnDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQ------ 743
Cdd:PRK13548 92 ---TVEEVVAMGraphglsRAEDDALVAAALAQVDL-AHLA----------GRDYPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 744 EKALYLLDDPLAAVD-------ADVANHLLHRCILGVLS--H----TTRllcthrteYlerADVVLLMEAGQLVRTGPPS 810
Cdd:PRK13548 158 PPRWLLLDEPTSALDlahqhhvLRLARQLAHERGLAVIVvlHdlnlAAR--------Y---ADRIVLLHQGRLVADGTPA 226
|
...
gi 24850123 811 EIL 813
Cdd:PRK13548 227 EVL 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
621-765 |
5.93e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 53.22 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKgFGLATQepwiqcatirdnilfgktfdaqlyrevl 700
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-IGYFEQ---------------------------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 701 eacalnddlsilpagdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLaavdadvaNHL 765
Cdd:cd03221 71 --------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT--------NHL 101
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
623-789 |
6.30e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 623 QVKKGMLVGIVGKVGCGKSSLLAaITGELHRLCGWV-AVSELSKGFGLAtQEPWIQCATIRDNILFGKTFDAQLYR---- 697
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRlTKPAKGKLFYVP-QRPYMTLGTLRDQIIYPDSSEDMKRRglsd 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 698 EVLEACALNDDLS-ILpagdQTEVGEKGV-----TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRC-- 769
Cdd:TIGR00954 552 KDLEQILDNVQLThIL----EREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCre 627
|
170 180
....*....|....*....|...
gi 24850123 770 ---ILGVLSHTTRLLCTHrtEYL 789
Cdd:TIGR00954 628 fgiTLFSVSHRKSLWKYH--EYL 648
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-813 |
8.61e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.23 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLL------------AAITGELhRLCGWVAVS------ELSKGFGLATQEP-WIQCATIR 682
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLrtfnrllelneeARVEGEV-RLFGRNIYSpdvdpiEVRREVGMVFQYPnPFPHLTIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 683 DNILFGKTFDA---------QLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:PRK14267 104 DNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 754 LAAVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK14267 177 TANIDP-VGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1271-1466 |
9.51e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.17 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPNA---GRVLL--DNVDTSQLELAELRSQLAVIPQEPFLFS 1343
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFhgKNLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 GTIRENL-------DPQGlHEDRALWQALEQCHL-SEVavamgglDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 1415
Cdd:PRK14243 105 KSIYDNIaygarinGYKG-DMDELVERSLRQAALwDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1416 EATASVDQ----KTDQLLQQtICKRFankTVLTIAHRLNtilnsdrvlvlQAGRV 1466
Cdd:PRK14243 177 EPCSALDPistlRIEELMHE-LKEQY---TIIIVTHNMQ-----------QAARV 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1273-1479 |
9.78e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.09 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1273 DGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN----AGRVLLDNVdtsQLELAELRSQL-AVIPQEP---FLFSG 1344
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRGRKiATIMQNPrsaFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1345 TI----RENLDPQGLHEDRA-LWQALEQCHLSEVAVAMGGLDGElgergqnLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:PRK10418 97 TMhthaRETCLALGKPADDAtLTAALEAVGLENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1420 SVD----QKTDQLLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK10418 170 DLDvvaqARILDLLESIVQKR--ALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
622-812 |
9.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.14 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS--------------KGFGLATQEPWIQC--ATIRDNI 685
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirKKVGLVFQFPESQLfeETVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 686 LFG-------KTFDAQLYREVLEACALNDDLsilpagdqteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:PRK13649 108 AFGpqnfgvsQEEAEALAREKLALVGISESL----------FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 759 ADVANHL------LHRcilgvlSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13649 178 PKGRKELmtlfkkLHQ------SGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDI 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
622-819 |
1.11e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.65 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS------KGFGLATQEPWI-QCATIRDNIL--- 686
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgedITHLPmhkrarLGIGYLPQEASIfRKLTVEDNILavl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 --FGKTFDAQlyREVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----AD 760
Cdd:COG1137 104 elRKLSKKER--EERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 761 VAN---HLLHRCIlGVL--SHTTRllcthrtEYLERADVVLLMEAGQLVRTGPPSEIL--PLVQAV 819
Cdd:COG1137 175 IQKiirHLKERGI-GVLitDHNVR-------ETLGICDRAYIISEGKVLAEGTPEEILnnPLVRKV 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
623-812 |
1.16e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 623 QVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS--------------ELSKGFGLATQEPWIQC--ATIRDNIL 686
Cdd:PRK13641 29 ELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgnknlkKLRKKVSLVFQFPEAQLfeNTVLKDVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FG-KTFDAQlyrevlEACALNDDLS-ILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:PRK13641 109 FGpKNFGFS------EDEAKEKALKwLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 764 HLLHRCILGVLSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
622-790 |
1.33e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRL--CGWVAVSELskgfglatqePWIQCATIRDNILFGKTFDAQLyrEV 699
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpvAGCVDVPDN----------QFGREASLIDAIGRKGDFKDAV--EL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 700 LEACALNDDLSILpagdqTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH--- 776
Cdd:COG2401 119 LNAVGLSDAVLWL-----RRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR--NLQKLARrag 187
|
170
....*....|....
gi 24850123 777 TTRLLCTHRTEYLE 790
Cdd:COG2401 188 ITLVVATHHYDVID 201
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1265-1467 |
1.33e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1265 RPGLPNA--LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDtSQLELAELRSQLAVIPQEP 1339
Cdd:cd03233 14 GKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIP-YKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1340 FLFSG-TIRENLdpqglheDRALwqaleQCHLSEVAvamggldgelgeRGqnLSLGQRQLLCLARALLTDAKILCIDEAT 1418
Cdd:cd03233 93 VHFPTlTVRETL-------DFAL-----RCKGNEFV------------RG--ISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24850123 1419 ASVDQKTD-QLLQ--QTICKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVV 1467
Cdd:cd03233 147 RGLDSSTAlEILKciRTMADVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQI 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1277-1433 |
1.37e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1277 FRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPqepflfsgTIRENLDP-QGL 1355
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP--------GLKADLSTlENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1356 HedraLWQALEQCHLSEV---AVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQT 1432
Cdd:PRK13543 104 H----FLCGLHGRRAKQMpgsALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
.
gi 24850123 1433 I 1433
Cdd:PRK13543 180 I 180
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1252-1468 |
1.75e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1252 QGSVEFQDVVLVYRpglpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEpNAGRVLLDNVDTSQLELAEL--- 1328
Cdd:PRK11022 8 KLSVHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRIsek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1329 -RSQL-----AVIPQEP-------FLFSGTIRENLDP-QGLHEDRALWQALEQCHLsevaVAMGGLDGELGERGQNLSLG 1394
Cdd:PRK11022 82 eRRNLvgaevAMIFQDPmtslnpcYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQ----VGIPDPASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1395 QRQLLCLARALLTDAKILCIDEATASVD-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVVE 1468
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDvtiqaQIIELLLE---LQQKENMALVLITHDLALVAEAaHKIIVMYAGQVVE 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
622-812 |
1.80e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelskgfGLATQEPWIQ----C-----------ATIRDNIL 686
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID------GEDVTHRSIQqrdiCmvfqsyalfphMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FG----KTFDAQLYREVLEACALNDdlsilPAG------DQtevgekgvtLSGGQRARIALARA-VYQEKALyLLDDPLA 755
Cdd:PRK11432 101 YGlkmlGVPKEERKQRVKEALELVD-----LAGfedryvDQ---------ISGGQQQRVALARAlILKPKVL-LFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 756 AVDADvanhlLHRCI----------LGVlshtTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11432 166 NLDAN-----LRRSMrekirelqqqFNI----TSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
622-813 |
1.94e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE---------------LSKGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrLRKEIGLVFQFPEYQLfqETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFGKTFDAQLYREVLEACALNDDLSILPagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA----D 760
Cdd:PRK13645 112 IAFGPVNLGENKQEAYKKVPELLKLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 761 VANHLLHrciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13645 189 FINLFER---LNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1250-1470 |
2.06e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1250 LTQGSVEFQDVVLvyrpglpnaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLfrllepnAGRVLLD--------NVDTS 1321
Cdd:PRK11147 6 IHGAWLSFSDAPL---------LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyeqDLIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1322 QL---------------------ELAE-------LRSQLAVIPQEPFLFS-GTIRENLDPQGlhedraLWQaLEQcHLSE 1372
Cdd:PRK11147 70 RLqqdpprnvegtvydfvaegieEQAEylkryhdISHLVETDPSEKNLNElAKLQEQLDHHN------LWQ-LEN-RINE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1373 VAVAMgGLDGE--LGErgqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANKTVLtIAHrln 1450
Cdd:PRK11147 142 VLAQL-GLDPDaaLSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQGSIIF-ISH--- 211
|
250 260
....*....|....*....|.
gi 24850123 1451 tilnsDRVLVLQ-AGRVVELD 1470
Cdd:PRK11147 212 -----DRSFIRNmATRIVDLD 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
622-813 |
2.54e-07 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 53.58 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGfGLATQE-----------PWiqcaTIRDN 684
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTpssgevRLNG-RPLAAWSPW-ELARRRavlpqhsslafPF----TVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFG-------KTFDAQLYREVLEACalndDLSILPAGDQTevgekgvTLSGGQRARIALARAVYQ--------EKALyL 749
Cdd:COG4559 96 VALGraphgssAAQDRQIVREALALV----GLAHLAGRSYQ-------TLSGGEQQRVQLARVLAQlwepvdggPRWL-F 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 750 LDDPLAAVD-------ADVANHLLHR-----CILGVLSHTTRllcthrteYlerADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4559 164 LDEPTSALDlahqhavLRLARQLARRgggvvAVLHDLNLAAQ--------Y---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
632-812 |
3.07e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 632 IVGKVGCGKSSLLAAI------------TGEL----HRLCG-WVAVSELSKGFGLATQEPWIQCATIRDNILFGKTFDAQ 694
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrmndlnpevtiTGSIvyngHNIYSpRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 695 LYREVLEACALNddlSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCI 770
Cdd:PRK14239 116 KDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24850123 771 LGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK14239 192 LGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
622-818 |
3.14e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.87 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQC--ATIRDNILFGk 689
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseetvwDVRRQVGMVFQNPDNQFvgATVQDDVAFG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 tfdaqlyrevLEACALNDDLSIlPAGDQ--TEVG------EKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-- 759
Cdd:PRK13635 107 ----------LENIGVPREEMV-ERVDQalRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrg 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 760 -----DVANHLLHRCILGVLShttrllCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQA 818
Cdd:PRK13635 176 rrevlETVRQLKEQKGITVLS------ITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
622-812 |
3.50e-07 |
|
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: 52.76 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSS-------LLAAITGELHrLCGWVAVSE---LSKGFGLATQEPWIQCA-TIRDNI-LFGK 689
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRAT-VAGHDVVREpreVRRRIGIVFQDLSVDDElTGWENLyIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 TFD------AQLYREVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03265 100 LYGvpgaerRERIDELLDFVGL------------LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 763 NHLLHRCILGVLSH-TTRLLCTHrteYLERA----DVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03265 168 AHVWEYIEKLKEEFgMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1275-1472 |
4.66e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1275 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQG 1354
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1355 LHEDRALWQALEQCHLSEVAVAM--GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD--QKTDQLLQ 1430
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMqaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDisHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24850123 1431 QTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAP 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
622-758 |
6.04e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLL------------AAITGEL----HRL-CGWVAVSELSKGFGLATQEPWIQCATIRDN 684
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILrcfnrlndlipgFRVEGKVtfhgKNLyAPDVDPVEVRRRIGMVFQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFGKTFDA------QLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:PRK14243 111 IAYGARINGykgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
562-803 |
6.07e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 562 LLESKVSLDRIQRFlDLPSYSPEAyysPDPPAEPS-TALELHEALFSWDPIGASQKTFisHLQVKKGMLVGIVGKVGCGK 640
Cdd:PRK10522 289 LLSAQVAFNKLNKL-ALAPYKAEF---PRPQAFPDwQTLELRNVTFAYQDNGFSVGPI--NLTIKRGELLFLIGGNGSGK 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 641 SSLLAAITGELHRLCGWVAVSelSKGFGLATQEPWIQ--CATIRDNILFGKTFDAQlyREVLEACALNDDLSILPAGDQT 718
Cdd:PRK10522 363 STLAMLLTGLYQPQSGEILLD--GKPVTAEQPEDYRKlfSAVFTDFHLFDQLLGPE--GKPANPALVEKWLERLKMAHKL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 719 EVGEKGVT---LSGGQRARIALARAVYQEKALYLLDDplAAVDAD-VANHLLHRCILGVLSHT--TRLLCTHRTEYLERA 792
Cdd:PRK10522 439 ELEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFYQVLLPLLQEMgkTIFAISHDDHYFIHA 516
|
250
....*....|.
gi 24850123 793 DVVLLMEAGQL 803
Cdd:PRK10522 517 DRLLEMRNGQL 527
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
622-807 |
6.66e-07 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 51.98 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSE----------LSKGFGLAtqePWIqcaTIRDNI 685
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpdagfaTVDGFDVVKEpaearrrlgfVSDSTGLY---DRL---TARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 686 LFgktFdAQLY---REVLEAcALNDDLSILPAGDQTEVGEKGvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03266 100 EY---F-AGLYglkGDELTA-RLEELADRLGMEELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 763 NHLL----HRCILGvlshTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03266 173 RALRefirQLRALG----KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1271-1480 |
7.94e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN----AGRVLLDNVDTSQLELAELRS----QLAVIPQEPflf 1342
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1343 sgtiRENLDP-----------------QGLHEDRALWQ---ALEQCH---LSEVAVAMGGLDGELGErgqnlslGQRQLL 1399
Cdd:PRK15093 99 ----QSCLDPservgrqlmqnipgwtyKGRWWQRFGWRkrrAIELLHrvgIKDHKDAMRSFPYELTE-------GECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1400 CLARALLTDAKILCIDEATASVDQKTdqllQQTICKRFA------NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1472
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPS 243
|
....*...
gi 24850123 1473 SALRNQPH 1480
Cdd:PRK15093 244 KELVTTPH 251
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
622-803 |
1.08e-06 |
|
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: 50.99 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhRLCGWV------AVSELSKGFGLATQE----PWIqcaTIRDN 684
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTI-IIDGLKltddkkNINELRQKVGMVFQQfnlfPHL---TVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFGKTF-------DAQ-LYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:cd03262 97 ITLAPIKvkgmskaEAEeRALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24850123 757 VDADVANHllhrcILGVL-----SHTTRLLCTHRTEY-LERADVVLLMEAGQL 803
Cdd:cd03262 166 LDPELVGE-----VLDVMkdlaeEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
622-813 |
1.09e-06 |
|
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: 51.28 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS------KGFGLATQEPWI-QCATIRDNILFG 688
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPprsgsiRFDG-RDITGLPpherarAGIGYVPEGRRIfPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ktfdAQLYREVLEACALNDDLSILPAGDQTEvGEKGVTLSGGQRARIALARAVYQEKALYLLDDP---LA-AVDADVANH 764
Cdd:cd03224 100 ----AYARRRAKRKARLERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIVEEIFEA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 765 LLHRCILGVlshtTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03224 175 IRELRDEGV----TILLVEQNaRFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
622-791 |
1.17e-06 |
|
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: 51.25 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV-------------AVSELSKGFGLATQE-PWIQCATIRDNILF 687
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgrAIPYLRRKIGVVFQDfRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 GKTFDAQLYRE-------VLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:cd03292 102 ALEVTGVPPREirkrvpaALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 24850123 761 VANHllhrcILGVLSH-----TTRLLCTHRTEYLER 791
Cdd:cd03292 171 TTWE-----IMNLLKKinkagTTVVVATHAKELVDT 201
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
716-813 |
1.26e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.51 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 716 DQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH--TTRLLCTHRTEYLER-A 792
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEegKTMVVVTHEMGFARHvS 219
|
90 100
....*....|....*....|.
gi 24850123 793 DVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10619 220 SHVIFLHQGKIEEEGAPEQLF 240
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1272-1472 |
1.43e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLF-RLLEPNA-------GRVLLDNVDTSQLE---LAELRSQLAVIPQEPF 1340
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDaprLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1341 LFSgtIRE-NLDPQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARAL---------LTDAK 1410
Cdd:PRK13547 97 AFS--AREiVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 1411 ILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSP 1472
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVrrLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
622-813 |
1.45e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 51.29 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS--KGFGLATQEPWIQcaTIRDNILF-GKTFDAQLYRE 698
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidTARSLSQQKGLIR--QLRQHVGFvFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 699 VLE----------------ACALNDDL--SILPAGDQTEVGEKgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:PRK11264 102 VLEniiegpvivkgepkeeATARARELlaKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24850123 761 VANHLLHRCILGVLSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
624-804 |
1.87e-06 |
|
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: 50.24 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 624 VKKGMLVGIVGKVGCGKSSLLAAITGEL--HRLCGWVAVSelskgfGLATQEPWIQCATI---RDNILFGktfdaQL-YR 697
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLIN------GRPLDKRSFRKIIGyvpQDDILHP-----TLtVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 698 EVLE-ACALnddlsilpagdqtevgeKGvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH 776
Cdd:cd03213 101 ETLMfAAKL-----------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLAD 159
|
170 180 190
....*....|....*....|....*....|..
gi 24850123 777 TTR-LLCT-H--RTEYLERADVVLLMEAGQLV 804
Cdd:cd03213 160 TGRtIICSiHqpSSEIFELFDKLLLLSQGRVI 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1287-1467 |
1.91e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1287 IVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN---VDTSQ-LELAELRSQLAVIPQEPFLFSG-TIRENLDPQGLHEDRAL 1361
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1362 WQALeqchlsevaVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQ--QTICKRFa 1438
Cdd:PRK11144 109 FDKI---------VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPylERLAREI- 178
|
170 180 190
....*....|....*....|....*....|
gi 24850123 1439 NKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1467
Cdd:PRK11144 179 NIPILYVSHSLDEILRlADRVVVLEQGKVK 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1272-1461 |
2.54e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnVDTSQLELAELRSQLAVIPQEPFLFSGTIRenLD 1351
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLRIGYVPQKLYLDTTLPLTVNRFLR--LR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1352 PqGLHEDRALwQALEQCHLSEVavamggLDGELgergQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ 1431
Cdd:PRK09544 94 P-GTKKEDIL-PALKRVQAGHL------IDAPM----QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|...
gi 24850123 1432 TI--CKRFANKTVLTIAHRLNTIL-NSDRVLVL 1461
Cdd:PRK09544 162 LIdqLRRELDCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1272-1447 |
3.03e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVdtsqlelaelrsQLAVIPQEpflfsgtiRENL 1350
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KLAYVDQS--------RDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 DPqglheDRALWQaleqchlsEVAvamGGLD---------------GELGERGQ-------NLSLGQRQLLCLARALLTD 1408
Cdd:TIGR03719 398 DP-----NKTVWE--------EIS---GGLDiiklgkreipsrayvGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSG 461
|
170 180 190
....*....|....*....|....*....|....*....
gi 24850123 1409 AKILCIDEATASVDQKTDQLLQQTICKrFANkTVLTIAH 1447
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLN-FAG-CAVVISH 498
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-813 |
3.05e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLL------------AAITGELHrLCGW----VAVSELSKGFGLATQEP-WIQCATIRDN 684
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVSGEVY-LDGQdifkMDVIELRRRVQMVFQIPnPIPNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFGKTFD---------AQLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:PRK14247 103 VALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 756 AVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK14247 176 NLDP-ENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
632-812 |
3.21e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.03 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 632 IVGKVGCGKSSLLAAITGELHRLCGWVAVSE-----LSKGFGLATQEPWI----QCA------TIRDNILFG-KTFDAQL 695
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKRRIgyvfQDArlfphyKVRGNLRYGmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 696 YREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS 775
Cdd:PRK11144 109 FDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24850123 776 HTTR---LLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11144 176 REINipiLYVSHSlDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
621-769 |
3.90e-06 |
|
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: 48.69 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELHRLCGwvavselSKGFGLAtQEPWIQCATIRDNIlfgktfda 693
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgSGRIGMPEG-------EDLLFLP-QRPYLPLGTLREQL-------- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 694 qlyrevleacalnddlsILPAGDqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRC 769
Cdd:cd03223 85 -----------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-813 |
4.79e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.66 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------------ELSKGFGLATQEP-WIQCATIRDN 684
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfgkdifqidaiKLRKEVGMVFQQPnPFPHLSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFG-KTFDAQLYREVLEACalndDLSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:PRK14246 111 IAYPlKSHGIKEKREIKKIV----EECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 760 dVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK14246 187 -VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
523-804 |
5.63e-06 |
|
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: 50.95 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 523 FITYVLMGHQLTATKVFTALALVRM-LILPLNNFPWVINGLLESKVSLDRIQRF-LDLPSYSPEAYYSPDPPAEPS-TAL 599
Cdd:COG4615 249 LILFLLPALGWADPAVLSGFVLVLLfLRGPLSQLVGALPTLSRANVALRKIEELeLALAAAEPAAADAAAPPAPADfQTL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 600 ELHEALFSWDPIGASqKTF----IShLQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSElskgfgl 669
Cdd:COG4615 329 ELRGVTYRYPGEDGD-EGFtlgpID-LTIRRGELVFIVGGNGSGKSTLAKLLTG-LYRpesgeiLLDGQPVTA------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 670 ATQEPWIQ--CATIRDNILF------GKTFDAQLYREVLEACALNDDLSIlpagdqtevgEKG----VTLSGGQRARIAL 737
Cdd:COG4615 399 DNREAYRQlfSAVFSDFHLFdrllglDGEADPARARELLERLELDHKVSV----------EDGrfstTDLSQGQRKRLAL 468
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 738 ARAVYQEKALYLLDDpLAAvDADVAN-HLLHRCILGVL----------SHTTRllcthrteYLERADVVLLMEAGQLV 804
Cdd:COG4615 469 LVALLEDRPILVFDE-WAA-DQDPEFrRVFYTELLPELkargktviaiSHDDR--------YFDLADRVLKMDYGKLV 536
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
622-806 |
6.00e-06 |
|
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: 47.81 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRlcgwvavselSKGfglatqepwiqcatirdNILF-GKTFDAQLYREVL 700
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKP----------DSG-----------------EILVdGKEVSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 701 EAcalnddlsilpagdqtevgekGVT----LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVL-- 774
Cdd:cd03216 74 RA---------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLra 130
|
170 180 190
....*....|....*....|....*....|...
gi 24850123 775 SHTTRLLCTHR-TEYLERADVVLLMEAGQLVRT 806
Cdd:cd03216 131 QGVAVIFISHRlDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
630-812 |
6.61e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 630 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEP--WIQCATIRDNILFGKT---FD-- 692
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepitkeniREVRKFVGLVFQNPddQIFSPTVEQDIAFGPInlgLDee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 693 --AQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcI 770
Cdd:PRK13652 113 tvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID--F 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24850123 771 LGVLSHT---TRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13652 180 LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
622-759 |
6.86e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWiqcATIRDNILFGKTF 691
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDG-KPVEGPGAERGVVFQNegllPW---RNVQDNVAFGLQL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 692 dAQLYREVLEACALnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:PRK11248 98 -AGVEKMQRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
615-813 |
8.31e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 615 QKTFISHL--QVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELSKG---FGLATQ----EPWIqca 679
Cdd:PRK13537 19 DKLVVDGLsfHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpdagsiSLCGEPVPSRARHArqrVGVVPQfdnlDPDF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 680 TIRDNIL-FGKTF--DAQLYREVLEACAlndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:PRK13537 96 TVRENLLvFGRYFglSAAAARALVPPLL---EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 757 VDADvANHLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
622-807 |
8.59e-06 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 48.34 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLvGIVGKVGCGKSSLLAAITGELHRLCGWVAV---------SELSKGFGLATQEP-WIQCATIRD-----NIL 686
Cdd:cd03264 21 LTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpQKLRRRIGYLPQEFgVYPNFTVREfldyiAWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 687 FG---KTFDAQLyREVLEACALNDdlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVdaDVAN 763
Cdd:cd03264 100 KGipsKEVKARV-DEVLELVNLGD-----------RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL--DPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24850123 764 HLLHRCILGVLSHT-TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03264 166 RIRFRNLLSELGEDrIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
623-812 |
9.05e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.34 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 623 QVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQC--ATIRDNILFG-- 688
Cdd:PRK13650 29 HVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteenvwDIRHKIGMVFQNPDNQFvgATVEDDVAFGle 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 -KTFDAQLYRE-VLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 766
Cdd:PRK13650 109 nKGIPHEEMKErVNEALEL--------VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24850123 767 hRCILGVLS--HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13650 181 -KTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
622-759 |
9.25e-06 |
|
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: 48.26 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQEPWIQCA--------------TIRDNILF 687
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGllylghapgikttlSVLENLRF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 688 gktfdaqlyrevleACALNDDLSILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:cd03231 97 --------------WHADHSDEQVEEALAR--VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
621-784 |
9.67e-06 |
|
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: 48.12 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelSKGFGLATQEPWIQCA------------TIRDNILFG 688
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN--GTPLAEQRDEPHENILylghlpglkpelSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 KTFDAQLYREVLEACALN--DDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 766
Cdd:TIGR01189 98 AAIHGGAQRTIEDALAAVglTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170 180
....*....|....*....|..
gi 24850123 767 HRcilgVLSHTTR----LLCTH 784
Cdd:TIGR01189 168 GL----LRAHLARggivLLTTH 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1272-1465 |
1.30e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.88 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN--AGRVLLDNVDTSQlelaELRSQLAVIPQEPFLFSG-TIRE 1348
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1349 NLD-------PQGLHEDRALWQAleQCHLSEVAVAMGG--LDGELGERGqnLSLGQRQLLCLARALLTDAKILCIDEATA 1419
Cdd:PLN03211 160 TLVfcsllrlPKSLTKQEKILVA--ESVISELGLTKCEntIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24850123 1420 SVDQKTDQLLQQTICKrFAN--KTVLTIAHRLNTILNS--DRVLVLQAGR 1465
Cdd:PLN03211 236 GLDATAAYRLVLTLGS-LAQkgKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
588-813 |
1.31e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.06 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 588 SPDPPAEPSTALELHEALFSW-DPIGASQKTFishlQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV------ 660
Cdd:PRK13536 31 ASIPGSMSTVAIDLAGVSKSYgDKAVVNGLSF----TVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 661 --SELSK-GFGLATQ-EPWIQCATIRDNIL-FGKTFDAQLyREVLEACALNDDLSILPAGDQTEVGEkgvtLSGGQRARI 735
Cdd:PRK13536 107 arARLARaRIGVVPQfDNLDLEFTVRENLLvFGRYFGMST-REIEAVIPSLLEFARLESKADARVSD----LSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 736 ALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
622-810 |
1.50e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.58 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQ--CATIRDNILFG- 688
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmgrevnaeneKWVRSKVGLVFQDPDDQvfSSTVWDDVAFGp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ---KTFDAQLYREVLEAcalnddlsiLPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:PRK13647 106 vnmGLDKDEVERRVEEA---------LKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24850123 765 LlhRCILGVLSH--TTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPS 810
Cdd:PRK13647 177 L--MEILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
621-812 |
1.71e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS--------------KGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrKRIGMVFQFPESQLfeDTVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFG-KTFDAQL-------YREVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:PRK13646 107 IIFGpKNFKMNLdevknyaHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 757 VDADvANHLLHRCI--LGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13646 176 LDPQ-SKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
727-813 |
1.73e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 47.68 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 727 LSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVanhllhrciLGVL-----SHTTRLLCTH-----RteylERA 792
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvGEV---------LDVMrdlakEGMTMVVVTHemgfaR----EVA 203
|
90 100
....*....|....*....|.
gi 24850123 793 DVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1126 204 DRVVFMDGGRIVEEGPPEEFF 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
632-768 |
1.75e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 632 IVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELS-----KGFGLATQEPWIQCATIRDNILfgktFDAQLYREVLE 701
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLlfegeDISTLKpeiyrQQVSYCAQTPTLFGDTVYDNLI----FPWQIRNQQPD 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 702 ACALNDDLSI--LPagdqTEVGEKGVT-LSGGQRARIALARAV-YQEKALyLLDDPLAAVDAD---VANHLLHR 768
Cdd:PRK10247 114 PAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLqFMPKVL-LLDEITSALDESnkhNVNEIIHR 182
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
598-813 |
2.08e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 598 ALELHEALFSWDpigaSQKTFIS-HLQVKKGMLVGIVGKVGCGKSSLLAAITgELHRLCGWVAVSELSKGFGLATQEPWI 676
Cdd:PRK14258 7 AIKVNNLSFYYD----TQKILEGvSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 677 QCATIRDNI--LFGKT--FDAQLYREVLEACALN--------DDL--SILPAGD-----QTEVGEKGVTLSGGQRARIAL 737
Cdd:PRK14258 82 NLNRLRRQVsmVHPKPnlFPMSVYDNVAYGVKIVgwrpkleiDDIveSALKDADlwdeiKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 738 ARAVYQEKALYLLDDPLAAVDADVA---NHLLHRciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEA-----GQLVRTGP 808
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASmkvESLIQS--LRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGL 239
|
....*
gi 24850123 809 PSEIL 813
Cdd:PRK14258 240 TKKIF 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
622-758 |
2.47e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFGL----------ATQEPWIQCATIRDNILFGKTF 691
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvpqSEEVDWSFPVLVEDVVMMGRYG 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24850123 692 DAQLYRE--------VLEACALNDDLSIlpagDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:PRK15056 108 HMGWLRRakkrdrqiVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
622-807 |
3.62e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 46.50 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVseLSKGFGLATQEPW---------IQCATIRDNILFGktfd 692
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF--DGKPLDIAARNRIgylpeerglYPKMKVIDQLVYL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 693 AQLyREVLEACALNDDLSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCIL 771
Cdd:cd03269 95 AQL-KGLKKEEARRRIDEWLERLELSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIR 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 24850123 772 GVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03269 173 ELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1272-1479 |
3.67e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.79 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLAVIPQEPFLFSG-TIREN- 1349
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSLGENv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1350 ---LDPQGLHEDRALWQALEqchlsevAVAMGGLDGeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1425
Cdd:PRK11432 100 gygLKMLGVPKEERKQRVKE-------ALELVDLAG-FEDRYvDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1426 DQLLQQTI---CKRFaNKTVLTIAH-RLNTILNSDRVLVLQAGRVVELDSPSALRNQP 1479
Cdd:PRK11432 172 RRSMREKIrelQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
625-815 |
3.91e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.12 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 625 KKGMLVGIVGKVGCGKSSLLAAITG----------------------ELHRLCGWVAVSELSKGfGLATQEPWIQCATIR 682
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFrspkgvkgsgsvllngmpidakEMRAISAYVQQDDLFIP-TLTVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 683 DNILFGKTFDAQLYREVLEacalndDLSILPAGDqTEVGEKGVT--LSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:TIGR00955 128 MPRRVTKKEKRERVDEVLQ------ALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24850123 761 VANHLLHrcILGVLSHTTR-LLCT-HR--TEYLERADVVLLMEAGQLVRTGPPSEILPL 815
Cdd:TIGR00955 201 MAYSVVQ--VLKGLAQKGKtIICTiHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
627-781 |
3.94e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 627 GMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAvseLSKGFGL------------ATQEPWIQCATIRDNILfgktfdAQ 694
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG---LAKGIKLgyfaqhqleflrADESPLQHLARLAPQEL------EQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 695 LYREVLEACALNddlsilpaGDQteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI---- 770
Cdd:PRK10636 409 KLRDYLGGFGFQ--------GDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIdfeg 478
|
170
....*....|..
gi 24850123 771 -LGVLSHTTRLL 781
Cdd:PRK10636 479 aLVVVSHDRHLL 490
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
622-812 |
4.67e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS------------ELSKGFGLATQEPWIQ--CATIRDNILF 687
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikydkksllEVRKTVGIVFQNPDDQlfAPTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 688 G----KTFDAQLYREVLEACAlnddlsilpagdqtEVGEKGVT------LSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK13639 103 GplnlGLSKEEVEKRVKEALK--------------AVGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 758 DADVANHLLHrcILGVLSH--TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13639 169 DPMGASQIMK--LLYDLNKegITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
705-798 |
5.62e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 705 LNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaDVANHLLHRCILGVLSHTTR--LLC 782
Cdd:PTZ00265 558 IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRitIII 636
|
90
....*....|....*.
gi 24850123 783 THRTEYLERADVVLLM 798
Cdd:PTZ00265 637 AHRLSTIRYANTIFVL 652
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
609-813 |
5.96e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 609 DPIGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAitgeLHRLCGWVAVSELSKGFGLATqepwIQCATIRD----- 683
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRL----LNRLIEPTRGQVLIDGVDIAK----ISDAELREvrrkk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 -NILFgKTFDAQLYREVLEACALNDDLSILPAGDQTE--------VGEKGVT------LSGGQRARIALARAVYQEKALY 748
Cdd:PRK10070 108 iAMVF-QSFALMPHMTVLDNTAFGMELAGINAEERREkaldalrqVGLENYAhsypdeLSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 749 LLDDPLAAVDADVANHLLHRCI-LGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1221-1433 |
7.35e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1221 ERLEEYSCDVPQEPHSQPLQSPHQQRISwLTQGSVEFQDvvlvyRPglpnALDGVTFRVEPGEKLGIVGRTGSGKSSLF- 1299
Cdd:PRK10938 235 EQLEGVQLPEPDEPSARHALPANEPRIV-LNNGVVSYND-----RP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLs 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1300 -------------LVLF---RllepNAGRVLLD-----NVDTSQLELaELRsqlavipqepflFSGTIReNLDPQGLHED 1358
Cdd:PRK10938 305 litgdhpqgysndLTLFgrrR----GSGETIWDikkhiGYVSSSLHL-DYR------------VSTSVR-NVILSGFFDS 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1359 RALWQAL--EQCHLSEVAVAMGGLDGELGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTI 1433
Cdd:PRK10938 367 IGIYQAVsdRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
621-769 |
9.39e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.18 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQepwiqcatirdnilfgktfDAQLYREVL 700
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV----LWQGEPIRRQ-------------------RDEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 701 ---EACALNDDLSILP--------AGDQTE---------VGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:PRK13538 78 ylgHQPGIKTELTALEnlrfyqrlHGPGDDealwealaqVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170
....*....|....*....
gi 24850123 755 AAVD----ADVANHLLHRC 769
Cdd:PRK13538 158 TAIDkqgvARLEALLAQHA 176
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
624-760 |
1.36e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.86 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 624 VKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselsKGFGLATQEPWIQCA------------TIRDNILFGKTF 691
Cdd:PRK13539 25 LAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL----DGGDIDDPDVAEACHylghrnamkpalTVAENLEFWAAF 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 692 DAQLYREVLEA-CALN-DDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:PRK13539 101 LGGEELDIAAAlEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
622-813 |
1.78e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH--------RLCGWVAVSelskGFGLATQEP---------WIQCA----- 679
Cdd:PRK13547 22 LRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN----GEPLAAIDAprlarlravLPQAAqpafa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 680 -TIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ--------EKALY-L 749
Cdd:PRK13547 98 fSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaQPPRYlL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 750 LDDPLAAVDADVANHLLH--RCI-----LGVLS--HTTRLLCTHrteylerADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDtvRRLardwnLGVLAivHDPNLAARH-------ADRIAMLADGAIVAHGAPADVL 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
727-803 |
2.24e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.42 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 727 LSGGQRARIALARAVYQEKALYLLDDPLAAVD---ADVANHLLHRciLGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGE--LNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
624-814 |
2.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.79 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 624 VKKGMLVGIVGKVGCGKSSLLAAITG-----------------ELHRLCGWvavsELSKGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13640 30 IPRGSWTALIGHNGSGKSTISKLINGlllpddnpnskitvdgiTLTAKTVW----DIREKVGIVFQNPDNQFvgATVGDD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 685 ILFGKTFDA-------QLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK13640 106 VAFGLENRAvprpemiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 758 DA-------DVANHLLHRCILGVLShttrllCTHRTEYLERADVVLLMEAGQLVRTGPPSEILP 814
Cdd:PRK13640 175 DPagkeqilKLIRKLKKKNNLTVIS------ITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
621-813 |
3.91e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.91 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 621 HLQVKKGMLVGIVGKVGCGKSSL---LAAITGELHRLCGW--VAVSELSKGFGLATQEPwIQCA------------TIRD 683
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLarlLVGLESPSQGNVSWrgEPLAKLNRAQRKAFRRD-IQMVfqdsisavnprkTVRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NI------LFGKTFDAQLYR--EVLEACALND-DLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:PRK10419 111 IIreplrhLLSLDKAERLARasEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 755 AAVDAdvanhLLHRCILGVL------SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10419 180 SNLDL-----VLQAGVIRLLkklqqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKL 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
627-819 |
4.12e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 627 GMLVGIVGKVGCGKSSLLAAITGELHRLC--GWVAVS------ELSKGFGLATQepwiqcatirDNILFGKTfdaqLYRE 698
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANnrkptkQILKRTGFVTQ----------DDILYPHL----TVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 699 VLEACALNDDLSILPAGDQTEVGEK-----GVT--------------LSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESviselGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24850123 760 DVANHLLHrcILGVLSHTTRLLCTHRTEYLERA----DVVLLMEAGQLVRTGPPSEILPLVQAV 819
Cdd:PLN03211 240 TAAYRLVL--TLGSLAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
622-812 |
4.45e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.92 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL----HRLCGWV-------AVSELsKGFGLAT--QEPwiQCA-----TIRD 683
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVlldgkpvAPCAL-RGRKIATimQNP--RSAfnplhTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 684 NIL-----FGKTFDAQLYREVLEACALNDDLSILPAgdqtevgeKGVTLSGG--QRARIALAraVYQEKALYLLDDPLAA 756
Cdd:PRK10418 101 HARetclaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGmlQRMMIALA--LLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24850123 757 VDADVANHllhrcILGVLSHTTR------LLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK10418 171 LDVVAQAR-----ILDLLESIVQkralgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
941-1056 |
4.45e-04 |
|
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: 44.07 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 941 LLLFSPGNLYTPLLSTPL--HKAASNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPV 1018
Cdd:cd18572 5 LVVAALSELAIPHYTGAVidAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110
....*....|....*....|....*....|....*...
gi 24850123 1019 TFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSV 1056
Cdd:cd18572 85 AFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
728-837 |
5.45e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 728 SGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVAN---------HLLHRCI---LGVLSHTtrllcthrteyler 791
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNlmmdlqqelGLSYVFIshdLSVVEHI-------------- 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 792 ADVVLLMEAGQLVRTGPPSEIL--P-------LVQAVPTAWAE--KEQVATSGQSPS 837
Cdd:PRK11308 222 ADEVMVMYLGRCVEKGTKEQIFnnPrhpytqaLLSATPRLNPDdrRERIKLTGELPS 278
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1271-1452 |
5.87e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1271 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIpqepflfsgtirENL 1350
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1351 DPQGlhedraLWQALEQCHLSEVA---VAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TD 1426
Cdd:PRK13545 107 ELKG------LMMGLTKEKIKEIIpeiIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTfTK 180
|
170 180
....*....|....*....|....*.
gi 24850123 1427 QLLQQTICKRFANKTVLTIAHRLNTI 1452
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
727-813 |
7.32e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 727 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVL--SHTTRLLCTHRTEY-LERADVVLLMEAGQL 803
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNvLEWTKRTIFFKDGKI 243
|
90
....*....|
gi 24850123 804 VRTGPPSEIL 813
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
619-758 |
7.75e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.85 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 619 IShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA---------------------VSELSKGFGLatqepwIQ 677
Cdd:COG1129 271 VS-FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsprdairagiayVPEDRKGEGL------VL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 678 CATIRDNI---LFGKTFDAQLY---REVLEACALNDDLSILPAGDQTEVGekgvTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:COG1129 344 DLSIRENItlaSLDRLSRGGLLdrrRERALAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
....*..
gi 24850123 752 DPLAAVD 758
Cdd:COG1129 420 EPTRGID 426
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
622-820 |
8.15e-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: 43.90 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAI------TGELhRLCGwVAVSELSKG------------F---------------- 667
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEI-RFDG-QDLDGLSRRalrplrrrmqvvFqdpfgslsprmtvgqi 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 668 ---GLATQEPWIQCATIRDNIlfgktfdaqlyREVLEacalnddlsilpagdqtEVGEKGVTL-------SGGQRARIAL 737
Cdd:COG4172 385 iaeGLRVHGPGLSAAERRARV-----------AEALE-----------------EVGLDPAARhryphefSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 738 ARAVYQEKALYLLDDPLAAVDADVANHllhrcILGVLShttRLLCTHRTEYL----------ERADVVLLMEAGQLVRTG 807
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQ-----ILDLLR---DLQREHGLAYLfishdlavvrALAHRVMVMKDGKVVEQG 508
|
250 260
....*....|....*....|..
gi 24850123 808 PPSEIL--P-------LVQAVP 820
Cdd:COG4172 509 PTEQVFdaPqhpytraLLAAAP 530
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
622-837 |
8.36e-04 |
|
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: 43.12 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHRLCGWVA---------VSELS---------KGFGLATQEP-------Wi 676
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSgeilfdgedLLKLSekelrkirgREIQMIFQDPmtslnpvM- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 677 qcaTIRDNI-----LFGKTFDAQLY---REVLEACALNDDLSIL---PagdqtevGEkgvtLSGGQRARIALARAVYQEK 745
Cdd:COG0444 104 ---TVGDQIaeplrIHGGLSKAEAReraIELLERVGLPDPERRLdryP-------HE----LSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 746 ALYLLDDPLAAVD----ADVANHLLHRC---------I---LGVLSHTtrllcthrteylerADVVLLMEAGQLVRTGPP 809
Cdd:COG0444 170 KLLIADEPTTALDvtiqAQILNLLKDLQrelglailfIthdLGVVAEI--------------ADRVAVMYAGRIVEEGPV 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 24850123 810 SEIL-----P----LVQAVPTAWAEKEQVAT-SGQSPS 837
Cdd:COG0444 236 EELFenprhPytraLLSSIPRLDPDGRRLIPiPGEPPS 273
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1279-1424 |
8.47e-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: 42.74 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1279 VEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV--------LLDNVDTSQLE--LAELRS-QLAVI--PQE----PFL 1341
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFRGSELQnyFTKLLEgDVKVIvkPQYvdliPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1342 FSGTIRENLDPQglHEDRALWQALEQCHLSEVavamggLDGELgergQNLSLGQRQLLCLARALLTDAKILCIDEATASV 1421
Cdd:cd03236 103 VKGKVGELLKKK--DERGKLDELVDQLELRHV------LDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
...
gi 24850123 1422 DQK 1424
Cdd:cd03236 171 DIK 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
622-812 |
9.16e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELSKG---------------FGLATQEpwiqcaT 680
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCINL-LERptsgrvLVDGQDLTALSEKelrkarrqigmifqhFNLLSSR------T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 681 IRDNILF----GKTFDAQLYR---EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:PRK11153 99 VFDNVALplelAGTPKAEIKArvtELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24850123 754 LAAVDADVAnhllhRCILGVLS------HTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11153 168 TSALDPATT-----RSILELLKdinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
611-822 |
1.20e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.78 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 611 IGASQKTFIShlQVKKGM----LVGIVGKVGCGKSSLLAAITGELHRLCGWVA----------------VSELSKGFGLA 670
Cdd:PRK14271 29 LGFAGKTVLD--QVSMGFparaVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvllggrsifnyrdVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 671 TQEPWIQCATIRDNILFG----KTFDAQLYREVLEAC--------ALNDDLSILPagdqtevgekgVTLSGGQRARIALA 738
Cdd:PRK14271 107 FQRPNPFPMSIMDNVLAGvrahKLVPRKEFRGVAQARltevglwdAVKDRLSDSP-----------FRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 739 RAVYQEKALYLLDDPLAAVDADVANHlLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEILPLVQ 817
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPK 254
|
....*
gi 24850123 818 AVPTA 822
Cdd:PRK14271 255 HAETA 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
623-813 |
1.41e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.23 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 623 QVKKGMLVGIVGKVGCGKSSLLAAI------TGELH----RLCGWVAvSELSKGFG-LATQE------PWIQCATIRDNI 685
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMagllpgSGSIQfagqPLEAWSA-AELARHRAyLSQQQtppfamPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 686 LFGKTFDAQLYREVLEACALNDDLSilpagdqTEVGekgvTLSGGQRARIALARAVYQ-------EKALYLLDDPLAAVD 758
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLG-------RSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24850123 759 -ADVA--NHLLHR-CILGVlshtTRLLCTH---RTeyLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK03695 166 vAQQAalDRLLSElCQQGI----AVVMSSHdlnHT--LRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
630-765 |
1.58e-03 |
|
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: 43.00 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 630 VGIVGKVGCGKSSLL---AAI----TGElhrlcgwvAVSELSKGFGLATQEPWI-QCATIRDNILFG------------- 688
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLrimAGVdkdfNGE--------ARPQPGIKVGYLPQEPQLdPTKTVRENVEEGvaeikdaldrfne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 689 ---------KTFDAQLYR-----EVLEACA---LNDDLSI------LPAGDQtevgeKGVTLSGGQRARIALARAVYQEK 745
Cdd:TIGR03719 106 isakyaepdADFDKLAAEqaelqEIIDAADawdLDSQLEIamdalrCPPWDA-----DVTKLSGGERRRVALCRLLLSKP 180
|
170 180
....*....|....*....|....
gi 24850123 746 ALYLLDDPLAAVDAD-VA---NHL 765
Cdd:TIGR03719 181 DMLLLDEPTNHLDAEsVAwleRHL 204
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1265-1422 |
1.99e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1265 RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelRSQLAVIPQE-PFLFS 1343
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQEtPALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1344 GTIRENLDpqGLHEDRALWQALEQCHLSE----VAVAMGGLDG----------------------ELGERGQNLSLGQRQ 1397
Cdd:PRK10636 79 PALEYVID--GDREYRQLEAQLHDANERNdghaIATIHGKLDAidawtirsraasllhglgfsneQLERPVSDFSGGWRM 156
|
170 180
....*....|....*....|....*
gi 24850123 1398 LLCLARALLTDAKILCIDEATASVD 1422
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1272-1448 |
2.00e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.09 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1272 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAVIPQE----PFLfsgTIR 1347
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRsginPYL---TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1348 EN--LDpqgLHEDRALWQALEQCHLSEVAVAmggLDGELGErgqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1425
Cdd:PRK13540 93 ENclYD---IHFSPGAVGITELCRLFSLEHL---IDYPCGL----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 24850123 1426 DQLLQQTI-CKRFANKTVLTIAHR 1448
Cdd:PRK13540 163 LLTIITKIqEHRAKGGAVLLTSHQ 186
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
630-781 |
2.02e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 630 VGIVGKVGCGKSSLLAAITGELHRLCGWV--------AVSELSKGFGL-ATQEPWIQCATIRDNILfgktfdAQLYREVL 700
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmAVFSQHHVDGLdLSSNPLLYMMRCFPGVP------EQKLRAHL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 701 EACALNDDLSILPAgdqtevgekgVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCIL---GVL--S 775
Cdd:PLN03073 612 GSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLfqgGVLmvS 681
|
....*.
gi 24850123 776 HTTRLL 781
Cdd:PLN03073 682 HDEHLI 687
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
728-795 |
2.29e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 728 SGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL---------HRCILGVLSH---TTRLLCtHRTEYLERADVV 795
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILallkslqqkHQLAYLFISHdlhVVRALC-HQVIVLRQGEVV 505
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
726-767 |
2.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 24850123 726 TLSGGQRARIALARAVYQEKALYLLDDPlaavdadvANHL-LH 767
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEP--------TNHLdLH 378
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1287-1455 |
3.18e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1287 IVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLelaelrsqlavipQEPFLfsGTIRENLdpqGLH------EDRA 1360
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKPYC--TYIGHNL---GLKlemtvfENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1361 LWQAL-EQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTIC-KRFA 1438
Cdd:PRK13541 93 FWSEIyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANS 172
|
170
....*....|....*..
gi 24850123 1439 NKTVLTIAHRLNTILNS 1455
Cdd:PRK13541 173 GGIVLLSSHLESSIKSA 189
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1273-1425 |
4.99e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1273 DGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVdtsqlelaelrsQLAVIPQEpflfsgtiRENLD 1351
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETV------------KLAYVDQS--------RDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1352 PqglheDRALWQaleqchlsEVAvamGGLD---------------GELGERGQ-------NLSLGQRQLLCLARALLTDA 1409
Cdd:PRK11819 401 P-----NKTVWE--------EIS---GGLDiikvgnreipsrayvGRFNFKGGdqqkkvgVLSGGERNRLHLAKTLKQGG 464
|
170
....*....|....*.
gi 24850123 1410 KILCIDEATASVDQKT 1425
Cdd:PRK11819 465 NVLLLDEPTNDLDVET 480
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
725-796 |
5.88e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.27 E-value: 5.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24850123 725 VTLSGGQRARIALARAV----YQEKALYLLDDPLAAVDADVANHLLhRCILGVLSHTTRLLC-THRTEYLERADVVL 796
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHLVKGAQVIViTHLPELAELADKLI 151
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1267-1461 |
6.42e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1267 GLPNALDG-VTFR-------------VEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV--------LLDNVDTSQL- 1323
Cdd:PRK13409 70 NLPEELEEePVHRygvngfklyglpiPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKRFRGTELq 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 1324 ----ELAELRSQLAVIPQE----PFLFSGTIRENLDpqglhedralwQALEQCHLSEVAVAMGgLDGELGERGQNLSLGQ 1395
Cdd:PRK13409 150 nyfkKLYNGEIKVVHKPQYvdliPKVFKGKVRELLK-----------KVDERGKLDEVVERLG-LENILDRDISELSGGE 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24850123 1396 RQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLnTILN--SDRVLVL 1461
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
622-802 |
7.55e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.23 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLcgwVAVSELSKGFglatqepwiqcatiRDNILFGKtfdaQLYRevle 701
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKA---RLISFLPKFS--------------RNKLIFID----QLQF---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 702 acALNDDLSILPagdqteVGEKGVTLSGGQRARIALARAVYQE--KALYLLDDPLAAVDADVANHLLhRCI--LGVLSHT 777
Cdd:cd03238 71 --LIDVGLGYLT------LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLL-EVIkgLIDLGNT 141
|
170 180
....*....|....*....|....*
gi 24850123 778 TrLLCTHRTEYLERADVVLLMEAGQ 802
Cdd:cd03238 142 V-ILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
627-813 |
7.96e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 39.77 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 627 GMLVGIVGKVGCGKSSLL-------AAITGELhRLCGWVAVSELSKGFG-----LATQEPWIQCATIRDNILFGK----- 689
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLkmlgrhqPPSEGEI-LLDAQPLESWSSKAFArkvayLPQQLPAAEGMTVRELVAIGRypwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24850123 690 ---TFDAQLYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVD-- 758
Cdd:PRK10575 116 algRFGAADREKVEEAISL--------------VGLKPLahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDia 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24850123 759 --ADVANhLLHRcilgvLSHT---TRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10575 182 hqVDVLA-LVHR-----LSQErglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| |
