|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-1052 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 768.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 16 SDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSLKLKLTA 95
Cdd:PLN03130 475 TDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 96 SMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPS-KALVFEEATLSWQQTcpgivng 174
Cdd:PLN03130 555 ARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGlPAISIKNGYFSWDSK------- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 175 aleLERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLE-GSVGVQG 253
Cdd:PLN03130 628 ---AER-------------------------PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 254 SLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDR 333
Cdd:PLN03130 680 TVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 334 QIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMqKKGKyaqLIQK 413
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS-NNGP---LFQK 835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 414 -MHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQ-------LTQEEEMEEGSLSWRVYHHYIQAAGGYM 485
Cdd:PLN03130 836 lMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKskegksvLIKQEERETGVVSWKVLERYKNALGGAW 915
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 486 VSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGtnssrESNGTMadlgniadnpqlsFYQLVYGLNALLLICVGVCSSGIF 565
Cdd:PLN03130 916 VVMILFLCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPL-------------FYNLIYALLSFGQVLVTLLNSYWL 977
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 566 TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFL--VLSLMVIAVLL-IVSVLSPY 642
Cdd:PLN03130 978 IMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqIFQLLSTFVLIgIVSTISLW 1057
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 643 ILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTEDFISQFK-RLTDAQNNYLLLFL 721
Cdd:PLN03130 1058 AIMPLLVLFYGAYLYYQSTAREV---KRLDSITRSPVYAQFGEALNGLSTIRAY-KAYDRMAEINgRSMDNNIRFTLVNM 1133
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 722 SSTRWMALRLEIMTNLVTLAVALFVAFGIS--STPYSFKV---MAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:PLN03130 1134 SSNRWLAIRLETLGGLMIWLTASFAVMQNGraENQAAFAStmgLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYI 1213
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 797 KMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPM 876
Cdd:PLN03130 1214 DL-PSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE 1292
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 877 AGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENG 956
Cdd:PLN03130 1293 RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAG 1372
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 957 GNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
1050
....*....|....*.
gi 1034596369 1037 FDRPEVLRKKPGSLFA 1052
Cdd:PLN03130 1453 FDTPENLLSNEGSAFS 1468
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-1052 |
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: 748.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 4 MAVKA---QHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVAT- 79
Cdd:TIGR00957 477 MAMKTktyQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVAl 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 80 -AVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQES---PVFYVQTLQD-PSKA 154
Cdd:TIGR00957 557 iTFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEElepDSIERRTIKPgEGNS 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 155 LVFEEATLSWQQTCPgivngalelernghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSL 234
Cdd:TIGR00957 637 ITVHNATFTWARDLP------------------------------------PTLNGITFSIPEGALVAVVGQVGCGKSSL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 235 LSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLN 314
Cdd:TIGR00957 681 LSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVN 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECI--KKTLRGKTVVLVTHQLQYLEFCGQIILLENGKIC 392
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 393 ENGTHSELMQKKGKYAQLI-------QKMHKEATSDMLQdTAKIAEKPKVESQALAT-----------SLEESLNGNAVP 454
Cdd:TIGR00957 841 EMGSYQELLQRDGAFAEFLrtyapdeQQGHLEDSWTALV-SGEGKEAKLIENGMLVTdvvgkqlqrqlSASSSDSGDQSR 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 455 EH----------------QLTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVfLTIFSFWWLSYWleqgsgt 518
Cdd:TIGR00957 920 HHgssaelqkaeakeetwKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHV-SALASNYWLSLW------- 991
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 519 nssreSNGTMADLGNIADNPQLSFYQLVYGLN--ALLLICVGVCSSGIFtkvtrkASTALHNKLFNKVFRCPMSFFDTIP 596
Cdd:TIGR00957 992 -----TDDPMVNGTQNNTSLRLSVYGALGILQgfAVFGYSMAVSIGGIQ------ASRVLHQDLLHNKLRSPMSFFERTP 1060
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 597 IGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyilLMGAIIMVICFIYYMMFKKAIGV---FKRLEN 673
Cdd:TIGR00957 1061 SGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATP---IAAVIIPPLGLLYFFVQRFYVASsrqLKRLES 1137
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 674 YSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISST 753
Cdd:TIGR00957 1138 VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSL 1217
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 754 PYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRD 833
Cdd:TIGR00957 1218 SAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYRE 1296
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 834 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTI 913
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL 1376
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 993
Cdd:TIGR00957 1377 RMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 994 DTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1052
Cdd:TIGR00957 1457 DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-1055 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 705.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTsevsDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:PLN03232 464 MRKLTKEGLQWT----DKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 81 VWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQT-LQDPSKALVFEE 159
Cdd:PLN03232 540 VSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPpLQPGAPAISIKN 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 160 ATLSWQqtcpgivngaLELERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL 239
Cdd:PLN03232 620 GYFSWD----------SKTSK-------------------------PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 240 EEM-HLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGG 318
Cdd:PLN03232 665 GELsHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGG 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 319 QKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHS 398
Cdd:PLN03232 745 QKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFA 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 399 ELMQKKGKYAQLIQKMHK-EATSDMLQDTAKIAEK-PKVE---SQALATSLEESLNGNAVpehqLTQEEEMEEGSLSWRV 473
Cdd:PLN03232 825 ELSKSGSLFKKLMENAGKmDATQEVNTNDENILKLgPTVTidvSERNLGSTKQGKRGRSV----LVKQEERETGIISWNV 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 474 YHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSResngtmadlgniadnpqlSFYQLVYGLNALL 553
Cdd:PLN03232 901 LMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSP------------------GFYIVVYALLGFG 962
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 554 LICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ----LLPIFSEQFLVLsLMV 629
Cdd:PLN03232 963 QVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRnvanLMNMFMNQLWQL-LST 1041
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 630 IAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTEDFISQFK-R 708
Cdd:PLN03232 1042 FALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREV---RRLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRMAKINgK 1117
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 709 LTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTP-----YSFKVMAVNIVLQLASSFQATARIGLETE 783
Cdd:PLN03232 1118 SMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAE 1197
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 784 AQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKS 863
Cdd:PLN03232 1198 NSLNSVERVGNYIDL-PSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKS 1276
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 864 SLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISK 943
Cdd:PLN03232 1277 SMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDR 1356
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 944 FPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNC 1023
Cdd:PLN03232 1357 NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC 1436
|
1050 1060 1070
....*....|....*....|....*....|..
gi 1034596369 1024 DHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 1055
Cdd:PLN03232 1437 DKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-1055 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 613.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 3 RMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVW 82
Cdd:PTZ00243 408 KHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVV 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 83 VLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFlqESPVFYVQTLQDPSK--------- 153
Cdd:PTZ00243 488 FTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFL--ECDNATCSTVQDMEEywreqrehs 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 154 -----ALVFEEAT-----------------------LSW----------QQTCPGIVNGALE----LERNGHASEGMTRP 191
Cdd:PTZ00243 566 tacqlAAVLENVDvtafvpvklprapkvktsllsraLRMlcceqcrptkRHPSPSVVVEDTDygspSSASRHIVEGGTGG 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 192 RDALGPEEEGNSLGPE--------------LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAY 257
Cdd:PTZ00243 646 GHEATPTSERSAKTPKmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAY 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 258 VPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYL 337
Cdd:PTZ00243 726 VPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 338 LDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK---KGKYAQLIQKM 414
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyATLAAELKENK 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 415 H-KEATSDMLQDTAKIAE------KPKVESQALATSLEESLNGNAVpEHQLTQEEEMEEGSLSWRVYHHYIQAAGGYMVS 487
Cdd:PTZ00243 886 DsKEGDADAEVAEVDAAPggavdhEPPVAKQEGNAEGGDGAALDAA-AGRLMTREEKASGSVPWSTYVAYLRFCGGLHAA 964
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 488 CIIFFFVVLIVFLTIFSFWWLSYWleqgsGTNSSRESNGTmadlgniadnpqlsfYQLVYglnaLLLICVGVCSSGIFTK 567
Cdd:PTZ00243 965 GFVLATFAVTELVTVSSGVWLSMW-----STRSFKLSAAT---------------YLYVY----LGIVLLGTFSVPLRFF 1020
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 568 VT----RKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYI 643
Cdd:PTZ00243 1021 LSyeamRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFV 1100
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 644 LLmgAIIMViCFIYY--MMFKKAIG-VFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLF 720
Cdd:PTZ00243 1101 LV--ALVPC-GYLYYrlMQFYNSANrEIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLE 1177
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 721 LSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQAT----ARIGLETEAQFTAVERILQYM 796
Cdd:PTZ00243 1178 NVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATlnwlVRQVATVEADMNSVERLLYYT 1257
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 797 KMCVSEAPLHM-----------------------EGTSCPQGWP---QHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHE 850
Cdd:PTZ00243 1258 DEVPHEDMPELdeevdalerrtgmaadvtgtvviEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPRE 1337
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 851 VVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWD 930
Cdd:PTZ00243 1338 KVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWA 1417
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 931 ALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVL-RNSKIILIDEATASIDMETDTLIQRTIREAFQGCT 1009
Cdd:PTZ00243 1418 ALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYT 1497
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*.
gi 1034596369 1010 VLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 1055
Cdd:PTZ00243 1498 VITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-1038 |
3.11e-150 |
|
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: 485.57 E-value: 3.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 18 QRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI--IPTVATAV--WVLIHTSLKLKL 93
Cdd:TIGR01271 258 ERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFsgFFVVFLSVvpYALIKGIILRRI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 94 TASMAFSMLASLNLLRLsvffVPIAVKGLTNSKSAVMRFKKFFLQESpvFYVQTLQDPSKALVFEEATLSWQQtcpGIvn 173
Cdd:TIGR01271 338 FTTISYCIVLRMTVTRQ----FPGAIQTWYDSLGAITKIQDFLCKEE--YKTLEYNLTTTEVEMVNVTASWDE---GI-- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 174 GAL-ELERNGHASEGMTRPRDALGPEEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQ 252
Cdd:TIGR01271 407 GELfEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 253 GSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSD 332
Cdd:TIGR01271 487 GRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKD 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 333 RQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI- 411
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLl 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 412 -----QKMHKEATSDMLQDT---------------------------AKIAEKPK-------------------VESQAL 440
Cdd:TIGR01271 647 gleafDNFSAERRNSILTETlrrvsidgdstvfsgpetikqsfkqppPEFAEKRKqsiilnpiasarkfsfvqmGPQKAQ 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 441 ATSLEESLNG------NAVPE------------------------------------------HQLT------------- 459
Cdd:TIGR01271 727 ATTIEDAVREpserkfSLVPEdeqgeeslprgnqyhhglqhqaqrrqsvlqlmthsnrgenrrEQLQtsfrkkssitqqn 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 460 -------------------------QEEEMEE----------GSLSWRVYHHYIQAAGGyMVSCIIFFFVVlivFLTIFS 504
Cdd:TIGR01271 807 elaseldiysrrlskdsvyeiseeiNEEDLKEcfaderenvfETTTWNTYLRYITTNRN-LVFVLIFCLVI---FLAEVA 882
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 505 FWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQL----SFYQLVYglnalllICVGVCSS----GIF-------TKVT 569
Cdd:TIGR01271 883 ASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIitptSAYYIFY-------IYVGTADSvlalGFFrglplvhTLLT 955
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 570 rkASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAI 649
Cdd:TIGR01271 956 --VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIP 1033
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 650 IMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMAL 729
Cdd:TIGR01271 1034 VAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQM 1113
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 730 RLEIMTNLVTLAVAlFVAFGISSTpysfKVMAVNIVLQLA----SSFQATARIGLETEAQFTAVERILQYMKMCVSEAP- 804
Cdd:TIGR01271 1114 RIDIIFVFFFIAVT-FIAIGTNQD----GEGEVGIILTLAmnilSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRp 1188
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 805 ------------LHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 872
Cdd:TIGR01271 1189 sggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL 1268
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 873 VEpMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDV 952
Cdd:TIGR01271 1269 LS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVL 1347
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 953 VENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNG 1032
Cdd:TIGR01271 1348 VDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGS 1427
|
....*.
gi 1034596369 1033 KVVEFD 1038
Cdd:TIGR01271 1428 SVKQYD 1433
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
483-796 |
9.22e-135 |
|
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: 409.26 E-value: 9.22e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 483 GYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 562
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDN-STVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 563 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 642
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 643 ILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLS 722
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 723 STRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
820-1040 |
2.99e-124 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 378.37 E-value: 2.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 899
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 979
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 1040
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
470-1054 |
9.93e-110 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 353.32 E-value: 9.93e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 470 SWRVYHHYIQAAGGYMVSCII-FFFVVLIVFLTIFSFWWLSYWLEQGSgtnssreSNGTMADLGNIAdnpqlsfyqLVYG 548
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILaLLLLLLSALLELLLPLLLGRIIDALL-------AGGDLSALLLLL---------LLLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 549 LNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 628
Cdd:COG1132 69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 629 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 708
Cdd:COG1132 149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 709 LTDaqnNYLLLFLSSTRWMAL---RLEIMTNLVTLAVALFVAFGISS---TPYSFkVMAVNIVLQLASSFQATARIGLET 782
Cdd:COG1132 229 ANE---ELRRANLRAARLSALffpLMELLGNLGLALVLLVGGLLVLSgslTVGDL-VAFILYLLRLFGPLRQLANVLNQL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 783 EAQFTAVERILQYMkmcvSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGK 862
Cdd:COG1132 305 QRALASAERIFELL----DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 863 SSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAI 941
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKAAQAHEFI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 942 SKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVL 1021
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
|
570 580 590
....*....|....*....|....*....|...
gi 1034596369 1022 NCDHILVMGNGKVVEFDRPEVLRKKPGsLFAAL 1054
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGG-LYARL 571
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
198-390 |
3.87e-104 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 324.42 E-value: 3.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 198 EEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 277
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 278 AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC 357
Cdd:cd03250 91 PFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC 170
|
170 180 190
....*....|....*....|....*....|....
gi 1034596369 358 IKKTLR-GKTVVLVTHQLQYLEFCGQIILLENGK 390
Cdd:cd03250 171 ILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
816-1040 |
3.60e-98 |
|
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: 308.57 E-value: 3.60e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 816 WPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL 895
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 896 RSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALErtfltkaiskfpkklhtdVVENGGNFSVGERQLLCIARAVLR 975
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 976 NSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 1040
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
564-1056 |
2.30e-92 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 310.61 E-value: 2.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 564 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYI 643
Cdd:COG2274 219 LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 644 LLMGAIIMVICFIYYMMFKKAIG--VFKRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLlfl 721
Cdd:COG2274 298 ALVVLLLIPLYVLLGLLFQPRLRrlSREESEASAK--RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARF--- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 722 sSTRWMALRLEIMTNLVT-LAVALFVAFGisstpySFKVM----------AVNIVL-QLASSFQATARIGLETEAQFTAV 789
Cdd:COG2274 373 -KLRRLSNLLSTLSGLLQqLATVALLWLG------AYLVIdgqltlgqliAFNILSgRFLAPVAQLIGLLQRFQDAKIAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 790 ERILQYMKMcVSEAPLHMEGTSCPQgwpQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL 869
Cdd:COG2274 446 ERLDDILDL-PPEREEGRSKLSLPR---LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 870 FRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAISKFPKKL 948
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGY 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 949 HTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILV 1028
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
490 500
....*....|....*....|....*...
gi 1034596369 1029 MGNGKVVEFDRPEVLRKKPGsLFAALMA 1056
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKG-LYAELVQ 708
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
820-1057 |
6.41e-75 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 247.90 E-value: 6.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 899
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 979
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALMAT 1057
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRT 255
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
598-1048 |
1.53e-73 |
|
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: 254.31 E-value: 1.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 598 GRLLNCFAGDLEQLDQL-----LPIfseqfLVLSLMVIAVLLIVSVLSPYI-LLMGAIIMVICFIY-YMMFKKAIGVFKR 670
Cdd:COG4987 112 GDLLNRLVADVDALDNLylrvlLPL-----LVALLVILAAVAFLAFFSPALaLVLALGLLLAGLLLpLLAARLGRRAGRR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 671 LENySRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQNNYLLLFLSSTRWMALR---LEIMTNLVTLAVALFVA 747
Cdd:COG4987 187 LAA-ARAALRARLTDLLQGAAELAAYGALDRAL---ARLDAAEARLAAAQRRLARLSALAqalLQLAAGLAVVAVLWLAA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 748 FGISSTPYSFKVMAVnIVLQLASSFQATARIGL---ETEAQFTAVERILQymkmcVSEAPLHMEGTSCPQGWPQHGEIIF 824
Cdd:COG4987 263 PLVAAGALSGPLLAL-LVLAALALFEALAPLPAaaqHLGRVRAAARRLNE-----LLDAPPAVTEPAEPAPAPGGPSLEL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 825 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 904
Cdd:COG4987 337 EDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIIL 981
Cdd:COG4987 417 RPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 982 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1048
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
487-796 |
5.72e-73 |
|
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: 243.57 E-value: 5.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 487 SCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTnssresngtmadlgniaDNPQLSFYQLVY-GLNALLLICVGVCSSGIF 565
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSS-----------------PNSSSGYYLGVYaALLVLASVLLVLLRWLLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 566 TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILL 645
Cdd:cd18580 64 VLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 646 MGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 725
Cdd:cd18580 144 VLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 726 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18580 224 WLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
820-1048 |
3.92e-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: 235.97 E-value: 3.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 899
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSGTIRFNLDPFD-RHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSK 978
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 979 IILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1048
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
822-1033 |
7.28e-66 |
|
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: 219.18 E-value: 7.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 901
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDPVLLSGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIIL 981
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 982 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGK 1033
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
552-1036 |
9.98e-64 |
|
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: 226.91 E-value: 9.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 552 LLLICVGVC---SSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLpifSEQFLVL--- 625
Cdd:TIGR02203 62 GLAVLRGICsfvSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA---TDAFIVLvre 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 626 SLMVIA---VLLIVS-VLSPYILLMGAIIMVICFIYYmmfkkaigvfKRLENYSRsplfsHILNS-----------LQGL 690
Cdd:TIGR02203 139 TLTVIGlfiVLLYYSwQLTLIVVVMLPVLSILMRRVS----------KRLRRISK-----EIQNSmgqvttvaeetLQGY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 691 SSIHVYGKTEdfiSQFKRLtDAQNNYLLLFlsstrwmALRLEIMTNL--------------VTLAVALFVAFGISSTPYS 756
Cdd:TIGR02203 204 RVVKLFGGQA---YETRRF-DAVSNRNRRL-------AMKMTSAGSIsspitqliaslalaVVLFIALFQAQAGSLTAGD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 757 FKVMAVNIvLQLASSFQATARIGLETEAQFTAVERILQYmkmcVSEAPLHMEGTSCPQgwPQHGEIIFQDYHMKYRDNTP 836
Cdd:TIGR02203 273 FTAFITAM-IALIRPLKSLTNVNAPMQRGLAAAESLFTL----LDSPPEKDTGTRAIE--RARGDVEFRNVTFRYPGRDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 916
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPFDRHT--DQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETD 994
Cdd:TIGR02203 426 IAYGRTEQadRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1034596369 995 TLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:TIGR02203 506 RLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
822-1054 |
6.59e-63 |
|
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: 213.63 E-value: 6.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 901
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDPVLLSGTIRFNLdpfdRH-----TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 976
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 977 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAAL 1054
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEM 232
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
487-795 |
3.58e-62 |
|
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: 214.49 E-value: 3.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 487 SCIIFFFVVLIVFLT----IFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 562
Cdd:cd18601 1 GVFVFILLVLLNIAAqvlyVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 563 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 642
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 643 ILLmGAIIMVICFI----YYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLL 718
Cdd:cd18601 161 VLI-PVIPLVILFLflrrYYLKTSREV---KRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 719 LFLSSTRWMALRLEIMTnLVTLAVALFVAFGISSTPYSFKV-MAVNIVLQLASSFQATARIGLETEAQFTAVERILQY 795
Cdd:cd18601 237 LFLATSRWLAVRLDALC-ALFVTVVAFGSLFLAESLDAGLVgLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
489-796 |
6.44e-61 |
|
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: 210.03 E-value: 6.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 489 IIFFFVVLIVFLTIFSFWWLSYWLEQgsgtnssresngtmADLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKV 568
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSEWSDD--------------PALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 569 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILlmgA 648
Cdd:cd18603 69 CVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFL---V 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 649 IIMVICFIYYMMFKKAIGV---FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 725
Cdd:cd18603 146 VIIPLAILYFFIQRFYVATsrqLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 726 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18603 226 WLAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
489-796 |
7.67e-61 |
|
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: 209.64 E-value: 7.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 489 IIFFFVVLIVFLTIFSFWWLSYWLEqgsgtNSSRESNGtmadlgniadnpqlsFYQLVY-GLNALLLICVgVCSSGIFTK 567
Cdd:cd18606 3 LLLLLLILSQFAQVFTNLWLSFWTE-----DFFGLSQG---------------FYIGIYaGLGVLQAIFL-FLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 568 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMg 647
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 648 AIIMVICFIYYMMFKKAIGV-FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRW 726
Cdd:cd18606 141 LPPLLVLYYFIANYYRASSReLKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRW 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 727 MALRLEIMTNLVTLAVALFVAFGISS-TPYSFKVmAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSiSPSSTGL-VLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
822-1036 |
1.19e-60 |
|
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: 207.08 E-value: 1.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 901
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 979
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
489-796 |
2.63e-58 |
|
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: 202.70 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 489 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTmadlgniadnpqLSFYQLVYGLNALLLICVGVCSSGIFTKV 568
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVS------------VLYYLGIYALISLLSVLLGTLRYLLFFFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 569 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGA 648
Cdd:cd18604 71 SLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 649 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMA 728
Cdd:cd18604 151 VLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLS 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 729 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18604 231 VRIDLLGALFSFATAALLVYGPGIDA-GLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
822-1055 |
1.26e-57 |
|
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: 198.53 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 899
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSGTIRFN--LDPFDRhTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 977
Cdd:cd03249 80 GLVSQEPVLFDGTIAENirYGKPDA-TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALM 1055
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG-VYAKLV 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
206-389 |
6.13e-55 |
|
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: 190.23 E-value: 6.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV-----------------GVQGSLAYVPQQAWIVSGN 268
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 349 VGKHIFEECIKKTLRG--KTVVLVTHQLQYLEFCGQIILLENG 389
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
819-1036 |
6.30e-54 |
|
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: 199.28 E-value: 6.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 819 HGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK 898
Cdd:COG5265 355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 976
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNI-AYGRPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 977 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
206-411 |
1.93e-53 |
|
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: 188.53 E-value: 1.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYL 285
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 286 QVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGK 365
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 366 TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 411
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
822-1056 |
5.15e-53 |
|
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: 185.38 E-value: 5.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 901
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDPVLLSGTIRFNLDPFDRHTD-QQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKII 980
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 981 LIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAALMA 1056
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQ 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
820-1038 |
6.19e-52 |
|
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: 183.90 E-value: 6.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEpMAGRILIDGVDICSIGLEDLRSKL 899
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 979
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFD 1038
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-412 |
2.14e-51 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 191.15 E-value: 2.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKP----FAKIIEDLRRKERKLLEKCGLVQSLTSITLFIipT 76
Cdd:COG1132 181 FGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSALFFPLMELLGNL--G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 77 VATAVWVLIHTSLKLKLTASMAFSMLASLNLL-----RLSVFFVpiavkGLTNSKSAVMRFKKFFLQESPVfyvqtlQDP 151
Cdd:COG1132 259 LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLfgplrQLANVLN-----QLQRALASAERIFELLDEPPEI------PDP 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 152 SKALVFEEatlswqqtcpgiVNGALELERNGHAsegmtrprdalGPEEEgnslgPELHKINLVVSKGMMLGVCGNTGSGK 231
Cdd:COG1132 328 PGAVPLPP------------VRGEIEFENVSFS-----------YPGDR-----PVLKDISLTIPPGETVALVGPSGSGK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 232 SSLLSAILEEMHLLEGSV---GV----------QGSLAYVPQQAWIVSGNIRENILMG--GAyDKARYLQVLHCCSLNRD 296
Cdd:COG1132 380 STLVNLLLRFYDPTSGRIlidGVdirdltleslRRQIGVVPQDTFLFSGTIRENIRYGrpDA-TDEEVEEAAKAAQAHEF 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 297 LELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQY 376
Cdd:COG1132 459 IEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLST 537
|
410 420 430
....*....|....*....|....*....|....*.
gi 1034596369 377 LEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 412
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
581-1054 |
3.76e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 187.86 E-value: 3.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 581 FNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQL----LPIFSEQFLvlSLMVIAVLLIVSVlspYI-LLMGAIIMVICF 655
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTL---LRGTDALfglwLEFMREHLA--TLVALVVLLPLAL---FMnWRLSLVLVVLGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 656 IYYMM----FKKAIGVFKRLENYsRSPLFSHILNSLQGLSSIHVYGKTEDFISQFK----RLTDAQNNYL--------LL 719
Cdd:PRK13657 168 VYTLIttlvMRKTKDGQAAVEEH-YHDLFAHVSDAIGNVSVVQSYNRIEAETQALRdiadNLLAAQMPVLswwalasvLN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 720 FLSSTRWMALRLEIMTNLVT---LAVALFVAFgisstpYSFKVMAVNIVLQLAS----SFQATARIgleteAQFTAVERI 792
Cdd:PRK13657 247 RAASTITMLAILVLGAALVQkgqLRVGEVVAF------VGFATLLIGRLDQVVAfinqVFMAAPKL-----EEFFEVEDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 793 LQYmkmcVSEAPlhmeGTSCPQGWpqHGEIIFQDYHMKYrDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 872
Cdd:PRK13657 316 VPD----VRDPP----GAIDLGRV--KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 873 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL-----DPfdrhTDQQIWDALERTFLTKAISKFPKK 947
Cdd:PRK13657 385 FDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 948 LHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHIL 1027
Cdd:PRK13657 461 YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
|
490 500 510
....*....|....*....|....*....|
gi 1034596369 1028 VMGNGKVVE---FDrpEVLRKkpGSLFAAL 1054
Cdd:PRK13657 541 VFDNGRVVEsgsFD--ELVAR--GGRFAAL 566
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
598-1016 |
1.43e-49 |
|
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: 184.49 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 598 GRLLNCFAGDLEQLDQLLP--IFSeqfLVLSLMV--IAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLEN 673
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVrvIVP---AGVALVVgaAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 674 YSRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI--- 750
Cdd:TIGR02868 187 RLRGELAAQLTDALDGAAELVASGALPAAL---AQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGpav 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 751 SSTPYSFKVMAVNIVLQLASsFQATARIGLE----TEAQfTAVERILQYM--KMCVSEAPLHMEGTSCPQGWPqhgeIIF 824
Cdd:TIGR02868 264 ADGRLAPVTLAVLVLLPLAA-FEAFAALPAAaqqlTRVR-AAAERIVEVLdaAGPVAEGSAPAAGAVGLGKPT----LEL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 825 QDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 904
Cdd:TIGR02868 338 RDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DPVLLSGTIRFNLDpFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILI 982
Cdd:TIGR02868 417 DAHLFDTTVRENLR-LARPdaTDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
410 420 430
....*....|....*....|....*....|....
gi 1034596369 983 DEATASIDMETDTLIQRTIREAFQGCTVLVIAHR 1016
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
488-796 |
2.35e-49 |
|
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: 177.41 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 488 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADlgniaDNPQLSFYQLVYGLNALLLICVGVCSSGIFTK 567
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSL-----EDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 568 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 647
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 648 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqNNYLLLFLSST-RW 726
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDR-NNTAFLFLNTAnRW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 727 MALRLEIMTNLVTLA---VALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18602 236 LGIRLDYLGAVIVFLaalSSLTAALAGYISP-SLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
1-132 |
2.57e-49 |
|
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: 176.60 E-value: 2.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:cd18592 156 IAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASV 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 81 VWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRF 132
Cdd:cd18592 236 VTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
569-1029 |
4.16e-49 |
|
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: 183.26 E-value: 4.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 569 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 648
Cdd:TIGR02857 72 AAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA---LEGVEALDGYFARYLPQLVLAVIVPLAILAAVFP-QDWISG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 649 IIMVICFIYYMMFKKAIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnylllFLS 722
Cdd:TIGR02857 148 LILLLTAPLIPIFMILIGWAaqaaarKQWAALSR--LSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEE-------YRE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 723 STrwMA-LRLEIMTNLV-----TLAVALfVAFGISstpysFKVMAVNIVL------------------QLASSFQATAri 778
Cdd:TIGR02857 219 RT--MRvLRIAFLSSAVlelfaTLSVAL-VAVYIG-----FRLLAGDLDLatglfvlllapefylplrQLGAQYHARA-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 779 glETEAQFTAVERILQymkmcVSEAPLHMEGtscPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRT 858
Cdd:TIGR02857 289 --DGVAAAEALFAVLD-----AAPRPLAGKA---PVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 859 GSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFL 937
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 938 TKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRV 1017
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRL 517
|
490
....*....|..
gi 1034596369 1018 TTVLNCDHILVM 1029
Cdd:TIGR02857 518 ALAALADRIVVL 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
205-405 |
7.27e-49 |
|
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: 183.42 E-value: 7.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 205 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRE 271
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:COG4988 430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 351 KHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKG 405
Cdd:COG4988 510 AEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
820-1035 |
1.20e-48 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 172.39 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 899
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSGTIRFNL---DPFdrHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 976
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 977 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRvTTVLN-CDHILVMGNGKVV 1035
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR-PSLLDlVDRIIVMDSGRIV 217
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
489-796 |
3.22e-47 |
|
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: 171.17 E-value: 3.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 489 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 568
Cdd:cd18605 3 LILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFIND-------------SFNFFLTVYGFLAGLNSLFTLLRAFLFAYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 569 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLmga 648
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 649 IIMVICFIYYMM---FKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQF-KRLTDAQNNYLLLfLSST 724
Cdd:cd18605 147 LLLPLAFIYYRIqryYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYlEKLENNQRAQLAS-QAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 725 RWMALRLEIMTNLVTLAVALFVAFGIS---STPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
208-412 |
3.42e-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: 181.19 E-value: 3.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRENIL 274
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENIT 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 MGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI 353
Cdd:COG2274 571 LGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 354 FeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 412
Cdd:COG2274 651 L-ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
580-1056 |
2.94e-46 |
|
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: 177.84 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 580 LFNKVFRCPMSFFDTIPIGRLLNCFAGdLEQLDQLLP----------IFSEQFLVLSLMVIAVLLIVSVLspyILLmgAI 649
Cdd:TIGR03797 215 VWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSgstlttllsgIFALLNLGLMFYYSWKLALVAVA---LAL--VA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 650 IMVICFIYYMMFKKaigVFKRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQnnylllflsstRWMAL 729
Cdd:TIGR03797 289 IAVTLVLGLLQVRK---ERRLLELSGK--ISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQ-----------RKLEL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 730 RLEIMTNLVT------LAVALFVAFGISSTPYSFKVMAVNIVLQLASSF-QATARIGLETEAQFTAVERILQYMKMC-VS 801
Cdd:TIGR03797 353 SAQRIENLLTvfnavlPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFgSFSGAVTQLSNTLISILAVIPLWERAKpIL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 802 EAPLHMEGTSCPQGwPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMA 877
Cdd:TIGR03797 433 EALPEVDEAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfeTPES 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 878 GRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGG 957
Cdd:TIGR03797 508 GSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 958 NFSVGERQLLCIARAVLRNSKIILIDEATASIDMETdtliQRTIREAF--QGCTVLVIAHRVTTVLNCDHILVMGNGKVV 1035
Cdd:TIGR03797 588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLerLKVTRIVIAHRLSTIRNADRIYVLDAGRVV 663
|
490 500
....*....|....*....|.
gi 1034596369 1036 EFDRPEVLRKKPGsLFAALMA 1056
Cdd:TIGR03797 664 QQGTYDELMAREG-LFAQLAR 683
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
582-1036 |
3.35e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.06 E-value: 3.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 582 NKVFRCPMSFFDTIPIGRLLNCFAGDLEQL-DQLLPIFSEQFLVLSL---MVIAVLLI---VSVLSPYILLMGAIIMVIc 654
Cdd:PRK10790 106 DAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLYVTVVATVLRSAALigaMLVAMFSLdwrMALVAIMIFPAVLVVMVI- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 655 fiyYMMFKKAIgvFKRLenysRSPL------FSHILNslqGLSSIHVYGKTEDFisqFKRLTDAQNNYLLlflssTRWMA 728
Cdd:PRK10790 185 ---YQRYSTPI--VRRV----RAYLadindgFNEVIN---GMSVIQQFRQQARF---GERMGEASRSHYM-----ARMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 729 LRLE--IMTNLVTLAVA-----LFVAFGISSTP-------YSFkvmaVNIVLQLASSF-QATARIGLETEAqFTAVERIL 793
Cdd:PRK10790 245 LRLDgfLLRPLLSLFSAlilcgLLMLFGFSASGtievgvlYAF----ISYLGRLNEPLiELTTQQSMLQQA-VVAGERVF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 794 QYMkmcvsEAPLHMEGTScpqGWP-QHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 872
Cdd:PRK10790 320 ELM-----DGPRQQYGND---DRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 873 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLdPFDRH-TDQQIWDALERTFLTKAISKFPKKLHTD 951
Cdd:PRK10790 391 YPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRDiSEEQVWQALETVQLAELARSLPDGLYTP 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 952 VVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGN 1031
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549
|
....*
gi 1034596369 1032 GKVVE 1036
Cdd:PRK10790 550 GQAVE 554
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
560-1048 |
2.40e-44 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 172.21 E-value: 2.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 560 CSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVL 639
Cdd:TIGR00958 220 LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 640 SPYILLMGAIIMVICFIYYMMFKKAI-GVFKRLENySRSPLFSHILNSLQGLSSIHVYG-------KTEDFISQFKRLTD 711
Cdd:TIGR00958 300 SPRLTMVTLINLPLVFLAEKVFGKRYqLLSEELQE-AVAKANQVAEEALSGMRTVRSFAaeegeasRFKEALEETLQLNK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 712 AQNNYLLLFLSSTRWMALRLE----------IMTNLVTlaVALFVAFGIsstpYSFKV-MAVNIVLQLASSFQATArigl 780
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQvlvlyyggqlVLTGKVS--SGNLVSFLL----YQEQLgEAVRVLSYVYSGMMQAV---- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 781 eteaqfTAVERILQYM--KMCVSE----APLHMEGTscpqgwpqhgeIIFQDYHMKY--RDNTPtVLHGINLTIRGHEVV 852
Cdd:TIGR00958 449 ------GASEKVFEYLdrKPNIPLtgtlAPLNLEGL-----------IEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 853 GIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLD-PFDRHTDQQIWDA 931
Cdd:TIGR00958 511 ALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 932 LERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTirEAFQGCTVL 1011
Cdd:TIGR00958 591 AKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVL 668
|
490 500 510
....*....|....*....|....*....|....*..
gi 1034596369 1012 VIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1048
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
566-1056 |
4.93e-44 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 171.28 E-value: 4.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 566 TKVTRKASTALHNKLFNKVFRCPMSFFDTipigRllncFAGDLE---QL-DQLLPIFSEQFL--VLSLMVIAVLLIVSVL 639
Cdd:TIGR03796 219 RRLEIKLAVGMSARFLWHILRLPVRFFAQ----R----HAGDIAsrvQLnDQVAEFLSGQLAttALDAVMLVFYALLMLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 640 spYILLMGAIIMVICFIYYMMFKKaigVFKRLENYSRS------PLFSHILNSLQGLSSIHVYGKTEDFisqFKRLTDAQ 713
Cdd:TIGR03796 291 --YDPVLTLIGIAFAAINVLALQL---VSRRRVDANRRlqqdagKLTGVAISGLQSIETLKASGLESDF---FSRWAGYQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 714 NNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGisstpySFKVMAVNIVL-------QLASSFQA--TARIGL---- 780
Cdd:TIGR03796 363 AKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVG------GLRVMEGQLTIgmlvafqSLMSSFLEpvNNLVGFggtl 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 781 -ETEAQFTAVERILQYMKMCVSEAPLHMEGTSCPQgWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTG 859
Cdd:TIGR03796 437 qELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPP-RRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSG 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 860 SGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLT 938
Cdd:TIGR03796 516 SGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTiPDADLVRACKDAAIH 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 939 KAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREafQGCTVLVIAHRVT 1018
Cdd:TIGR03796 596 DVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLS 673
|
490 500 510
....*....|....*....|....*....|....*...
gi 1034596369 1019 TVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMA 1056
Cdd:TIGR03796 674 TIRDCDEIIVLERGKVVQRGTHEELWAVGG-AYARLIR 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
208-412 |
3.68e-42 |
|
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: 163.40 E-value: 3.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRENIL 274
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 MG--GAYDkARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKH 352
Cdd:COG4987 431 LArpDATD-EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 353 IFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 412
Cdd:COG4987 510 LLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
598-1036 |
7.18e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 162.69 E-value: 7.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 598 GRLLNCFAGDLEQLDQL-LPIFSEqfLVLSLMVIAVLLI-VSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRLENY 674
Cdd:PRK11160 117 GDLLNRLVADVDTLDHLyLRLISP--LVAALVVILVLTIgLSFFDLTLaLTLGGILLLLLLLLPLLFYRLGKKPGQDLTH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 675 SRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQnnylllflssTRWMAlRLEIMTNLVTLAVALFVAFGisstp 754
Cdd:PRK11160 195 LRAQYRVQLTEWLQGQAELTLFGAEDRYR---QQLEQTE----------QQWLA-AQRRQANLTGLSQALMILAN----- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 755 ysfkVMAVNIVLQLASS-----FQATARIGLETEAQFTAVERIL------QYMKMCVS-----------EAPLHMEGTSC 812
Cdd:PRK11160 256 ----GLTVVLMLWLAAGgvggnAQPGALIALFVFAALAAFEALMpvagafQHLGQVIAsarrineiteqKPEVTFPTTST 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 813 PQgwPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 892
Cdd:PRK11160 332 AA--ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 893 EDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCI 969
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGI 486
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 970 ARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
817-1034 |
4.53e-41 |
|
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: 150.70 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 817 PQH--GEIIFQDYHMKYRDNTPT-VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 893
Cdd:cd03248 5 PDHlkGIVKFQNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 894 DLRSKLSVIPQDPVLLSGTIRFNLD------PFDRHTDQQIwDALERTFltkaISKFPKKLHTDVVENGGNFSVGERQLL 967
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAyglqscSFECVKEAAQ-KAHAHSF----ISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 968 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1034
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
842-1062 |
8.85e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 159.63 E-value: 8.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFD 921
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 922 RH-TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 1000
Cdd:PRK11174 448 PDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 1001 IREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMATATSSL 1062
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG-LFATLLAHRQEEI 588
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
820-1048 |
3.21e-40 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 157.87 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 899
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSGTIRFNLD--PFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 977
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1048
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
206-405 |
4.60e-39 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 145.06 E-value: 4.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:cd03254 97 IRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 352 HIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKG 405
Cdd:cd03254 177 LI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
206-410 |
6.11e-39 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 145.07 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG--GAyDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 350
Cdd:cd03251 96 IAYGrpGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ES 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 351 KHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 410
Cdd:cd03251 174 ERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
830-1034 |
1.36e-37 |
|
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: 138.89 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 830 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLL 909
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 910 SGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATASI 989
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 990 DMETDTLIQRTIREA-FQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1034
Cdd:cd03246 128 DVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
206-413 |
2.12e-37 |
|
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: 140.44 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG--GAYDKARYLQVLHCCsLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:cd03253 95 IRYGrpDATDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 351 KHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 413
Cdd:cd03253 174 REIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
838-1045 |
2.18e-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: 148.74 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL 917
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 918 DPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLI 997
Cdd:COG4618 427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 998 QRTIREA-FQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEF-DRPEVLRK 1045
Cdd:COG4618 507 AAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
202-395 |
2.39e-36 |
|
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: 136.95 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 202 NSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGN 268
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:cd03245 94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034596369 348 HVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENG 395
Cdd:cd03245 174 NSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
212-413 |
3.53e-36 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 137.29 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 212 NLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENILMGGa 278
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIRYGK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 279 yDKARYLQVLHCCSL-NRD--LELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfE 355
Cdd:cd03249 102 -PDATDEEVEEAAKKaNIHdfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV-Q 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 356 ECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 413
Cdd:cd03249 180 EALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
201-390 |
5.64e-36 |
|
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: 134.05 E-value: 5.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 201 GNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG 267
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 268 NIRENILmggaydkarylqvlhccslnrdlellpfgdmteigerglnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:cd03228 91 TIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 348 HVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGK 390
Cdd:cd03228 130 ETEALIL-EALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
8-421 |
9.29e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.08 E-value: 9.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 8 AQHHTSEVSDQrirvTSEVLTCIKLIKMYTWEK----PFAKIIEDLRRKERKLLEkcglVQSLTSITLFIIPTVAT--AV 81
Cdd:PRK10789 168 AQAAFSSLNDR----TQESLTSIRMIKAFGLEDrqsaLFAADAEDTGKKNMRVAR----IDARFDPTIYIAIGMANllAI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 82 ----WVLIHTSLKL-KLTASMAFSMLASLNLLRLSVFFvPIAVKGltnskSAVMRFKKFFLQESPVfyvqtLQDPSKALV 156
Cdd:PRK10789 240 gggsWMVVNGSLTLgQLTSFVMYLGLMIWPMLALAWMF-NIVERG-----SAAYSRIRAMLAEAPV-----VKDGSEPVP 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 157 FEEATLSWqqtcpgivngalelernghASEGMTRPRdalgpeeegnSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLS 236
Cdd:PRK10789 309 EGRGELDV-------------------NIRQFTYPQ----------TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 237 AILEEMHLLEGSVGVQ-------------GSLAYVPQQAWIVSGNIRENILMGG-AYDKARYLQVLHCCSLNRDLELLPF 302
Cdd:PRK10789 360 LIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 303 GDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQ 382
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASE 518
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034596369 383 IILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSD 421
Cdd:PRK10789 519 ILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALD 557
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
204-396 |
1.43e-35 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 134.93 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 204 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 270
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahvg 350
Cdd:cd03244 96 SNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD---- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 351 kHIFEECIKKTLR----GKTVVLVTHQLQYLEFCGQIILLENGKICENGT 396
Cdd:cd03244 172 -PETDALIQKTIReafkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
832-1037 |
4.78e-35 |
|
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: 133.40 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 832 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 908
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 lsgtirfNLDPfdRHT-DQQIWDALERTFLTKAISKFPKKLHTDVVENGGN----------FSVGERQLLCIARAVLRNS 977
Cdd:cd03257 94 -------SLNP--RMTiGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlnrypheLSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1037
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
839-987 |
6.37e-35 |
|
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: 130.46 E-value: 6.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIRFNL 917
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 918 -------DPFDRHTDQQIWDALERTfltkaisKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATA 987
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
205-413 |
1.88e-34 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 132.22 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 205 GPE-LHKINLVVSKGMMLGVCGNTGSGKSSLlSAILEEMHLLE-GSVGVQG-------------SLAYVPQQAWIVSGNI 269
Cdd:cd03252 14 GPViLDNISLRIKPGEVVGIVGRSGSGKSTL-TKLIQRFYVPEnGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:cd03252 93 RDNIALADpGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 349 vGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 413
Cdd:cd03252 173 -SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
205-386 |
4.19e-34 |
|
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: 138.57 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 205 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRE 271
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:TIGR02857 415 NIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034596369 351 KHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILL 386
Cdd:TIGR02857 495 AEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
831-1033 |
4.51e-34 |
|
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: 128.13 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 831 YRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQdpvlLS 910
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----LS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 GtirfnldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASID 990
Cdd:cd00267 83 G--------------------------------------------------GQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034596369 991 METDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGK 1033
Cdd:cd00267 113 PASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
822-1036 |
1.45e-33 |
|
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: 127.43 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSV 901
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDPVLLSGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIIL 981
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 982 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
832-1041 |
7.72e-33 |
|
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: 7.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 832 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 908
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 -------LSGTIRFNLDPFDRHTDQQIWD----ALERTFL-TKAISKFPkklHTdvvenggnFSVGERQLLCIARAVLRN 976
Cdd:COG1123 354 slnprmtVGDIIAEPLRLHGLLSRAERRErvaeLLERVGLpPDLADRYP---HE--------LSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 977 SKIILIDEATASIDMetdtLIQRTIREAFQ------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1041
Cdd:COG1123 423 PKLLILDEPTSALDV----SVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
204-412 |
2.74e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 133.82 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 204 LGPelhkINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLlEGSVGVQG-------------SLAYVPQQAWIVSGNIR 270
Cdd:PRK11174 366 AGP----LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:PRK11174 441 DNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 350 GKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 412
Cdd:PRK11174 521 EQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
300-1031 |
3.46e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.31 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 300 LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKHIFEECIKkTLRG---KTVVLVTHQLQY 376
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTIN-NLKGnenRITIIIAHRLST 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 377 LEFCGQIILLENGK-----------------------------------------------ICENGTHSELMQKK-GKYA 408
Cdd:PTZ00265 643 IRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYY 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 409 QLI--QKMHKEAT--------SDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQLTQEEEME---EGSLSW--RV 473
Cdd:PTZ00265 723 TMInnQKVSSKKSsnndndkdSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASEnnaGGKLPFlrNL 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 474 YHHYIQAAGGY-MVSCIIFFFV--VLIVFLTI---------FSFWWLSYWleqgsgtnssresnGTMADLGNI-ADNPQL 540
Cdd:PTZ00265 803 FKRKPKAPNNLrIVYREIFSYKkdVTIIALSIlvagglypvFALLYAKYV--------------STLFDFANLeANSNKY 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 541 SFYQLVYglnALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDT---IPiGRLLNCFAGDLEQLDQLLP- 616
Cdd:PTZ00265 869 SLYILVI---AIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVn 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 617 ---IFSeQFLVLslmviavLLIVSVLSPYIL-LMGAIIMVICFIYYMMF-------------KKAIG------VFKRLEN 673
Cdd:PTZ00265 945 nivIFT-HFIVL-------FLVSMVMSFYFCpIVAAVLTGTYFIFMRVFairarltankdveKKEINqpgtvfAYNSDDE 1016
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 674 YSRSPLFShILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNylllflsstrwmALRLEIMTNLVTLAVALFVAFGISST 753
Cdd:PTZ00265 1017 IFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNK------------GQKRKTLVNSMLWGFSQSAQLFINSF 1083
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 754 PYSFK-------VMAVNIVLQLASSFQATAR-----IGLETEAQfTAVERILQYMKMCVSEAPLHME---GTSCPQGWPQ 818
Cdd:PTZ00265 1084 AYWFGsflirrgTILVDDFMKSLFTFLFTGSyagklMSLKGDSE-NAKLSFEKYYPLIIRKSNIDVRdngGIRIKNKNDI 1162
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 819 HGEIIFQDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL------------------------ 872
Cdd:PTZ00265 1163 KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqd 1241
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 873 ------------------------------VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDpFDR 922
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGK 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 923 H--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 1000
Cdd:PTZ00265 1321 EdaTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
890 900 910
....*....|....*....|....*....|...
gi 1034596369 1001 IREAFQGC--TVLVIAHRVTTVLNCDHILVMGN 1031
Cdd:PTZ00265 1401 IVDIKDKAdkTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
822-1053 |
3.90e-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: 132.33 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSIGLEDLRSK 898
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQDP--VLLSGTIRF-------NLDPFDRHTDQQIWDALERTFLTKAISKFPkklHTdvvenggnFSVGERQLLCI 969
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDqiaealeNLGLSRAEARARVLELLEAVGLERRLDRYP---HQ--------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 970 ARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKK 1046
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
....*..
gi 1034596369 1047 PGSLFAA 1053
Cdd:COG1123 234 PQALAAV 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
208-392 |
7.55e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 123.80 E-value: 7.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQA---WIVSGNIRENILMG 276
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRsidRDFPISVRDVVLMG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 gaydkaRYLQVLHCCSLNRD-----LELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:cd03235 95 ------LYGHKGLFRRLSKAdkakvDEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034596369 351 KHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKIC 392
Cdd:cd03235 169 EDIYE--LLRELRreGMTILVVTHDLgLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
470-796 |
3.80e-31 |
|
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: 125.30 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 470 SWRVYHHYIQAAGGYM-VSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTmadlgNIADNPQLSFYQL-VY 547
Cdd:cd18600 2 TWNTYLRYITSHKSLIfVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTY-----AVIVTFTSSYYVFyIY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 548 GLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSL 627
Cdd:cd18600 77 VGVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 628 MVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFK 707
Cdd:cd18600 157 IVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 708 RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAlFVAFGISstpySFKVMAVNIVLQLA----SSFQATARIGLETE 783
Cdd:cd18600 237 KALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVT-FISIGTT----GDGEGRVGIILTLAmnimSTLQWAVNTSIDVD 311
|
330
....*....|...
gi 1034596369 784 AQFTAVERILQYM 796
Cdd:cd18600 312 SLMRSVSRIFKFI 324
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
206-412 |
5.88e-31 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 130.63 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLlSAILEEMHLLE-GSVGVQG-------------SLAYVPQQAWIVSGNIRE 271
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTL-TKLLQRLYTPQhGQVLVDGvdlaiadpawlrrQMGVVLQENVLFSRSIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGGAydKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:TIGR01846 550 NIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 349 vGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 412
Cdd:TIGR01846 628 -SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQ 690
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
837-1043 |
7.17e-31 |
|
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: 122.46 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP---------- 906
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPpapfgltvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 907 -VLLSgtiRFN-LDPFDRHTD---QQIWDALERTfltkAISKFpkkLHTDVVEnggnFSVGERQLLCIARAVLRNSKIIL 981
Cdd:COG1120 95 lVALG---RYPhLGLFGRPSAedrEAVEEALERT----GLEHL---ADRPVDE----LSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 982 IDEATASIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP-EVL 1043
Cdd:COG1120 161 LDEPTSHLDLahqlEVLELLRRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
206-410 |
8.81e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 129.05 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:TIGR02204 354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVMEN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGGAydKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHv 349
Cdd:TIGR02204 434 IRYGRP--DATDEEVEAAARAAHAHEFisaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE- 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 350 GKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 410
Cdd:TIGR02204 511 SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
488-768 |
1.19e-30 |
|
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: 122.37 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 488 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTK 567
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ--------------ALNVYSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 568 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 647
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 648 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWM 727
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034596369 728 ALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQL 768
Cdd:pfam00664 228 FGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
822-1033 |
4.74e-30 |
|
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: 118.34 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDN---TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsK 898
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQDPVLLSGTIRFNL---DPFDrhtDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLR 975
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFD---EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 976 NSKIILIDEATASIDMET-DTLIQRTIREAFQGC-TVLVIAHRVTTVLNCDHILVMGNGK 1033
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
206-411 |
5.78e-30 |
|
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: 127.55 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGgAYDKARYLQVLHCCSL---NRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:TIGR01193 568 LLLG-AKENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 350 GKHIFEECIKktLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 411
Cdd:TIGR01193 647 EKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
208-402 |
1.68e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQAWIVSG---NIRENILMG 276
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAEVDWDfpiTVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 --------GAYDKARYLQVLHCcslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDLADRPIGeLSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 348 HvGKHIFEECIKKtLR--GKTVVLVTHQLQYL-EFCGQIILLENGKICEnGTHSELMQ 402
Cdd:COG1121 173 A-TEEALYELLRE-LRreGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
206-413 |
4.06e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 123.78 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG--GAYDkARYLQVLHCCSLNRDLELLPfGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:PRK11160 434 LLLAapNASD-EALIEVLQQVGLEKLLEDDK-GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 351 KHIFEeCIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 413
Cdd:PRK11160 512 RQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQR 573
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
1-131 |
6.04e-29 |
|
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: 117.59 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:cd18579 158 LAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSL 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 81 VWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 131
Cdd:cd18579 238 ATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
801-1048 |
7.29e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 122.90 E-value: 7.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 801 SEAPLHMEGT-SCPQGwpqHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGR 879
Cdd:PRK10789 295 AEAPVVKDGSePVPEG---RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 880 ILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENG 956
Cdd:PRK10789 372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 957 GNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:PRK10789 450 VMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
250
....*....|..
gi 1034596369 1037 FDRPEVLRKKPG 1048
Cdd:PRK10789 530 RGNHDQLAQQSG 541
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
830-1033 |
1.26e-28 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 114.49 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 830 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP--V 907
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LLSGTIR---------FNLDPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 978
Cdd:cd03225 88 FFGPTVEeevafglenLGLPEEEI--EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 979 IILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1033
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
828-1035 |
4.06e-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: 111.76 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 828 HMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQdpV 907
Cdd:cd03214 6 SVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LlsgtIRFNLDPFdrhtdqqiwdaLERTFLTkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATA 987
Cdd:cd03214 82 L----ELLGLAHL-----------ADRPFNE--------------------LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 988 SIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:cd03214 127 HLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
837-1040 |
4.43e-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: 113.22 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLRS----KLSVIPQD---- 905
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 906 --PVLlsgTIRFNL-DPFDRHTD-------QQIWDALERTFLTKA---ISKFPkklHtdvvenggNFSVGERQLLCIARA 972
Cdd:COG0444 99 lnPVM---TVGDQIaEPLRIHGGlskaearERAIELLERVGLPDPerrLDRYP---H--------ELSGGMRQRVMIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 973 VLRNSKIILIDEATASIDMetdtLIQRTI-------REAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE-------F 1037
Cdd:COG0444 165 LALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelF 239
|
...
gi 1034596369 1038 DRP 1040
Cdd:COG0444 240 ENP 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
837-1045 |
6.70e-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: 110.28 E-value: 6.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDPVLLSG-T 912
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 913 IRFNLD-PFDRHT-------DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:cd03261 94 VFENVAfPLREHTrlseeeiREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 985 ATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRK 1045
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
208-391 |
7.48e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.14 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALadLDPPT--SGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 I-----LMGGAYDKARYLQVLHccSLNRDLELLpfgDmTEIGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:COG4619 94 LpfpfqLRERKFDRERALELLE--RLGLPPDIL---D-KPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034596369 348 HvGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKI 391
Cdd:COG4619 164 E-NTRRVEELLREYLAeeGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
822-1036 |
8.04e-27 |
|
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: 109.98 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSI---GLEDL 895
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 896 RSKLSVIPQDPVLLSG-TIRFNLD-PF------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLL 967
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 968 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
838-1043 |
1.97e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 108.81 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLLS 910
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 GTIRFNLDPFDRHT---DQQIWDALERTFLTKAiskfpkKLHTDVVE--NGGNFSVGERQLLCIARAVLRNSKIILIDEA 985
Cdd:cd03260 95 GSIYDNVAYGLRLHgikLKEELDERVEEALRKA------ALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 986 TASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVL 1043
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
831-1040 |
2.10e-26 |
|
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: 108.81 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 831 YRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPV 907
Cdd:cd03256 10 YPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 L----------LSG------TIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 971
Cdd:cd03256 89 LierlsvlenvLSGrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQL-----------SGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 972 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVL-NCDHILVMGNGKVVeFDRP 1040
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIV-FDGP 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
206-411 |
2.23e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 116.36 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG-GAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:TIGR00958 575 IAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 352 HIFEEcikKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 411
Cdd:TIGR00958 655 LLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
206-403 |
5.34e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 113.98 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGGayDKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhV 349
Cdd:TIGR01842 412 IARFG--ENADPEKIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-E 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 350 GKHIFEECIKKT-LRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 403
Cdd:TIGR01842 489 GEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
837-1033 |
1.11e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 104.96 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLLSgtir 914
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 915 fnldpfdrhtdqqiwdalertfltkaiskfpkklHTDVVENGG-NFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 993
Cdd:cd03229 90 ----------------------------------HLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 994 DTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGK 1033
Cdd:cd03229 136 RREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
838-1044 |
1.71e-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: 105.59 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDPVLLSG-TIRF 915
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 916 NLD-PFDRHTDQQIWDALERTFltkaiSKFPK---KLHTDvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATA---- 987
Cdd:cd03224 95 NLLlGAYARRRAKRKARLERVY-----ELFPRlkeRRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEglap 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 988 SIDMETDTLIqRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLR 1044
Cdd:cd03224 166 KIVEEIFEAI-RELRD--EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
837-1035 |
1.94e-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: 105.31 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSKLSVIPQ------------ 904
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQrrsidrdfpisv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 -DPVLLSGTIRFNLDPFDRHTDQQIWD-ALERTfltkAISKFPKKlhtdvveNGGNFSVGERQLLCIARAVLRNSKIILI 982
Cdd:cd03235 88 rDVVLMGLYGHKGLFRRLSKADKAKVDeALERV----GLSELADR-------QIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 983 DEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMgNGKVV 1035
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
839-1041 |
2.14e-25 |
|
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: 111.70 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPvllsgtirF 915
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--------F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 916 N-LDPfdRHT---------------------DQQIWDALERTFLTKA-ISKFPkklHtdvvEnggnFSVGERQLLCIARA 972
Cdd:COG4172 373 GsLSP--RMTvgqiiaeglrvhgpglsaaerRARVAEALEEVGLDPAaRHRYP---H----E----FSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 973 VLRNSKIILIDEATASIDMetdtLIQRTIREAFQ------GCTVLVIAH--RVTTVLnCDHILVMGNGKVVE-------F 1037
Cdd:COG4172 440 LILEPKLLVLDEPTSALDV----SVQAQILDLLRdlqrehGLAYLFISHdlAVVRAL-AHRVMVMKDGKVVEqgpteqvF 514
|
....
gi 1034596369 1038 DRPE 1041
Cdd:COG4172 515 DAPQ 518
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
208-410 |
6.69e-25 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 111.07 E-value: 6.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLL-------EGSVGV---------QGSL----AYVPQQawIVSG 267
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLA-------RLLfrfydvtSGRILIdgqdirdvtQASLraaiGIVPQD--TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 268 N--IRENILMG--GAyDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:COG5265 445 NdtIAYNIAYGrpDA-SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 344 AVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 410
Cdd:COG5265 524 ALDSRTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
206-410 |
9.19e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.49 E-value: 9.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------SLAYVPQQAWIVSGN-------IREN 272
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdyTLASLRNQVALVSQNvhlfndtIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 IlmggAY---DKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:PRK11176 437 I----AYartEQYSREQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 347 AHVgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 410
Cdd:PRK11176 513 TES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
208-401 |
9.47e-25 |
|
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: 104.36 E-value: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAwIVSGNI--REN 272
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEP-PAPFGLtvREL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG--------GAYDKARYLQVLHCcslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:COG1120 96 VALGryphlglfGRPSAEDREAVEEA------LERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 344 AVDAHvgkHIFE--ECIKK--TLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 401
Cdd:COG1120 167 HLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
206-403 |
2.67e-24 |
|
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: 108.68 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 272
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 IlmggaydkARYLQV-------------LHccslnrDLEL-LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:COG4618 426 I--------ARFGDAdpekvvaaaklagVH------EMILrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 339 DDPLSAVDAhVGKHIFEECI---KKtlRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 403
Cdd:COG4618 492 DEPNSNLDD-EGEAALAAAIralKA--RGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
837-1035 |
5.26e-24 |
|
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: 99.43 E-value: 5.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQdpvllsgtirf 915
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 916 nldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATASI-DMETD 994
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALtPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034596369 995 TLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:cd03216 120 RLFKviRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
833-1034 |
9.12e-24 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 100.64 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 833 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPV 907
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LLSG-TIRFNLD-------PFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKI 979
Cdd:cd03255 93 LLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1034
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
822-1036 |
1.19e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 898
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQDPVLLsgtirFNLDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQ 965
Cdd:COG2884 81 IGVVFQDFRLL-----PDRTVYEnvalplrvtgksrKEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 966 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKVVE 1036
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
822-1034 |
1.27e-23 |
|
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: 100.17 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 898
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQDPVLLSgtirfNLDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQ 965
Cdd:cd03292 80 IGVVFQDFRLLP-----DRNVYEnvafalevtgvppREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 966 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKV 1034
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
206-374 |
1.38e-23 |
|
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: 106.29 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIREN 272
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG-GAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:TIGR02868 429 LRLArPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
170 180
....*....|....*....|...
gi 1034596369 352 HIFEEcIKKTLRGKTVVLVTHQL 374
Cdd:TIGR02868 509 ELLED-LLAALSGRTVVLITHHL 530
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
208-406 |
1.44e-23 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 100.70 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSGN-IRENIL 274
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRLtVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 M-GGAYDKARYLQVLHCCSLNRDLELLPFGDMteigeRGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHI 353
Cdd:COG4555 97 YfAELYGLFDEELKKRIEELIELLGLEEFLDR-----RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 354 FEECIKKtLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKGK 406
Cdd:COG4555 171 LREILRA-LKkeGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
204-396 |
1.61e-23 |
|
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: 99.79 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 204 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 270
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMGGAYDKARYLQVLhccslnrdlellpfgdmtEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVg 350
Cdd:cd03369 100 SNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 351 KHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 396
Cdd:cd03369 161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
208-391 |
4.20e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 97.51 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpqqawivsgnirENILMGGAYDKARYL-- 285
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-----------------KDLASLSPKELARKIay 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 286 --QVLHCCslnrdlellpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHVGKHIFEECI 358
Cdd:cd03214 78 vpQALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLAR 145
|
170 180 190
....*....|....*....|....*....|....
gi 1034596369 359 KktlRGKTVVLVTHQL-QYLEFCGQIILLENGKI 391
Cdd:cd03214 146 E---RGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
208-390 |
9.65e-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: 97.16 E-value: 9.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIRENI- 273
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVRENLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 ----LMGGAYDKARYLQVLHCCSLnRDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHv 349
Cdd:COG4133 98 fwaaLYGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034596369 350 GKHIFEECIKKTL-RGKTVVLVTHQLQYLEFCgQIILLENGK 390
Cdd:COG4133 166 GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
822-1046 |
1.72e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.52 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 901
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDP------VLLSGTIRFNLD--PFDRH-TDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 972
Cdd:PRK13632 88 IFQNPdnqfigATVEDDIAFGLEnkKVPPKkMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 973 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP-EVLRKK 1046
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNK 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
186-412 |
1.91e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 103.26 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 186 EGMTRPRDALGPEEEGNSLG---------------PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVG 250
Cdd:PRK10790 320 ELMDGPRQQYGNDDRPLQSGrididnvsfayrddnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 251 VQG-------------SLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSG 317
Cdd:PRK10790 400 LDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 318 GQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifEECIKKTLRG----KTVVLVTHQLQYLEFCGQIILLENGKICE 393
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAIQQALAAvrehTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
250
....*....|....*....
gi 1034596369 394 NGTHSELMQKKGKYAQLIQ 412
Cdd:PRK10790 555 QGTHQQLLAAQGRYWQMYQ 573
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
208-403 |
2.01e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.44 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIRENI- 273
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMGGAYD------KARYLQVLhccslnRDLELLPFGDmTEIGerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:COG1131 96 FFARLYGlprkeaRERIDELL------ELFGLTDAAD-RKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 348 hVGKHIFEECIKK-TLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQK 403
Cdd:COG1131 165 -EARRELWELLRElAAEGKTVLLSTHYLEEAErLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
206-391 |
2.38e-22 |
|
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: 94.98 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIREN 272
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILmggaydkarylqvlhccslnrdlellpfgdmteigerglnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKH 352
Cdd:cd03246 96 IL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034596369 353 IFEECIKKT-LRGKTVVLVTHQLQYLEFCGQIILLENGKI 391
Cdd:cd03246 134 ALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
1-131 |
2.61e-22 |
|
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: 98.29 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 81 VWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 131
Cdd:cd18597 242 LSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKR 292
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
205-390 |
4.87e-22 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 93.85 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 205 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAWivsgniRENILMggaydkar 283
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEEL------RRRIGY-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 284 ylqvLHCcslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL- 362
Cdd:cd00267 78 ----VPQ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLRELAe 128
|
170 180
....*....|....*....|....*....
gi 1034596369 363 RGKTVVLVTHQLQYLE-FCGQIILLENGK 390
Cdd:cd00267 129 EGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1-132 |
5.70e-22 |
|
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: 97.32 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:cd18594 158 LGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSF 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 81 VWVLIHTSLKLKLTASMAFSMLASLNLLRLSV-FFVPIAVKGLTNSKSAVMRF 132
Cdd:cd18594 238 ATFVPYVLTGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
822-1036 |
6.88e-22 |
|
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: 95.23 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGledlrSKL 899
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLL-----SGTIRFNLD---PFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 971
Cdd:cd03293 76 GYVFQQDALLpwltvLDNVALGLElqgVPKAEARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 972 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVT-TVLNCDHILVMGN--GKVVE 1036
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
837-1036 |
9.75e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.84 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDPVLLS--- 910
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLSsrt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 --GTIRFNL-----DPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILID 983
Cdd:COG1135 99 vaENVALPLeiagvPKAEI--RKRVAELLELVGLSDKADAYPSQL-----------SGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 984 EATASIDMETdT-----LIQRtIREAFqGCTVLVIAH------RVttvlnCDHILVMGNGKVVE 1036
Cdd:COG1135 166 EATSALDPET-TrsildLLKD-INREL-GLTIVLITHemdvvrRI-----CDRVAVLENGRIVE 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
208-395 |
1.62e-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: 92.76 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------------LAYVPQQAWIVSGNIRENIlm 275
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTLRNNL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 ggaydkarylqvlhccslnrdlellpfgdmteigerGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFe 355
Cdd:cd03247 96 ------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034596369 356 ECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENG 395
Cdd:cd03247 139 SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
842-1031 |
1.74e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 101.64 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI-DGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL--- 917
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 918 ----------------DPFDRHT---------------------------------------DQQIWDALERTFLTKAIS 942
Cdd:PTZ00265 484 lyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 943 KFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIR--EAFQGCTVLVIAHRVTTV 1020
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
250
....*....|.
gi 1034596369 1021 LNCDHILVMGN 1031
Cdd:PTZ00265 644 RYANTIFVLSN 654
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
208-391 |
2.52e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 93.71 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhLL----EGSVGVQG-----------------SLAYVPQQ-AWIV 265
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG----GLdrptSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 266 SGNIRENILMGgaydkARYLQVLHCCSLNRDLELLpfgDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYLLDD 340
Cdd:cd03255 96 DLTALENVELP-----LLLAGVPKKERRERAEELL---ERVGLGDR-LNhypseLSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 341 PLSAVDAHVGKHIFEEcIKKT--LRGKTVVLVTHQLQYLEFCGQIILLENGKI 391
Cdd:cd03255 167 PTGNLDSETGKEVMEL-LRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
837-1045 |
3.10e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIgLEDLRSKLSVIPQDPVL---LS- 910
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLvpnLSv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 -------------GTIRfnldpfdrhtdqqiWDALERTFlTKAISKFpkKLHTDVVENGGNFSVGERQLLCIARAVLRNS 977
Cdd:COG1129 97 aeniflgreprrgGLID--------------WRAMRRRA-RELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 978 KIILIDEATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EFDRPEVLRK 1045
Cdd:COG1129 160 RVLILDEPTASLtEREVERLFRiiRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVgtgpvaELTEDELVRL 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
835-1034 |
4.31e-21 |
|
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: 91.72 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 835 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLL 909
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRkregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 910 SGTIRFNLdpfdrhtdqqiwdalertFLTKAISkfpkklhtdvvenGGNfsvgeRQLLCIARAVLRNSKIILIDEATASI 989
Cdd:cd03215 92 DLSVAENI------------------ALSSLLS-------------GGN-----QQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034596369 990 DMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:cd03215 136 DVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
208-390 |
4.41e-21 |
|
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: 92.53 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSL-------------AYVPQQA--WIVSGNIREN 272
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrkvGLVFQNPddQFFGPTVEEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 IL-----MGGAYDKARylqvlhccslNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:cd03225 97 VAfglenLGLPEEEIE----------ERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034596369 347 AHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGK 390
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
208-391 |
4.47e-21 |
|
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: 93.30 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLsAILEEMHLLE-GSVGVQGS-------------LAYVPQQAWIVSGNIRENI 273
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVV-ALLENFYQPQgGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMGgaydkarylqvLHCCSLNRDLEL------------LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDP 341
Cdd:cd03248 109 AYG-----------LQSCSFECVKEAaqkahahsfiseLASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 342 LSAVDAHvGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 391
Cdd:cd03248 178 TSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
822-1035 |
6.88e-21 |
|
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: 92.43 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdLRSKL 899
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDPVLLSG-TIRFNLDPFDR-HtdqqiwdALERTFLTKAISKFPKKLHTDVVEN--GGNFSVGERQLLCIARAVLR 975
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGlY-------GLKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 976 NSKIILIDEATASID-METDTLIQ--RTIREAfqGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:cd03266 154 DPPVLLLDEPTTGLDvMATRALREfiRQLRAL--GKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
208-374 |
8.27e-21 |
|
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: 92.15 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV--------GVQGSLAYVPQQA----WIvsgNIRENILM 275
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQQDallpWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 G----GAYDKARYLQVLHCcslnrdLELLpfgdmteigerGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPL 342
Cdd:cd03293 97 GlelqGVPKAEARERAEEL------LELV-----------GLSgfenayphqLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....
gi 1034596369 343 SAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQL 374
Cdd:cd03293 160 SALDALTREQLQEE-LLDIWRetGKTVLLVTHDI 192
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
1-131 |
9.10e-21 |
|
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: 94.10 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:cd18596 177 LAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTV 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 81 VWVLIHTSL-KLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 131
Cdd:cd18596 257 VTFATYTLVmGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDR 308
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
837-1038 |
1.01e-20 |
|
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: 91.81 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVL---LS--G 911
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALfphLTvaE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 TIRFNLDPF---DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATAS 988
Cdd:cd03259 92 NIAFGLKLRgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 989 IDMETDTLIQRTIREAF--QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 1038
Cdd:cd03259 161 LDAKLREELREELKELQreLGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
822-1034 |
1.13e-20 |
|
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: 91.44 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKL 899
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 900 SVIPQDpvllsgtirFNLDP----FDRHTDQQIW--------------DALERTFLTKAISKFPKKLhtdvvenggnfSV 961
Cdd:cd03262 79 GMVFQQ---------FNLFPhltvLENITLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 962 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
831-1041 |
1.15e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 831 YRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLRSKLSVIPQDPV-- 907
Cdd:PRK13644 11 YPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPEtq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 ---------LLSGTIRFNLDPFDrhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 978
Cdd:PRK13644 90 fvgrtveedLAFGPENLCLPPIE--IRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 979 IILIDEATASIDMET-DTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 1041
Cdd:PRK13644 157 CLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
822-1053 |
1.55e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.98 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLS- 900
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 901 VIPQDPVLLSGTIRFN------LDPFDRHT-DQQIWDALERTFLTKA--ISKFPKKLhtdvvenggnfSVGERQLLCIAR 971
Cdd:cd03295 80 VIQQIGLFPHMTVEENialvpkLLKWPKEKiRERADELLALVGLDPAefADRYPHEL-----------SGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 972 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPG 1048
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPA 228
|
....*
gi 1034596369 1049 SLFAA 1053
Cdd:cd03295 229 NDFVA 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
199-400 |
1.74e-20 |
|
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: 91.49 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 199 EEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG----------------SLAYV 258
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI----NGLErptsGSVLVDGtdltllsgkelrkarrRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 259 PQQAWIVSG-NIRENIlmggAYDkaryLQVLHCCSLNRD---LELLPFGDMTEIGER-GLNLSGGQKQRISLARAVYSDR 333
Cdd:cd03258 88 FQHFNLLSSrTVFENV----ALP----LEIAGVPKAEIEervLELLELVGLEDKADAyPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 334 QIYLLDDPLSAVDAHVGKHIFeECIKKTLR--GKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 400
Cdd:cd03258 160 KVLLCDEATSALDPETTQSIL-ALLRDINRelGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
205-439 |
3.37e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 205 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLsAILEEMH-------LLEG----SVGVQG---SLAYVPQQAWIVSGNIR 270
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFdpqsgriLIDGtdirTVTRASlrrNIAVVFQDAGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMG--GAYDkARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:PRK13657 427 DNIRVGrpDATD-EEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 349 VgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQkmhkeaTSDMLQ 424
Cdd:PRK13657 506 T-----EAKVKAALdelmKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR------AQGMLQ 574
|
250
....*....|....*
gi 1034596369 425 DTAKiAEKPKVESQA 439
Cdd:PRK13657 575 EDER-RKQPAAEGAN 588
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
208-343 |
4.08e-20 |
|
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: 88.09 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRENI 273
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 274 LMGG---AYDKARYLQVLHccslnRDLELLPFGDM--TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:pfam00005 81 RLGLllkGLSKREKDARAE-----EALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
211-391 |
4.43e-20 |
|
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: 89.89 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-----------SLAYVPQQA----WIvsgNIRENI 273
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIagLERPD--SGEILIDGrdvtgvpperrNIGMVFQDYalfpHL---TVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 -----LMGGAYDKARylqvlhccslNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:cd03259 94 afglkLRGVPKAEIR----------ARVRELLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034596369 348 HVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 391
Cdd:cd03259 164 KLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
834-1032 |
5.90e-20 |
|
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: 89.70 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 834 NTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK----LSVIPQDPVLL 909
Cdd:cd03290 13 GLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 910 SGTIRFNL---DPFDRHTDQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEAT 986
Cdd:cd03290 92 NATVEENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034596369 987 ASIDME-TDTLIQRTIREAFQG--CTVLVIAHRVTTVLNCDHILVMGNG 1032
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
208-391 |
7.57e-20 |
|
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: 87.84 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpQQAWIVSGNIRENIlmGGAYDKARYlqv 287
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRI--GYLPEEPSL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 288 lhccslnrdlellpFGDMTeiGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKK-TLRGKT 366
Cdd:cd03230 85 --------------YENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElKKEGKT 147
|
170 180
....*....|....*....|....*.
gi 1034596369 367 VVLVTHQLQYLE-FCGQIILLENGKI 391
Cdd:cd03230 148 ILLSSHILEEAErLCDRVAILNNGRI 173
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
489-796 |
8.68e-20 |
|
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: 91.12 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 489 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSsresngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 568
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQE------------------HGQVYLSVLGALAILQGITVFQYSMAVSIG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 569 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 648
Cdd:cd18559 66 GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 649 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLfLSSTRWMA 728
Cdd:cd18559 145 PLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPS-IVYLRALA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 729 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 796
Cdd:cd18559 224 VRLWCVGPCIVLFASFFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
17-119 |
1.08e-19 |
|
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: 90.61 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 17 DQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIP---TVAT-AVWVLIhtSLKLK 92
Cdd:cd18595 173 DERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPflvSLATfATYVLS--DPDNV 250
|
90 100
....*....|....*....|....*..
gi 1034596369 93 LTASMAFSMLASLNLLRLSVFFVPIAV 119
Cdd:cd18595 251 LDAEKAFVSLSLFNILRFPLSMLPMVI 277
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
208-391 |
1.18e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.95 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLL-------EGSVGVQG-----------------SLAYVPQQAW 263
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLL-------NILggldrptSGEVLIDGqdisslserelarlrrrHIGFVFQFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 IVSG-NIRENILMGGAYDKARYLQvlhccSLNRDLELLpfgDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYL 337
Cdd:COG1136 97 LLPElTALENVALPLLLAGVSRKE-----RRERARELL---ERVGLGDR-LDhrpsqLSGGQQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 338 LDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLEFCGQIILLENGKI 391
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLEllrELNRE--LGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
837-1047 |
1.29e-19 |
|
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: 89.03 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGVDICSIGlEDLRSKLSV-----IPQ--- 904
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIgrtfqIPRlfp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 -----DPVLLSGTIR----FNLDPFDRH---TDQQIWDALERTFLTKaiskfpkKLHTDVvengGNFSVGERQLLCIARA 972
Cdd:cd03219 89 eltvlENVMVAAQARtgsgLLLARARREereARERAEELLERVGLAD-------LADRPA----GELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 973 VLRNSKIILIDEATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1047
Cdd:cd03219 158 LATDPKLLLLDEPAAGLnPEETEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
199-448 |
1.44e-19 |
|
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: 89.91 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 199 EEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHlLEGSVGVQG-------------SLAYVPQQAWIV 265
Cdd:cd03289 14 EGGNAV---LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 266 SGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:cd03289 90 SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 346 DAhvgkhIFEECIKKTLR----GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIqkmhkeATSD 421
Cdd:cd03289 170 DP-----ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI------SPSD 238
|
250 260 270
....*....|....*....|....*....|..
gi 1034596369 422 MLQ-----DTAKIAEKPKVESQALATSLEESL 448
Cdd:cd03289 239 RLKlfprrNSSKSKRKPRPQIQALQEETEEEV 270
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
202-416 |
1.49e-19 |
|
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: 89.58 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 202 NSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGN 268
Cdd:cd03288 31 NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:cd03288 111 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 349 VgKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELM-QKKGKYAQLIqKMHK 416
Cdd:cd03288 191 T-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV-RTDK 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
834-1042 |
1.63e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 834 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGlEDLRSKLSVIPQD----PV 907
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPEDrkgeGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LLSGTIRFN-----LDPFDRHtdQQIWDALERTFLTKAISKF---PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKI 979
Cdd:COG1129 342 VLDLSIRENitlasLDRLSRG--GLLDRRRERALAEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVL-NCDHILVMGNGKVV-EFDRPEV 1042
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
837-1029 |
2.99e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFR------------LVEPMAGRILidgvdicsigledlrsklsVIPQ 904
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTL----LRaiaglwpygsgrIARPAGARVL-------------------FLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DPVLLSGTIRFNL---DPFDRHTDQQIWDALERTFLTKAISKFpkklhtDVVENGGN-FSVGERQLLCIARAVLRNSKII 980
Cdd:COG4178 434 RPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAERL------DEEADWDQvLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034596369 981 LIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVM 1029
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
822-1036 |
3.23e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 90.25 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS-- 897
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 898 -KLSVIPQDPVLLSG-TIRFN------LDPFDR-HTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLC 968
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNvalpleLAGTPKaEIKARVTELLELVGLSDKADRYPAQL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 969 IARAVLRNSKIILIDEATASIDMET-----DTL--IQRTIreafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
832-1033 |
4.58e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 86.76 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 832 RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG 911
Cdd:COG4133 12 RGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 -TIRFNLDpF------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:COG4133 90 lTVRENLR-FwaalygLRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 985 ATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRvTTVLNCDHILVMGNGK 1033
Cdd:COG4133 158 PFTALDAAGVALLAELIAAhLARGGAVLLTTHQ-PLELAAARVLDLGDFK 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
837-1042 |
4.81e-19 |
|
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: 87.49 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKL---SV---------IPQ 904
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARARLrarHVgfvfqsfqlLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 ----DPVLLSGTIRFNLDPFDRHTdqqiwDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKII 980
Cdd:COG4181 105 ltalENVMLPLELAGRRDARARAR-----ALLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 981 LIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEV 1042
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
1-131 |
8.24e-19 |
|
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: 88.05 E-value: 8.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:cd18593 159 FGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILF 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 81 VWVLIHTSLKLKLTASMAFSMLASLNLLRLSV-FFVPIAVKGLTNSKSAVMR 131
Cdd:cd18593 239 LTFLAYILLGNILTAERVFVTMALYNAVRLTMtLFFPFAIQFGSELSVSIRR 290
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
2-131 |
1.22e-18 |
|
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: 88.06 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 2 TRMAvKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAV 81
Cdd:cd18591 179 RKLS-KNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTLV 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 82 WVLIHTSLKLK-LTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 131
Cdd:cd18591 258 TFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
838-1053 |
1.49e-18 |
|
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: 85.85 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLLSG-TIRFN 916
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPFDRHtdqQIWDALERTFLTKAISKFpkkLHTDVVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET- 993
Cdd:cd03299 92 IAYGLKK---RKVDKKEIERKVLEIAEM---LGIDHLLNrkPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTk 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 994 DTLIQ--RTIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1053
Cdd:cd03299 166 EKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
208-400 |
1.89e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.28 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQGSLAYV---PQQAWIvsG------------NIR 270
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIagLE--TPDSGRIVLNGRDLFTnlpPRERRV--GfvfqhyalfphmTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMG---GAYDKARYLQVLHccslnrdlELLPFGDMTEIGER--GlNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:COG1118 94 ENIAFGlrvRPPSKAEIRARVE--------ELLELVQLEGLADRypS-QLSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 346 DAHVgkhifeeciKKTLR----------GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:COG1118 165 DAKV---------RKELRrwlrrlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
838-1037 |
1.94e-18 |
|
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: 84.94 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIrGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG-TIRFN 916
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPF-------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASI 989
Cdd:cd03264 93 LDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034596369 990 DMETDTLIQRTIREAFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEF 1037
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
208-400 |
2.40e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 85.31 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHLL------EGSVGVQGSLAYVP---------------QQAWIVS 266
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLR-LLNRLNDLipgapdEGEVLLDGKDIYDLdvdvlelrrrvgmvfQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 267 GNIRENILMGgaydkarylQVLHCCSLNRDL-----ELLPFGDMT-EIGER--GLNLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:cd03260 95 GSIYDNVAYG---------LRLHGIKLKEELderveEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 339 DDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSEL 400
Cdd:cd03260 166 DEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGRLVEFGPTEQI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
837-1053 |
2.86e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPvllsgTIRFN 916
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LD----------P----FDRHTD---QQIWDALERTfltkAISKFPKKLHTDVvenggnfSVGERQLLCIARAVLRNSKI 979
Cdd:PRK09536 92 FDvrqvvemgrtPhrsrFDTWTEtdrAAVERAMERT----GVAQFADRPVTSL-------SGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 980 ILIDEATASIDM----ETDTLIQRTIREafqGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE-VLrkKPGS 1049
Cdd:PRK09536 161 LLLDEPTASLDInhqvRTLELVRRLVDD---GKTAVAAIHD----LDlaaryCDELVLLADGRVRAAGPPAdVL--TADT 231
|
....
gi 1034596369 1050 LFAA 1053
Cdd:PRK09536 232 LRAA 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
208-390 |
3.38e-18 |
|
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: 83.39 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG---------------SLAYVPQQAWIVSG-NI 269
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIagLEE--PDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENILMGgaydkarylqvlhccslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:cd03229 94 LENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034596369 350 GKHIFEECikKTLR---GKTVVLVTHQLQYLE-FCGQIILLENGK 390
Cdd:cd03229 136 RREVRALL--KSLQaqlGITVVLVTHDLDEAArLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
206-401 |
3.54e-18 |
|
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: 85.04 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRE 271
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NI-----LMGgaYDKARYLQvlhccslnRDLELLPFGDMTEIGERGL---NLSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:cd03295 95 NIalvpkLLK--WPKEKIRE--------RADELLALVGLDPAEFADRyphELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 344 AVDAHVGKHIFEECIK-KTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELM 401
Cdd:cd03295 165 ALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
838-1043 |
5.53e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.70 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE--P---MAGRILIDGVDI--CSIGLEDLRSKLSVIPQDPVLLS 910
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 GTIRFN----------LDPfdRHTDQQIWDALERTFL---TKAiskfpkKLHtdvvENGGNFSVGERQLLCIARAVLRNS 977
Cdd:COG1117 106 KSIYDNvayglrlhgiKSK--SELDEIVEESLRKAALwdeVKD------RLK----KSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 978 KIILIDEATASID-METDTlIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVVEFDRPEVL 1043
Cdd:COG1117 174 EVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
208-402 |
5.72e-18 |
|
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: 84.48 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS----------------LAYVPQQ-AWIVSGNIR 270
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENI----LMGGAYDKARY----LQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPL 342
Cdd:cd03261 96 ENVafplREHTRLSEEEIreivLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 343 SAVDAhVGKHIFEECI---KKTLrGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELMQ 402
Cdd:cd03261 165 AGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
204-426 |
1.00e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.41 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 204 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 270
Cdd:PLN03130 1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV----D 346
Cdd:PLN03130 1331 FNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdvrtD 1410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 347 AHVGKHIFEEcikktLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGkyaqliqkmhkEATSDMLQDT 426
Cdd:PLN03130 1411 ALIQKTIREE-----FKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG-----------SAFSKMVQST 1474
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
837-1044 |
1.10e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL-----LSG 911
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpftVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 TIRFNLDPF--DRHTDQQIWD-ALERtfltkaiskfpkklhTDVVENGGNF----SVGERQLLCIARaVL-------RNS 977
Cdd:PRK13548 96 VVAMGRAPHglSRAEDDALVAaALAQ---------------VDLAHLAGRDypqlSGGEQQRVQLAR-VLaqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 978 KIILIDEATASIDM--ETDTLiqRTIRE--AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRP-EVLR 1044
Cdd:PRK13548 160 RWLLLDEPTSALDLahQHHVL--RLARQlaHERGLAVIVVLHD----LNlaaryADRIVLLHQGRLVADGTPaEVLT 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
206-402 |
1.63e-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: 87.27 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSL-------------------AYVPQQA---- 262
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALAL---MGLLPHGGRISGEVlldgrdllelsealrgrriGMVFQDPmtql 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 263 --WIVSGNIRE---NILMGGAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYL 337
Cdd:COG1123 97 npVTVGDQIAEaleNLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 338 LDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 402
Cdd:COG1123 166 ADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
545-1044 |
1.66e-17 |
|
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: 87.16 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 545 LVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEqFLV 624
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 625 LSLMVIAVLLIVSVLSPYILLMGAIIMVIC-FIYYMMFKKAIGVFKRL-ENYSRspLFSHILNSLQG-----LSSihvyG 697
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTLVLLGLGvAGYRLLVRRARRHLRRArEAEDR--LFKHFRALLEGfkelkLNR----R 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 698 KTEDFISQfkRLTDAQNNYLLLFLSSTRWMALrLEIMTN---LVTLAVALFVAFGISSTPYS----------FKVMAVNI 764
Cdd:COG4615 205 RRRAFFDE--DLQPTAERYRDLRIRADTIFAL-ANNWGNllfFALIGLILFLLPALGWADPAvlsgfvlvllFLRGPLSQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 765 VLQLASSFqATARIgleteaqftAVERILQyMKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYR---DNTPTVLHG 841
Cdd:COG4615 282 LVGALPTL-SRANV---------ALRKIEE-LELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPgedGDEGFTLGP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLlsgtirFN--LDP 919
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHL------FDrlLGL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 920 FDRHTDQQIWDALERtfLtkaiskfpkKLHTDV-VENGG----NFSVGERQLLCIARAVLRNSKIILIDEATASIDMEtd 994
Cdd:COG4615 425 DGEADPARARELLER--L---------ELDHKVsVEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPE-- 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 995 tliqrtIREAF----------QGCTVLVIAH-----RVttvlnCDHILVMGNGKVVEFDRPEVLR 1044
Cdd:COG4615 492 ------FRRVFytellpelkaRGKTVIAISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
206-374 |
1.82e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--SLAYVPQQ---AWIVSGNIRENILMG---- 276
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 -------GAYDKARYLQVLHCCSLnRDLELLPFGDmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:NF040873 86 rglwrrlTRDDRAAVDDALERVGL-ADLAGRQLGE----------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*
gi 1034596369 350 GKHIFEECIKKTLRGKTVVLVTHQL 374
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDL 179
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
208-404 |
2.00e-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: 82.38 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQG-------------SLAYVPQQAW--IVSGNI 269
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL---NGLLkptSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENIL-----MGGAYDKARyLQVLHCcslnrdLELLpfgDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:COG1122 94 EEDVAfgpenLGLPREEIR-ERVEEA------LELV---GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 344 AVDAHvGKHIFEECIKK-TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQKK 404
Cdd:COG1122 164 GLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
837-1041 |
2.22e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIR- 914
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 915 ---FNLDPFDRH------TDQQIWD-ALERTfltkAISKFPKKLHTDVvenggnfSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:PRK11231 96 lvaYGRSPWLSLwgrlsaEDNARVNqAMEQT----RINHLADRRLTDL-------SGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 985 ATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE 1041
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRElNTQGKTVVTVLHD----LNqasryCDHLVVLANGHVMAQGTPE 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
208-404 |
2.26e-17 |
|
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: 82.62 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS----------------LAYVPQQAWIVSG-NIR 270
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQFNLIERlSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMG------------GAYDKARYLQVLHCcsLNRdLELLPFgdmteIGERGLNLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:cd03256 97 ENVLSGrlgrrstwrslfGLFPKEEKQRALAA--LER-VGLLDK-----AYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 339 DDPLSAVD---AHVGKHIFEEcIKKTlRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQKK 404
Cdd:cd03256 169 DEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
825-1045 |
3.12e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.36 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 825 QDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVI 902
Cdd:PRK13636 9 EELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 903 PQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAV 973
Cdd:PRK13636 88 FQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-----------SFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 974 LRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTV-LNCDHILVMGNGKVV-------EFDRPEVL 1043
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVIlqgnpkeVFAEKEML 236
|
..
gi 1034596369 1044 RK 1045
Cdd:PRK13636 237 RK 238
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
208-402 |
3.76e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 82.16 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhLLE----GSVGVQGS-------------LAYVPQQA-------W 263
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALA----GLErpwsGEVTFDGRpvtrrrrkafrrrVQMVFQDPyaslhprH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 IVSGNIRENI-LMGGAYDKARYLQVLHCCSLNRDLellpfgdmteigergLN-----LSGGQKQRISLARAVYSDRQIYL 337
Cdd:COG1124 97 TVDRILAEPLrIHGLPDREERIAELLEQVGLPPSF---------------LDryphqLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 338 LDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYLEF-CGQIILLENGKICENGTHSELMQ 402
Cdd:COG1124 162 LDEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
837-1035 |
4.36e-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: 80.67 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVdicSIGLEDLRSKLSVIPQDPVLlsgtir 914
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDIL------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 915 fnldpfdrHTDQQIWDALERTFLTKAISKfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASIDMETD 994
Cdd:cd03213 94 --------HPTLTVRETLMFAAKLRGLSG------------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034596369 995 TLIQRTIRE-AFQGCTVLVIAHRVTTVL--NCDHILVMGNGKVV 1035
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
208-372 |
4.41e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.44 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSV--------GVQGSLAYVPQQA----WIvsgNIRENI 273
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIagLEK--PTSGEVlvdgkpvtGPGPDRGVVFQEPallpWL---TVLDNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMG---------GAYDKARYLqvlhccslnrdLELLpfgdmteigerGL---------NLSGGQKQRISLARAVYSDRQI 335
Cdd:COG1116 102 ALGlelrgvpkaERRERAREL-----------LELV-----------GLagfedayphQLSGGMRQRVAIARALANDPEV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034596369 336 YLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTH 372
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTH 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
199-448 |
1.05e-16 |
|
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: 85.73 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 199 EEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHlLEGSVGVQG-------------SLAYVPQQAWIV 265
Cdd:TIGR01271 1229 EAGRAV---LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 266 SGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 346 DAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHK-EATSDMLQ 424
Cdd:TIGR01271 1385 DP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRlKLFPLHRR 1463
|
250 260
....*....|....*....|....
gi 1034596369 425 DTAKIAEKPKVesQALATSLEESL 448
Cdd:TIGR01271 1464 NSSKRKPQPKI--TALREEAEEEV 1485
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
211-391 |
1.62e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 79.22 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMHlleGSVGVQG----------SLAYVPQ--QAWIVSGNIRENILM 275
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLakiLAGLIKESS---GSILLNGkpikakerrkSIGYVMQdvDYQLFTDSVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 G---GAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH---- 348
Cdd:cd03226 96 GlkeLDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmer 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034596369 349 VGKhIFEECikkTLRGKTVVLVTHQLQYL-EFCGQIILLENGKI 391
Cdd:cd03226 165 VGE-LIREL---AAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
837-1056 |
1.85e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLR-SKLSVIPQDP----VLLSG 911
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrgLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 TIRFNLDpFDRHTDQQI-------WDALeRTFLTKAISKF---PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIIL 981
Cdd:COG3845 352 SVAENLI-LGRYRRPPFsrggfldRKAI-RAFAEELIEEFdvrTPGPDTPA----RSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 982 IDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPEVLRKKPGslfaALMA 1056
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREEIG----LLMA 499
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
208-396 |
2.00e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLL----------SAILEEMHLLEGSVGVQGSLA-----------YVPQQAWIVS 266
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdKSAGSHIELLGRTVQREGRLArdirksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 267 G-NIRENILMGGAYDKARYLQVLHCCSLNRDLELLPfgDMTEIG------ERGLNLSGGQKQRISLARAVYSDRQIYLLD 339
Cdd:PRK09984 100 RlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQ--ALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 340 DPLSAVDAHVGKHIFEecikkTLR------GKTVVLVTHQLQY-LEFCGQIILLENGKICENGT 396
Cdd:PRK09984 178 EPIASLDPESARIVMD-----TLRdinqndGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
215-397 |
2.13e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 215 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslAYVPQQAWIVSGNI---------------RENILMGGAY 279
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARARIgvvpqfdnldleftvRENLLVFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 dkarylqvlhcCSLN-RDLE-----LLPFGDM-TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKH 352
Cdd:PRK13536 142 -----------FGMStREIEavipsLLEFARLeSKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARH 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034596369 353 IFEECIKKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KICENGTH 397
Cdd:PRK13536 210 LIWERLRSLLaRGKTILLTTHFMEEAErLCDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
827-1041 |
2.16e-16 |
|
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: 79.51 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 827 YHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLeDLRSKLSVI--PQ 904
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGylPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DPVLLSG-TIRFNLDPfdrhtdqqiwdALERTFLTKAISKfpKKL-------HTDVVEN--GGNFSVGERQLLCIARAVL 974
Cdd:cd03218 83 EASIFRKlTVEENILA-----------VLEIRGLSKKERE--EKLeelleefHITHLRKskASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 975 RNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1041
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPE 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
206-400 |
4.88e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.92 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-----------SLAYVPQQ-AWIVSGNIRENI 273
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMGgaydkaryLQVLHCCSL-------NRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:cd03296 96 AFG--------LRVKPRSERppeaeirAKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 346 DAHVGKHifeecIKKTLR------GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:cd03296 168 DAKVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
839-1047 |
1.00e-15 |
|
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: 78.45 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS----KLSVIPQDPVLLSG-TI 913
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RFN---------LDPFDRHtdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:cd03294 120 LENvafglevqgVPRAERE--ERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 985 ATASIdmetDTLIQRTIREAF------QGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKP 1047
Cdd:cd03294 187 AFSAL----DPLIRREMQDELlrlqaeLQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
208-402 |
1.06e-15 |
|
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: 77.47 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQGS--------------LAYVPQQAWIVSG-NI 269
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MGLLpprSGSIRFDGRditglppheraragIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENILMG---GAYDKARYlqvlhccSLNRDLELLPfgdmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDP- 341
Cdd:cd03224 93 EENLLLGayaRRRAKRKA-------RLERVYELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPs 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 342 --LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 402
Cdd:cd03224 161 egLAPK---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
208-395 |
1.07e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.19 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLayvpqqAWIVSGNI--------RENILMGGAy 279
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSLLGLGGgfnpeltgRENIYLNGR- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 dkarylqvLHCCSLNRDLELLPF-GDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvgkhiF 354
Cdd:cd03220 111 --------LLGLSRKEIDEKIDEiIEFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA-----F 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034596369 355 -EECIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENG 395
Cdd:cd03220 178 qEKCQRRlrelLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
838-1036 |
1.12e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSgt 912
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 913 irfNLDPFD---------------RHTDQQIWDALERTFLTKAISkfpKKLHTDvvenGGNFSVGERQLLCIARAVLRNS 977
Cdd:PRK14247 96 ---NLSIFEnvalglklnrlvkskKELQERVRWALEKAQLWDEVK---DRLDAP----AGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVVE 1036
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVE 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
831-1035 |
1.23e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.55 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 831 YRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKLSVIPQD 905
Cdd:PRK13637 12 YMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 906 P--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFLT----KAISKFpkklhtdvvenggNFSVGERQLLCIARA 972
Cdd:PRK13637 92 PeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLDyedyKDKSPF-------------ELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 973 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
208-387 |
1.31e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGV----------QGSLAYVPQQA---WIVSgNIRENIL 274
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptrqalqKNLVAYVPQSEevdWSFP-VLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 MGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI 353
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034596369 354 FEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLE 387
Cdd:PRK15056 182 IS--LLRELRdeGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
208-402 |
1.43e-15 |
|
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: 81.10 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemHLLE---GSVGVQG----------------SLAYVPQQ------- 261
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLL---GLLRptsGSILFDGkdltklsrrslrelrrRVQMVFQDpysslnp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 262 ----AWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRD-LELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIY 336
Cdd:COG1123 358 rmtvGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 337 LLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 402
Cdd:COG1123 427 ILDEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVvRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
843-1049 |
1.91e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 843 NLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS----KLSVIPQDPVLLSGTIRFNLD 918
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 919 PFD--------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID 990
Cdd:PRK10070 128 AFGmelaginaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 991 METDTLIQRTI--REAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGS 1049
Cdd:PRK10070 197 PLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
208-402 |
2.32e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.08 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQ-----AWIVsgni 269
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHsslafPFTV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENILMG-------GAYDKARYLQVLHCCslnrdlellpfgDMTEIGERG-LNLSGGQKQRISLARA-------VYSDRQ 334
Cdd:COG4559 93 EEVVALGraphgssAAQDRQIVREALALV------------GLAHLAGRSyQTLSGGEQQRVQLARVlaqlwepVDGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 335 IYLLDDPLSAVD-AHvgKHIFEECIKK-TLRGKTVVLVTHQL----QYlefCGQIILLENGKICENGTHSELMQ 402
Cdd:COG4559 161 WLFLDEPTSALDlAH--QHAVLRLARQlARRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVLT 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
837-1035 |
2.44e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI--------CSIGLEDLRSKLSVIPQDPVL 908
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 LSGTIrfnldpfDRHTDQQIW--DALERTFLTKAISKFPKK--LHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:PRK09700 99 ENLYI-------GRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 985 ATASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:PRK09700 172 PTSSLtNKEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
825-1041 |
3.78e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 825 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 904
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DP--VLLSGTIR----FNLD----PFDRHTdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 974
Cdd:PRK13635 89 NPdnQFVGATVQddvaFGLEnigvPREEMV-ERVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 975 RNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 1041
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
828-1039 |
4.14e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.91 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 828 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPV 907
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LLSGTIRFNLD-PF----DRHTDQQIWDALER-----TFLTKAISKfpkklhtdvvenggnFSVGERQLLCIARAVLRNS 977
Cdd:PRK10247 92 LFGDTVYDNLIfPWqirnQQPDPAIFLDDLERfalpdTILTKNIAE---------------LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 978 KIILIDEATASIDMETDT----LIQRTIREafQGCTVLVIAHRVTTVLNCDHILV----MGNGKVVEFDR 1039
Cdd:PRK10247 157 KVLLLDEITSALDESNKHnvneIIHRYVRE--QNIAVLWVTHDKDEINHADKVITlqphAGEMQEARYEL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
839-1042 |
4.97e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLgM-ALFRLVEPMAGRILIDG--VDICS--------IGLedlrsklsvIPQDPV 907
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSprdaialgIGM---------VHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 L-------------LSGTIRFNLDpfdrhtdqqiWDALERtfLTKAISK---FPKKLHTDVvengGNFSVGERQLLCIAR 971
Cdd:COG3845 91 LvpnltvaenivlgLEPTKGGRLD----------RKAARA--RIRELSErygLDVDPDAKV----EDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 972 AVLRNSKIILIDEATASI-DMETDTLIqRTIRE-AFQGCTVLVIAHR---VTTVlnCDHILVMGNGKVV-EFDRPEV 1042
Cdd:COG3845 155 ALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKlreVMAI--ADRVTVLRRGKVVgTVDTAET 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
211-395 |
7.30e-15 |
|
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: 74.85 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQA-------WIVSG 267
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDPmsslnprMTIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 268 NIRENILMGGAYDKARYLQVLhccsLNRDLELLPfgdmteIGERGLN-----LSGGQKQRISLARAVYSDRQIYLLDDPL 342
Cdd:cd03257 104 QIAEPLRIHGKLSKKEARKEA----VLLLLVGVG------LPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 343 SAVDAHVGKHIFEEcIK--KTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENG 395
Cdd:cd03257 174 SALDVSVQAQILDL-LKklQEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
208-400 |
7.92e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.06 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG-----------SLAYVPQqawivSG------N 268
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFET--PDSGRILLDGrdvtglppekrNVGMVFQ-----DYalfphlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENI---LMGGAYDKARYLQvlhccslnRDLELLpfgDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLDDP 341
Cdd:COG3842 94 VAENVafgLRMRGVPKAEIRA--------RVAELL---ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 342 LSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:COG3842 163 LSALDAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
838-1032 |
8.18e-15 |
|
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: 76.05 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsKLSVIPQDPVLLSGTIRFNL 917
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 918 ---DPFDRHTDQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETD 994
Cdd:cd03291 119 ifgVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 995 tliqrtiREAFQGC--------TVLVIAHRVTTVLNCDHILVMGNG 1032
Cdd:cd03291 196 -------KEIFESCvcklmankTRILVTSKMEHLKKADKILILHEG 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
211-402 |
1.02e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.79 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMhllEGSVGVQG-SLAYVPQQAWIVS-----GN------IRENILM 275
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIagfLPPD---SGRILWNGqDLTALPPAERPVSmlfqeNNlfphltVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 G-------GAYDKARYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-- 346
Cdd:COG3840 95 GlrpglklTAEQRAQVEQALERVGLAGLLDRLP-------GQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 347 -----AHVGKHIFEEcikktlRGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELMQ 402
Cdd:COG3840 164 lrqemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
838-1032 |
1.90e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 74.01 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILID----GVDICSIG---LEDLRSK--------LSVI 902
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 903 PQ--------DPVLLSGT-------------IRFNLDpfdrhtdQQIWDALERTFltkaiskfpkklhtdvvenggnfSV 961
Cdd:COG4778 106 PRvsaldvvaEPLLERGVdreearararellARLNLP-------ERLWDLPPATF-----------------------SG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 962 GERQLLCIARAVLRNSKIILIDEATASIDMET-DTLIQRtIREA-FQGCTVLVIAH------RVttvlnCDHILVMGNG 1032
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANrAVVVEL-IEEAkARGTAIIGIFHdeevreAV-----ADRVVDVTPF 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
530-749 |
1.92e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 75.28 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 530 DLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLE 609
Cdd:cd07346 28 DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 610 QLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQG 689
Cdd:cd07346 108 AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 690 LSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 749
Cdd:cd07346 188 IRVVKAFAAEEREIERFREANRD---LRDANLRAARLSALFSPLIGLLTALGTALVLLYG 244
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
211-400 |
1.94e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 73.69 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVG---------------VQGSLAYVPQqawivsgnirENILM 275
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKML---TGELRPTSGtayingysirtdrkaARQSLGYCPQ----------FDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 GG--AYDKARYLQVLHCCSLN----------RDLELLPFGDmTEIGerglNLSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:cd03263 88 DEltVREHLRFYARLKGLPKSeikeevelllRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 344 AVDaHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEF-CGQIILLENGKICENGTHSEL 400
Cdd:cd03263 163 GLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
844-1035 |
1.94e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 73.30 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 844 LTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSigLEDLRSKLSVIPQDPVL-----------LSGT 912
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLfahltveqnvgLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 913 IRFNLDPFDRhtdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID-- 990
Cdd:cd03298 97 PGLKLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDpa 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034596369 991 --METDTLIQRTIREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVV 1035
Cdd:cd03298 163 lrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
822-1035 |
2.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.74 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNT----PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLR 896
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 897 SKLSVIPQDP------VLLSGTIRF---NLDPFDRHTDQQIWDALERTFLTKaISKFPKKLhtdvvenggnFSVGERQLL 967
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYE-YRRHAPHL----------LSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 968 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVV 1035
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
814-1045 |
2.17e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 814 QGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 893
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 894 DLRSKLSVIPQD-PVLLSGTIRfNLDPFDR---HTDQQIWDALERTFLTKAISKFP-KKLHTDVVENggnFSVGERQLLC 968
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVR-ELVAIGRypwHGALGRFGAADREKVEEAISLVGlKPLAHRLVDS---LSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 969 IARAVLRNSKIILIDEATASIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EF 1037
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIaqgtpaEL 235
|
....*...
gi 1034596369 1038 DRPEVLRK 1045
Cdd:PRK10575 236 MRGETLEQ 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
834-1036 |
2.59e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.31 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 834 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE------PMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 906
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 907 ----VLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKfpkKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILI 982
Cdd:PRK14246 101 pfphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWK---EVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 983 DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
208-391 |
2.67e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.49 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG-----------SLAYVPQQaWIV--SGNIREN 272
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLED--PTSGEILIGGrdvtdlppkdrNIAMVFQS-YALypHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 I-----LMGgaYDKARylqvlhccslnRD------LELLpfgDMTEIGER-GLNLSGGQKQRISLARAVYSDRQIYLLDD 340
Cdd:COG3839 96 IafplkLRK--VPKAE-----------IDrrvreaAELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 341 PLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 391
Cdd:COG3839 160 PLSNLDAKL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
828-1045 |
3.00e-14 |
|
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: 72.56 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 828 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVDICSIGLEDlRSKLSVI--P 903
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 904 QDPVLLSGtIRFNldpfdrhtdqqiwdalerTFLtkaiskfpkklhTDVVEnggNFSVGERQLLCIARAVLRNSKIILID 983
Cdd:cd03217 84 QYPPEIPG-VKNA------------------DFL------------RYVNE---GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 984 EATASIDMETDTLIQRTIRE-AFQGCTVLVIAH--RVTTVLNCDHILVMGNGKVVEFDRPEVLRK 1045
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
837-1040 |
3.10e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.95 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDP---VLLS 910
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 GTIRFNLDPFDRH------TDQQ--IWDALERTFLTKAI-SKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIIL 981
Cdd:PRK10419 106 KTVREIIREPLRHllsldkAERLarASEMLRAVDLDDSVlDKRPPQL-----------SGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 982 IDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEfDRP 1040
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE-TQP 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
208-391 |
3.99e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 72.20 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLlEGSVGVQG----------SLAYVPQQAwIVSGN--IREN 272
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGV-SGEVLINGrpldkrsfrkIIGYVPQDD-ILHPTltVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMggaydkarylqVLHCcslnrdlellpfgdmteigeRGLnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKH 352
Cdd:cd03213 103 LMF-----------AAKL--------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 353 IFeecikKTLR-----GKTVVLVTHQLQYL--EFCGQIILLENGKI 391
Cdd:cd03213 150 VM-----SLLRrladtGRTIICSIHQPSSEifELFDKLLLLSQGRV 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
575-1032 |
4.02e-14 |
|
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: 77.26 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 575 ALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILL-MGAIIMVI 653
Cdd:TIGR01271 156 ALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCgLGFLILLA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 654 CF---IYYMMFK---KAIGVFKRlenysRSPLFSHILNSLQglsSIHVYGKTE------DFISQFKRLTDAQNNYLLLFL 721
Cdd:TIGR01271 236 LFqacLGQKMMPyrdKRAGKISE-----RLAITSEIIENIQ---SVKAYCWEEamekiiKNIRQDELKLTRKIAYLRYFY 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 722 SSTRWMAlrleimtnlvtlavALFVAFgISSTPYS----------FKVMAVNIVLQLASSFQATARIGL--ETEAQFTAV 789
Cdd:TIGR01271 308 SSAFFFS--------------GFFVVF-LSVVPYAlikgiilrriFTTISYCIVLRMTVTRQFPGAIQTwyDSLGAITKI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 790 E--------RILQYmKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDN--------------TPtVLHGINLTIR 847
Cdd:TIGR01271 373 QdflckeeyKTLEY-NLTTTEVEMVNVTASWDEGIGELFEKIKQNNKARKQPNgddglffsnfslyvTP-VLKNISFKLE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 848 GHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsKLSVIPQDPVLLSGTIRFNLD---PFDRHT 924
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIfglSYDEYR 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 925 DQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDtliqrtiREA 1004
Cdd:TIGR01271 518 YTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE-------KEI 587
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034596369 1005 FQGC--------TVLVIAHRVTTVLNCDHILVMGNG 1032
Cdd:TIGR01271 588 FESClcklmsnkTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
208-391 |
4.12e-14 |
|
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: 72.67 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-----------SLAYVPQQ-AWIVSGNIRENI 273
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIagLEEPT--SGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMG-------------GAYDKARYLQVLHCcsLNRdlellpfgdmteigeRGLNLSGGQKQRISLARAVYSDRQIYLLDD 340
Cdd:cd03301 94 AFGlklrkvpkdeideRVREVAELLQIEHL--LDR---------------KPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 341 PLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 391
Cdd:cd03301 157 PLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
208-400 |
4.99e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEE---------------MHLLEGSVGvqgslaYVPQQ-AWIVSGNI 269
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIagLEHqtsghirfhgtdvsrLHARDRKVG------FVFQHyALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENILMG-----------GAYDKARYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:PRK10851 92 FDNIAFGltvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 339 DDPLSAVDAHVGKHifeecIKKTLRGK------TVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:PRK10851 161 DEPFGALDAQVRKE-----LRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
842-1036 |
6.72e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICsIGLEDLRS-KLSVIPQDPV-----------LL 909
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqrisqIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 910 SGTIRFN--LDPFDRhtDQQIWDALERT-FLTKAISKFPKKLHTdvvenggnfsvGERQLLCIARAVLRNSKIILIDEAT 986
Cdd:PRK15112 111 DFPLRLNtdLEPEQR--EKQIIETLRQVgLLPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 987 ASIDMETDTLIQRTIRE--AFQGCT-VLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:PRK15112 178 ASLDMSMRSQLINLMLElqEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
208-396 |
6.90e-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: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLL---SAILE------EMH-----LLEGSVGVQGSLayvpqqawivSGniRENI 273
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLkliAGILEptsgrvEVNgrvsaLLELGAGFHPEL----------TG--RENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMGGAydkarylqvLHCCSLNRDLELLPF-GDMTEIGE------RglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:COG1134 110 YLNGR---------LLGLSRKEIDEKFDEiVEFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 347 AHvgkhiFEE-CIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGT 396
Cdd:COG1134 179 AA-----FQKkCLARirelRESGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
838-1035 |
7.84e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVdicsigledLRSKLS----------VIPQDPV 907
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTpakahqlgiyLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LLSG-TIRFN-LDPFDRHTDqqiwdALERtfLTKAISKFPKKLHTDVveNGGNFSVGERQLLCIARAVLRNSKIILIDEA 985
Cdd:PRK15439 97 LFPNlSVKENiLFGLPKRQA-----SMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 986 TASID-METDTLIQRtIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:PRK15439 168 TASLTpAETERLFSR-IRELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
837-1049 |
8.95e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSKLSVIPQDpvllSGTI--R 914
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-----NDPKVDERLIRQE----AGMVfqQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 915 FNLDP---------FD----RHTDQQIWDALERTFLTKA-----ISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRN 976
Cdd:PRK09493 86 FYLFPhltalenvmFGplrvRGASKEEAEKQARELLAKVglaerAHHYPSEL-----------SGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 977 SKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAH------RVTTVLncdhiLVMGNGKVVEFDRPEVLRKKPGS 1049
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHeigfaeKVASRL-----IFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
828-1044 |
9.04e-14 |
|
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: 71.63 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 828 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdLRSKLSVIPQDPV 907
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 L---LSGtiRFNLDPFDR-------HTDQQIWDALERTFLTKAISKFPKklhtdvvenggNFSVGERQLLCIARAVLRNS 977
Cdd:cd03265 84 VddeLTG--WENLYIHARlygvpgaERRERIDELLDFVGLLEAADRLVK-----------TYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEFDRPEVLR 1044
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
822-1050 |
1.13e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.48 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 901
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDP--VLLSGTIRF--------NLDPFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 971
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYdvafglenHAVPYDE-MHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 972 AVLRNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGS 1049
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
.
gi 1034596369 1050 L 1050
Cdd:PRK13648 236 L 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
211-391 |
1.14e-13 |
|
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: 71.16 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS---------LAYVPQQAwivsgnirenilmgGAY-- 279
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEER--------------GLYpk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 ----DKARYLQVLHCCS----LNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 350
Cdd:cd03269 85 mkviDQLVYLAQLKGLKkeeaRRRIDEWLERLELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 351 KHIFEECIKKTLR-GKTVVLVTHQLQYLE-FCGQIILLENGKI 391
Cdd:cd03269 164 VELLKDVIRELARaGKTVILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
207-403 |
1.24e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 71.60 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 207 ELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-----------LAYVPQQ-AWIVSGNIRENIL 274
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 MGgaydkaryLQVLHCCSLNRDLELLPFGDMTEIGE----RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:cd03299 94 YG--------LKKRKVDKKEIERKVLEIAEMLGIDHllnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 351 KHIFEEcIKKTLR--GKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQK 403
Cdd:cd03299 166 EKLREE-LKKIRKefGVTVLHVTHDFEEAWALAdKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
830-1043 |
1.85e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.07 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 830 KYRDNT--PTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 906
Cdd:PRK13650 13 KYKEDQekYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 907 -----VLLSGTIRFNLD----PFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 977
Cdd:PRK13650 92 nqfvgATVEDDVAFGLEnkgiPHEE-MKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 978 KIILIDEATASIDMETD-TLIQ--RTIREAFQgCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVL 1043
Cdd:PRK13650 160 KIIILDEATSMLDPEGRlELIKtiKGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
208-402 |
1.92e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRENI 273
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 lmggAYDKARYLQvlHCCSLNRDLELLPFGDM-----TEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:PRK11231 98 ----AYGRSPWLS--LWGRLSAEDNARVNQAMeqtriNHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 348 HvgkHIFEecIKKTLR-----GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQ 402
Cdd:PRK11231 172 N---HQVE--LMRLMRelntqGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
208-402 |
2.05e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.28 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEM---HLLEGSVGVQGSLAYV---PQQAWIVSGNIR--------E 271
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEItsgDLIVDGLKVNDPKVDErliRQEAGMVFQQFYlfphltalE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMG-----GAYDKARYLQVLhccslnrdlELLpfgdmTEIG--ERGLN----LSGGQKQRISLARAVYSDRQIYLLDD 340
Cdd:PRK09493 97 NVMFGplrvrGASKEEAEKQAR---------ELL-----AKVGlaERAHHypseLSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 341 PLSAVDAH-------VGKHIFEEcikktlrGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ 402
Cdd:PRK09493 163 PTSALDPElrhevlkVMQDLAEE-------GMTMVIVTHEIGFAEKVAsRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
826-1052 |
2.59e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 826 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 903
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 904 QDP------VLLSGTIRFNL-------DPFDRHTDQQIWDALERTFLTKAISkfpkklhtdvvenggNFSVGERQLLCIA 970
Cdd:PRK13638 84 QDPeqqifyTDIDSDIAFSLrnlgvpeAEITRRVDEALTLVDAQHFRHQPIQ---------------CLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 971 RAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDrpevlrkKPG 1048
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG-------APG 221
|
....
gi 1034596369 1049 SLFA 1052
Cdd:PRK13638 222 EVFA 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
208-373 |
3.08e-13 |
|
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: 68.72 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVG--VQGSLAYVPQQAWIVSGNIREnilmggaydkaryl 285
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGmpEGEDLLFLPQRPYLPLGTLRE-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 286 QVLHccslnrdlellPFGDMteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECikkTLRGK 365
Cdd:cd03223 83 QLIY-----------PWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KELGI 139
|
....*...
gi 1034596369 366 TVVLVTHQ 373
Cdd:cd03223 140 TVISVGHR 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
837-1038 |
3.44e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRL----VEPMAGRILIdGVDIcSIG-----LEDLRSKLSVIPqdpv 907
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVLD---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 llsgTIRfnlDPFDRHTDQQIWDALERtFLtkaiskF-PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEAT 986
Cdd:COG0488 399 ----ELR---DGAPGGTEQEVRGYLGR-FL------FsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 987 ASIDMETDTLIQRTIREaFQGcTVLVIAH------RVttvlnCDHILVMGNGKVVEFD 1038
Cdd:COG0488 461 NHLDIETLEALEEALDD-FPG-TVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
850-1036 |
3.47e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 850 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIG-LEDLRSKLSVIPQDPVLlsgtirfNLDPfdRHT-- 924
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPYA-------SLDP--RQTvg 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 925 ------------------DQQIWDALERTFLTKAIS-KFPKKlhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEA 985
Cdd:PRK10261 422 dsimeplrvhgllpgkaaAARVAWLLERVGLLPEHAwRYPHE-----------FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 986 TASIDMETDTLI-------QRTIREAFqgctvLVIAHRVTTVLNCDH-ILVMGNGKVVE 1036
Cdd:PRK10261 491 VSALDVSIRGQIinllldlQRDFGIAY-----LFISHDMAVVERISHrVAVMYLGQIVE 544
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
206-388 |
4.36e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.43 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLLEGSVGVQGS-----------LAYVPQQAWIVSG-NIR 270
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVLLNGRrltalpaeqrrIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMG------GAYDKARYLQVLhccslnRDLELLPFGD---MTeigerglnLSGGQKQRISLARAVYSDRQIYLLDDP 341
Cdd:COG4136 95 ENLAFAlpptigRAQRRARVEQAL------EEAGLAGFADrdpAT--------LSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 342 LSAVDAH----VGKHIFEEcIKKtlRGKTVVLVTHQLQYLEFCGQIILLEN 388
Cdd:COG4136 161 FSKLDAAlraqFREFVFEQ-IRQ--RGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
837-1053 |
4.47e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.03 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GmalfrLVEPMAGRILIDGVDIcsIGLEDLRSKLSVIPQDPVL--- 908
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV--TDLPPKDRNIAMVFQSYALyph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 LS--GTIRFNL-----DPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIIL 981
Cdd:COG3839 90 MTvyENIAFPLklrkvPKAEI--DRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 982 IDEATASID----METDTLIQRTIREafQGCTVLViahrVT-------TVlnCDHILVMGNGKVVEFDRPEVLRKKPGSL 1050
Cdd:COG3839 157 LDEPLSNLDaklrVEMRAEIKRLHRR--LGTTTIY----VThdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANL 228
|
...
gi 1034596369 1051 FAA 1053
Cdd:COG3839 229 FVA 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
837-1053 |
4.49e-13 |
|
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: 69.96 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsIGLEDLRSKLSVIPQDPVLLSgtirfN 916
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFP-----H 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILID 983
Cdd:cd03300 87 LTVFEniafglrlkklpkAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 984 EATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1053
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
211-400 |
4.92e-13 |
|
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: 69.71 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLS------------AILEEMHLLEGSVGVQGSLAYVPQQAwIVSGNI--RENILM- 275
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKmlttllkptsgrATVAGHDVVREPREVRRRIGIVFQDL-SVDDELtgWENLYIh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 GGAY----DKARylqvlhccslNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:cd03265 98 ARLYgvpgAERR----------ERIDELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 351 KHIFEEcIKKTLR--GKTVVLVTHqlqYLE----FCGQIILLENGKICENGTHSEL 400
Cdd:cd03265 168 AHVWEY-IEKLKEefGMTILLTTH---YMEeaeqLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
826-1045 |
5.74e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 826 DYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 903
Cdd:PRK13639 6 DLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 904 QDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 974
Cdd:PRK13639 85 QNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 975 RNSKIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE-------FDRPEVLRK 1045
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkEGITIIISTHDVDLVpVYADKVYVMSDGKIIKegtpkevFSDIETIRK 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
208-402 |
9.37e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIV-SGNIRENI 273
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMGGA-----YDKARYL--QVLHCCslnrdlellpfgDMTEIGERG-LNLSGGQKQRISLARA------VYSDRQIYLLD 339
Cdd:PRK13548 98 AMGRAphglsRAEDDALvaAALAQV------------DLAHLAGRDyPQLSGGEQQRVQLARVlaqlwePDGPPRWLLLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 340 DPLSAVD-AHvGKHIFEecIKKTL---RGKTVVLVTHQL----QYlefCGQIILLENGKICENGTHSELMQ 402
Cdd:PRK13548 166 EPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
837-1041 |
9.38e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL-EDLRSKLSVIPQDPvllsgTIRF 915
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEA-----SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 916 NLDPFDR-HTDQQIWDALERTFLTKAISKFPKKLHTDVVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME 992
Cdd:PRK10895 92 RLSVYDNlMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 993 TDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1041
Cdd:PRK10895 172 SVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPT 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
206-375 |
9.90e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.34 E-value: 9.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVP---------QQAWIVSGNIRENILMG 276
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 ---GAYDKARYLQVLHccslnrdlELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKH 352
Cdd:PRK11248 95 lqlAGVEKMQRLEIAH--------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....
gi 1034596369 353 IFEECIKKTLR-GKTVVLVTHQLQ 375
Cdd:PRK11248 167 MQTLLLKLWQEtGKQVLLITHDIE 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
221-391 |
1.06e-12 |
|
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: 68.48 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 221 LGVCGNTGSGKSSLLSAI------------LEEMHLLEGSVGV-----QGSLAYVPQQAWIVSG-NIRENILMGgaydka 282
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIaglekpdggtivLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHlNVRENLAFG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 283 rylqvLHCCSLNRDL----ELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC 357
Cdd:cd03297 100 -----LKRKRNREDRisvdELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034596369 358 --IKKTLRGkTVVLVTHQLQYLEF-CGQIILLENGKI 391
Cdd:cd03297 175 kqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
208-404 |
1.07e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAileeMHLLE----GSVGVQGS---LAYVPQQAWIVSgnIRENILM-GGAY 279
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLEmprsGTLNIAGNhfdFSKTPSDKAIRE--LRRNVGMvFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 DKARYLQVLH------CCSL--------NRDLELLPFGDMTEIGER-GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:PRK11124 92 NLWPHLTVQQnlieapCRVLglskdqalARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 345 VDAHVGKHIFEecIKKTLR--GKTVVLVTHQlqyLEFCGQI----ILLENGKICENGTHSELMQKK 404
Cdd:PRK11124 172 LDPEITAQIVS--IIRELAetGITQVIVTHE---VEVARKTasrvVYMENGHIVEQGDASCFTQPQ 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
208-393 |
1.15e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.54 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQAWIVSG-NIR 270
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENIL-------MGGAYDKARYLQVLhccslnrdlellpfgDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLD 339
Cdd:COG2884 98 ENVAlplrvtgKSRKEIRRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 340 DPLSAVDAHVGK---HIFEEcIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGKICE 393
Cdd:COG2884 163 EPTGNLDPETSWeimELLEE-INR--RGTTVLIATHDLELVDrMPKRVLELEDGRLVR 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
211-395 |
1.16e-12 |
|
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: 68.37 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMmLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------------LAYVPQQaWIVSGNIRenilmggA 278
Cdd:cd03264 19 VSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQE-FGVYPNFT-------V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 279 YDKARYLQVLHCCS-------LNRDLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 350
Cdd:cd03264 90 REFLDYIAWLKGIPskevkarVDEVLELV---NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 351 KHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENG 395
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
206-396 |
1.42e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMhllEGSVGVQG-------SLAYVPQQAWIVSGNiRENILM 275
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQ---KGKVLVSGidtgdfsKLQGIRKLVGIVFQN-PETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 GGAYDKARYLQVLHCCSlnRDLELLPFGDMTeIGERGL---------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:PRK13644 92 GRTVEEDLAFGPENLCL--PPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 347 AHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 396
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
213-395 |
1.71e-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: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 213 LVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAWIVSGNIRENILMGgaydkarYLQVLHcc 291
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFA-------HLTVEQ-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 292 slNRDLELLPFGDMTE---------IGERGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHV 349
Cdd:cd03298 90 --NVGLGLSPGLKLTAedrqaievaLARVGLAglekrlpgeLSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034596369 350 GKHIFEECIKktlRGKTVVLVTHQLQYLEFCGQ-IILLENGKICENG 395
Cdd:cd03298 168 LDLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
837-1036 |
2.21e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI------------------------CSIGL 892
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkglirqlrqhvgfvfQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 893 EDLRSKLSVIPQDPVLLSGTIRFNLDPFDRhtdqqiwDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 972
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEATARAR-------ELLAKVGLAGKETSYPRRL-----------SGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 973 VLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
833-1035 |
2.37e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 67.68 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 833 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDIcSIGLedLRSKLSVIPQDPVLL 909
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR-KPDQ--FQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 910 SG-----TIRF-NLDPFDRHTDQQIWDALERTFLTKAISkfpkklHTDVvenGGNF----SVGERQLLCIARAVLRNSKI 979
Cdd:cd03234 94 PGltvreTLTYtAILRLPRKSSDAIRKKRVEDVLLRDLA------LTRI---GGNLvkgiSGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVL--NCDHILVMGNGKVV 1035
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHQPRSDLfrLFDRILLLSSGEIV 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
208-391 |
2.55e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 67.17 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQGSLAYVPQQAWIvsgNIRENILM-GGAYDKARY 284
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNIN---ELRQKVGMvFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 285 LQVLHCCSLN-RDLELLPFGDMTEIGERGL--------------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:cd03262 91 LTVLENITLApIKVKGMSKAEAEERALELLekvgladkadaypaQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 350 GKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKI 391
Cdd:cd03262 171 VGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
837-1036 |
2.57e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVlLSGTI 913
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPN-SSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RFN---------------LDPFDRhtDQQIWDALERTFLTKAI-SKFPkklhtdvvengGNFSVGERQLLCIARAVLRNS 977
Cdd:PRK15134 378 RLNvlqiieeglrvhqptLSAAQR--EQQVIAVMEEVGLDPETrHRYP-----------AEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 978 KIILIDEATASIDMETDTLI-------QRTIREAFqgctvLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQIlallkslQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
211-400 |
2.58e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.86 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVP-----------QQAWIVSGNIRENILMGGA 278
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 279 YDKARYLQVLhccslNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC 357
Cdd:PRK11607 118 QDKLPKAEIA-----SRVNEMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034596369 358 IKKTLR-GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:PRK11607 193 VDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
208-401 |
2.92e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------------SLAYVPQQAWIVSG-NIREN 272
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGGAY-DKARYLQvlhccSLNRDLELLPFGDMTEIgERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:PRK11614 101 LAMGGFFaERDQFQE-----RIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 352 HIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 401
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
822-1047 |
3.39e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK 898
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQDP------VLLSGTIRFNLDpfDRHTDQQ-----IWDALERTFLTKAISKFPKklhtdvvenggNFSVGERQLL 967
Cdd:PRK13640 86 VGIVFQNPdnqfvgATVGDDVAFGLE--NRAVPRPemikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 968 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRK 1045
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
..
gi 1034596369 1046 KP 1047
Cdd:PRK13640 233 KV 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
839-1035 |
3.50e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI-CSIGLEDLRSKLSVIPQD-PVLLSGTIRFN 916
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 L--------DPFDRHtdqqiwDALERTflTKAISKfpkKLHTDV--VENGGNFSVGERQLLCIARAVLRNSKIILIDEAT 986
Cdd:PRK10982 94 MwlgryptkGMFVDQ------DKMYRD--TKAIFD---ELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 987 ASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:PRK10982 163 SSLtEKEVNHLftIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
841-1036 |
3.83e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 841 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL---RSKLSVIPQDPvLLSGTIRFNL 917
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 918 -----DPFDRH----TDQQIWDALeRTFLTKA------ISKFPKKlhtdvvenggnFSVGERQLLCIARAVLRNSKIILI 982
Cdd:PRK15079 118 geiiaEPLRTYhpklSRQEVKDRV-KAMMLKVgllpnlINRYPHE-----------FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 983 DEATA----SIDMETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK15079 186 DEPVSaldvSIQAQVVNLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
208-396 |
6.21e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.18 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG----------------SLAYVPQQA---Wi 264
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGvdltalserelraarrKIGMIFQHFnllS- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 265 vSGNIRENI-----LMGgaYDKARYLQvlhccslnRDLELLpfgDMTEIGERGL----NLSGGQKQRISLARAVYSDRQI 335
Cdd:COG1135 96 -SRTVAENValpleIAG--VPKAEIRK--------RVAELL---ELVGLSDKADaypsQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 336 YLLDDPLSAVDAHVGKHIFE---EcIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGT 396
Cdd:COG1135 162 LLCDEATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVrRICDRVAVLENGRIVEQGP 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
211-391 |
7.00e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 66.14 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLLEGSVGVQG----------SLAYVPQQAWIVSG-NIRE----- 271
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDILLPGlTVREtltyt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGGAYDKARYLQVLHCCSLNRDLELLPFGdmteiGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:cd03234 106 AILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034596369 352 HIFEECIKKTLRGKTVVLVTHQ--LQYLEFCGQIILLENGKI 391
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
206-393 |
7.02e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 67.14 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQA------- 262
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 263 ----WIVSGNIRENILMGGAYDKARYLQVLHCCSL-NRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYL 337
Cdd:TIGR02769 105 mtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLP-----------RQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 338 LDDPLSAVDAHVGKHIFEECIKKTLRGKTV-VLVTHQLQYLE-FCGQIILLENGKICE 393
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQsFCQRVAVMDKGQIVE 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
298-400 |
7.69e-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: 66.11 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 298 ELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC--IKKTLrGKTVVLVTH-Q 373
Cdd:cd03300 113 EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrLQKEL-GITFVFVTHdQ 191
|
90 100
....*....|....*....|....*..
gi 1034596369 374 LQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:cd03300 192 EEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
208-389 |
8.10e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEemhlL----EGSVGV--QGSLAYVPQQAWIVSGNIRENIL---MGGA 278
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLypaTAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 279 YDKARYLQVLHCCSLNRdleLLPfgDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcI 358
Cdd:COG4178 455 FSDAELREALEAVGLGH---LAE--RLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-L 528
|
170 180 190
....*....|....*....|....*....|.
gi 1034596369 359 KKTLRGKTVVLVTHQLQYLEFCGQIILLENG 389
Cdd:COG4178 529 REELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
175-403 |
9.41e-12 |
|
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: 66.51 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 175 ALELERNGHASEGMTrprdalgpEEEGNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLE---GSVGV 251
Cdd:cd03294 17 AFKLLAKGKSKEEIL--------KKTGQTVG--VNDVSLDVREGEIFVIMGLSGSGKSTLLRCI---NRLIEptsGKVLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 252 QG------------------------SLAYVPQQawivsgNIRENILMGgaydkaryLQVLHCCSLNRD------LELLP 301
Cdd:cd03294 84 DGqdiaamsrkelrelrrkkismvfqSFALLPHR------TVLENVAFG--------LEVQGVPRAEREeraaeaLELVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 302 FGDMTE--IGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYL 377
Cdd:cd03294 150 LEGWEHkyPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlQAELQKTIVFITHDLdEAL 225
|
250 260
....*....|....*....|....*.
gi 1034596369 378 EFCGQIILLENGKICENGTHSELMQK 403
Cdd:cd03294 226 RLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
833-1037 |
1.01e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 833 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSI---GLEDLRS-KLSVIPQD 905
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekELNKLRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 906 PVLlsgtirfNLDPFDRHTDQ---------------------QIWDALERTFLTKAISKFPKKlhtdvvenggnFSVGER 964
Cdd:PRK09473 106 PMT-------SLNPYMRVGEQlmevlmlhkgmskaeafeesvRMLDAVKMPEARKRMKMYPHE-----------FSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 965 QLLCIARAVLRNSKIILIDEATASIDMETD----TLIQRTIREaFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1037
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
841-1041 |
1.05e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.68 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 841 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG----RILIDGVDICSIGLED----------LRSKLSVIPQDP 906
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDGrgrakryigiLHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 907 VLLSGTIRFNLD-PFDRhtdqqiwdALERTFLTKAISKFPKKLHTDVVEN-GGNFSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:TIGR03269 382 VLDNLTEAIGLElPDEL--------ARMKAVITLKMVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 985 ATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1041
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPE 513
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
837-1018 |
1.14e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.10 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlRSKLSVIPQDPVLLSGTIRfn 916
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQRPYLPLGTLR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 ldpfdrhtdQQI---WDalertfltkaiskfpkklhtDVvenggnFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 993
Cdd:cd03223 82 ---------EQLiypWD--------------------DV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....*
gi 1034596369 994 DTLIQRTIREAfqGCTVLVIAHRVT 1018
Cdd:cd03223 127 EDRLYQLLKEL--GITVISVGHRPS 149
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
839-1034 |
1.14e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.19 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLgmalfrlVEPMAGRILIDGVDICSIGL------------EDLR---------- 896
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTL-------LRHLSGLITGDKSAGSHIELlgrtvqregrlaRDIRksrantgyif 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 897 ------SKLSVIPQdpvLLSGTI------RFNLDPFDRHTDQQIWDALERTfltkAISKFPkklHTDVvengGNFSVGER 964
Cdd:PRK09984 93 qqfnlvNRLSVLEN---VLIGALgstpfwRTCFSWFTREQKQRALQALTRV----GMVHFA---HQRV----STLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 965 QLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
208-402 |
1.24e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSG-NIRENI 273
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQLPAAEGmTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMG--------GAYDKARYLQVLHCCSLnrdLELLPFGdmteigERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:PRK10575 107 AIGrypwhgalGRFGAADREKVEEAISL---VGLKPLA------HRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 345 VD-AHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 402
Cdd:PRK10575 178 LDiAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
489-745 |
1.24e-11 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 66.66 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 489 IIFFFVVLIVFLTIFSFWWLsywleqGSGTN--SSRESNGTMADLGNIAdnPQLSFYQLVYGLNALLLICVGVcssgIFT 566
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLL------GKAIDliIEGLGGGGGVDFSGLL--RILLLLLGLYLLSALFSYLQNR----LMA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 567 KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ-LLPIFSeQFLVLSLMVIAVLLIVSVLSPYILL 645
Cdd:cd18547 71 RVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQaLSQSLT-QLISSILTIVGTLIMMLYISPLLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 646 MGAIIMVICFIYYMMF-KKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA--QNNYLLLFLS 722
Cdd:cd18547 150 IVLVTVPLSLLVTKFIaKRSQKYFRKQQK-ALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEElyKASFKAQFYS 228
|
250 260
....*....|....*....|...
gi 1034596369 723 STRWMALRLeiMTNLVTLAVALF 745
Cdd:cd18547 229 GLLMPIMNF--INNLGYVLVAVV 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
208-391 |
1.32e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLS--AILEEM---HLLEGSvgvqGSLAyvpqqawivsgNIRENI-LMggaYDK 281
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRllAGLETPsagELLAGT----APLA-----------EAREDTrLM---FQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 282 ARYL---QVLHccslNRDLELLpfGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:PRK11247 90 ARLLpwkKVID----NVGLGLK--GQWRDAALQALAavgladranewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 345 VDAhVGKHIFEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKI 391
Cdd:PRK11247 164 LDA-LTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
208-503 |
1.33e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSL----------------AYVPQQ-AWIVSGNIR 270
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFRSPKGVKGSGSVllngmpidakemraisAYVQQDdLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENIL------MGGAYDK----ARYLQVLhccslnRDLELLPFGDmTEIGERGL--NLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:TIGR00955 118 EHLMfqahlrMPRRVTKkekrERVDEVL------QALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 339 DDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFC--GQIILLENGKICENGTHSELMQKKGKYAQLIQKMHK 416
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 417 EAtsDMLQDTAKIAEKPKVESQA-------------LATSLEESLNGNAVPEHQLTQEEEMEEGSlswrvyhhyiqaagG 483
Cdd:TIGR00955 271 PA--DFYVQVLAVIPGSENESREriekicdsfavsdIGRDMLVNTNLWSGKAGGLVKDSENMEGI--------------G 334
|
330 340
....*....|....*....|.
gi 1034596369 484 YMVSCIIFFFVVLI-VFLTIF 503
Cdd:TIGR00955 335 YNASWWTQFYALLKrSWLSVL 355
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
208-395 |
1.48e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWI-VSGNIRENI 273
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMGgaydkarylqvlhccslnRDLELLPFGDMTEIGERGL------------------NLSGGQKQRISLARAVYSDRQI 335
Cdd:PRK09536 99 EMG------------------RTPHRSRFDTWTETDRAAVeramertgvaqfadrpvtSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 336 YLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENG 395
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
839-1052 |
1.98e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP------VLLSGT 912
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnqfvgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 913 IRFNLD----PFDRHTdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATAS 988
Cdd:PRK13642 103 VAFGMEnqgiPREEMI-KRVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 989 IDMETDTLIQRTIREAFQG--CTVLVIAHRVTTVLNCDHILVMGNGKVVEfdrpevlRKKPGSLFA 1052
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIK-------EAAPSELFA 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
822-1043 |
2.40e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 901
Cdd:PRK13647 5 IEVEDLHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 972
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 973 VLRNSKIILIDEATASIDMETdtliQRTIREAF-----QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1043
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILdrlhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
258-412 |
2.82e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 258 VPQQAWIVSGNIRENILMGGayDKARYLQVLHCC---SLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQ 334
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 335 IYLLDDPLSAVDAHVgkhifEECIKKTL------RGKTVVLVTHQLQYLEFCGQIILLEN----GKICE-NGTHSELMQ- 402
Cdd:PTZ00265 1379 ILLLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSv 1453
|
170
....*....|
gi 1034596369 403 KKGKYAQLIQ 412
Cdd:PTZ00265 1454 QDGVYKKYVK 1463
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
208-400 |
2.88e-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: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGV--------------QGSLAYVPQQAWIVSGNI 269
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeaGTIRVgditidtarslsqqKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 R--------ENILMGGAYDKarylQVLHCCSLNRDLELLpfgdmTEIGERG------LNLSGGQKQRISLARAVYSDRQI 335
Cdd:PRK11264 95 NlfphrtvlENIIEGPVIVK----GEPKEEATARARELL-----AKVGLAGketsypRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 336 YLLDDPLSAVDAH-VGKhifeecIKKTLRG-----KTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 400
Cdd:PRK11264 166 ILFDEPTSALDPElVGE------VLNTIRQlaqekRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
208-402 |
3.02e-11 |
|
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: 64.62 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL----------------------EEMHLLEGSVGV--QGSlayvpqqAW 263
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIgllrpdsgeilvdgqditglseKELYELRRRIGMlfQGG-------AL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 IVSGNIRENI----LMGGAYDKA----RYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQI 335
Cdd:COG1127 94 FDSLTVFENVafplREHTDLSEAeireLVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 336 YLLDDPLSAVDAhVGKHIFEECIKKT--LRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQ 402
Cdd:COG1127 163 LLYDEPTAGLDP-ITSAVIDELIRELrdELGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
222-401 |
3.63e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 65.89 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 222 GVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQG-----------------SLAYVPQQAwiv-sgNIRENILMG----- 276
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIagLE--RPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEArlfphlSVRGNLLYGrkrap 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 GAYDKARYLQVLhccslnrdlELLpfgdmtEIG---ERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKH 352
Cdd:COG4148 107 RAERRISFDEVV---------ELL------GIGhllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR-KA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 353 ifeECIK--KTLRGKT---VVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELM 401
Cdd:COG4148 171 ---EILPylERLRDELdipILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
210-404 |
4.05e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 65.90 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 210 KINLVVSKGMMLGVCGNTGSGKSSLLSAI------------LEEMHLLEGSVGVQGS-----LAYVPQQAWIVSG-NIRE 271
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIagltrpdegeivLNGRTLFDSRKGIFLPpekrrIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGGAYDKARYLQVlhccSLNRDLELLPFGDMTEIGERglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:TIGR02142 95 NLRYGMKRARPSERRI----SFERVIELLGIGHLLGRLPG--RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 352 HI--FEECIKKTLRgKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKK 404
Cdd:TIGR02142 169 EIlpYLERLHAEFG-IPILYVSHSLQEVLrLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
207-401 |
4.17e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 207 ELHK----------INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQGS-------------------- 254
Cdd:PRK10619 10 DLHKrygehevlkgVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPS--EGSIVVNGQtinlvrdkdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 255 ------LAYVPQQAWIVSG-NIRENILMGGaydkaryLQVLHCCSLNRDLELLPFGDMTEIGERG-----LNLSGGQKQR 322
Cdd:PRK10619 88 rllrtrLTMVFQHFNLWSHmTVLENVMEAP-------IQVLGLSKQEARERAVKYLAKVGIDERAqgkypVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 323 ISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELM 401
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
208-400 |
4.22e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSG-NIRENILMG---------- 276
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVGMVfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 GAYDKARYLQVLHCCSLNRDLE------LLPFGDMTEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKkiveecLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 347 AhVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 400
Cdd:PRK14246 186 I-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
822-1043 |
5.00e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 64.34 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG---RIL---IDGVDIC----SIG 891
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWelrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 892 L------EDLRSKLSVIpqDpVLLSGtiRFN-LDPFDRHTDQQ------------IWDALERTFLTkaiskfpkklhtdv 952
Cdd:COG1119 82 LvspalqLRFPRDETVL--D-VVLSG--FFDsIGLYREPTDEQrerarellellgLAHLADRPFGT-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 953 venggnFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLV-IAHRVTTVLNC-DHILVM 1029
Cdd:COG1119 143 ------LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLL 216
|
250
....*....|....*
gi 1034596369 1030 GNGKVVEF-DRPEVL 1043
Cdd:COG1119 217 KDGRVVAAgPKEEVL 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
206-391 |
5.08e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 63.58 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG---------SLAYVPQQAWIV--------SGN 268
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGVVfqdfrllpDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENIL--MGGAYDKARYLQ-----VLHCCSLNRDLELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDP 341
Cdd:cd03292 95 VYENVAfaLEVTGVPPREIRkrvpaALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 342 LSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKI 391
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
206-404 |
5.14e-11 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 64.37 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEmhlLEGSVGVQGSLAYVPQQAWivsgNIRENILMggaydka 282
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLLP---TSGKVTVDGLDTLDEENLW----EIRKKVGM------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 283 rYLQvlhccslNRD---------------LELL--PFGDMTEIGERGL--------------NLSGGQKQRISLARAVYS 331
Cdd:TIGR04520 82 -VFQ-------NPDnqfvgatveddvafgLENLgvPREEMRKRVDEALklvgmedfrdrephLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 332 DRQIYLLDDPLSAVDAhVGKhifEEcIKKTLR------GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKK 404
Cdd:TIGR04520 154 RPDIIILDEATSMLDP-KGR---KE-VLETIRklnkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
833-1047 |
5.70e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 833 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL-----VEPMAGRILIDGVDICSIGLEDLR----SKLSVIP 903
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 904 QDPVLlsgtirfNLDPFdrHTDQ--------------------QIWDALERTFLTKA---ISKFPKKLhtdvvenggnfS 960
Cdd:PRK15134 99 QEPMV-------SLNPL--HTLEkqlyevlslhrgmrreaargEILNCLDRVGIRQAakrLTDYPHQL-----------S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 961 VGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1037
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQ 238
|
250
....*....|
gi 1034596369 1038 DRPEVLRKKP 1047
Cdd:PRK15134 239 NRAATLFSAP 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
208-375 |
6.16e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.90 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAiLEEMHLLEGSVGVQGSLAY---------------------VPQQAwivs 266
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLIPGARVEGEILLdgediydpdvdvvelrrrvgmVFQKP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 267 gN-----IRENILMG----GAYDKArylqvlhccslnrdlellpfgDMTEIGER------------------GLNLSGGQ 319
Cdd:COG1117 102 -NpfpksIYDNVAYGlrlhGIKSKS---------------------ELDEIVEEslrkaalwdevkdrlkksALGLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 320 KQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKtLRGK-TVVLVTHQLQ 375
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EELILE-LKKDyTIVIVTHNMQ 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
314-396 |
6.97e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 314 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGK 390
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNE-LKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGR 222
|
....*.
gi 1034596369 391 ICENGT 396
Cdd:PRK09452 223 IEQDGT 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
837-1038 |
7.23e-11 |
|
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: 63.04 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSK---LSVIPQDPVL---LS 910
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKdrdIAMVFQNYALyphMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 G--TIRFNLD--PFDRHT-DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 985
Cdd:cd03301 89 VydNIAFGLKlrKVPKDEiDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 986 TASID----METDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 1038
Cdd:cd03301 158 LSNLDaklrVQMRAELKRLQQR--LGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
208-399 |
7.41e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.82 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG---------SLAYVPQQ-AWI--------- 264
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGqdltalsekELRKARRQiGMIfqhfnllss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 265 --VSGNI----------RENIlmggaydKARYLqvlhccslnrdlELLpfgDMTEIGERGL----NLSGGQKQRISLARA 328
Cdd:PRK11153 97 rtVFDNValplelagtpKAEI-------KARVT------------ELL---ELVGLSDKADrypaQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 329 VYSDRQIYLLDDPLSAVDAHVGKHIFE--ECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSE 399
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSE 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
315-391 |
7.46e-11 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 61.68 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQLQ-YLEFCGQIILLENGKI 391
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaqGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
838-1043 |
7.60e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDPVLLSG-TIRF 915
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 916 NLDPFDRHTD-QQIWDALERTFltkaiSKFPKkLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE-----ATASI 989
Cdd:PRK11614 100 NLAMGGFFAErDQFQERIKWVY-----ELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEpslglAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 990 DMETDTLIQrtIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1043
Cdd:PRK11614 174 QQIFDTIEQ--LRE--QGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
826-1041 |
7.68e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.71 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 826 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIGLE--DLRSK 898
Cdd:PRK14267 9 NLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQDPvllsgtirfnlDPFDRHTdqqIWD----ALERTFLTKAISKFPKKLHT--------DVVEN-----GGNFSV 961
Cdd:PRK14267 87 VGMVFQYP-----------NPFPHLT---IYDnvaiGVKLNGLVKSKKELDERVEWalkkaalwDEVKDrlndyPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 962 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVV 1035
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRVS-----DYVAFLYLGKLI 227
|
250
....*....|...
gi 1034596369 1036 E-------FDRPE 1041
Cdd:PRK14267 228 EvgptrkvFENPE 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
218-373 |
7.74e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.76 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 218 GMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSlaYVPQQAwivsGNIRENIL-------MGGAYDKARYLQVLHc 290
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT--PLAEQR----DEPHENILylghlpgLKPELSALENLHFWA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 291 cSLNRDLELLPFGDMTEIGERGLN------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-R 363
Cdd:TIGR01189 99 -AIHGGAQRTIEDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLaR 176
|
170
....*....|
gi 1034596369 364 GKTVVLVTHQ 373
Cdd:TIGR01189 177 GGIVLLTTHQ 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
839-1033 |
8.07e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDL-RSKLSVIPQDPVLLSG-TI 913
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RFN------LDPFDRhTDqqiWDALER---TFLTKAiskfpkKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:PRK13549 100 LENiflgneITPGGI-MD---YDAMYLraqKLLAQL------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 985 ATASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1033
Cdd:PRK13549 170 PTASLtESETAVLldIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
837-1056 |
8.91e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicSIGLEDLRSKLSVIPQDPVLLsgtirfn 916
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLL------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 ldPFDRHTD-----------QQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 985
Cdd:PRK11247 94 --PWKKVIDnvglglkgqwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 986 TASID----METDTLIQRTIREafQGCTVLVIAHRVT-TVLNCDHILVMGNGKV-----VEFDRPevlRKKPGSLFAALM 1055
Cdd:PRK11247 161 LGALDaltrIEMQDLIESLWQQ--HGFTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP---RRRGSARLAELE 235
|
.
gi 1034596369 1056 A 1056
Cdd:PRK11247 236 A 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
838-1060 |
9.16e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPVLLSG-T 912
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 913 IRFNLD-P-----FDRHTDQQIWDA-LERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 985
Cdd:PRK10535 103 AAQNVEvPavyagLERKQRLLRAQElLQRLGLEDRVEYQPSQL-----------SGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 986 TASIDM---ETDTLIQRTIREafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEfDRPEVLRKKPGSLFAALMATATS 1060
Cdd:PRK10535 172 TGALDShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPAQEKVNVAGGTEPVVNTASG 246
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
837-1051 |
9.29e-11 |
|
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: 63.13 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrSKLSVIPQDPVL-----LSG 911
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALfrhmtVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 TIRFNL-------DPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 984
Cdd:cd03296 94 NVAFGLrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 985 ATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLF 1051
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
820-1034 |
1.05e-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: 65.23 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPTVLHGIN---LTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-PMAGRILIDG--VDICSIgLE 893
Cdd:TIGR02633 254 GDVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNP-AQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 894 DLRSKLSVIPQD-------PVLLSGTiRFNLDPFDRHTDQ-QIWDALERTFLTKAISKFPKKLHTDVVENGGnFSVGERQ 965
Cdd:TIGR02633 333 AIRAGIAMVPEDrkrhgivPILGVGK-NITLSVLKSFCFKmRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 966 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
834-1036 |
1.07e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 834 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GMALFRLVEpmaGRILIDGVDICSIGLEDlRSKLSVIP--QDP 906
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLskviaGHPAYKILE---GDILFKGESILDLEPEE-RAHLGIFLafQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 907 VLLSGT-----IRFNLDPFDRHTDQQIWDALErtFLTKAISKF------PKKLHTDVVEnggNFSVGERQLLCIARAVLR 975
Cdd:CHL00131 94 IEIPGVsnadfLRLAYNSKRKFQGLPELDPLE--FLEIINEKLklvgmdPSFLSRNVNE---GFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 976 NSKIILIDEATASIDMetDTLiqRTIREAF-----QGCTVLVIAH--RVTTVLNCDHILVMGNGKVVE 1036
Cdd:CHL00131 169 DSELAILDETDSGLDI--DAL--KIIAEGInklmtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
813-1036 |
1.11e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 813 PQGWPQHGEIIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 892
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 893 EDLRSKLSVIPQDpvllsgtirFNLdpFDRHTD---QQIWDALERTFLtkAISKFPKKLHtdvVENGG----NFSVGERQ 965
Cdd:PRK10522 393 EDYRKLFSAVFTD---------FHL--FDQLLGpegKPANPALVEKWL--ERLKMAHKLE---LEDGRisnlKLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 966 LLCIARAVLRNSKIILIDEATAsidmETDTLIQRT--------IREafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAA----DQDPHFRREfyqvllplLQE--MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
837-1059 |
1.27e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGVDIC--SIGLEDLrsklSVIPQDPVL-- 908
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVThrSIQQRDI----CMVFQSYALfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 ---LSGTIRFNLDPFDRHTD---QQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILI 982
Cdd:PRK11432 92 hmsLGENVGYGLKMLGVPKEerkQRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 983 DEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGSLF-AALMATA 1058
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQPASRFmASFMGDA 240
|
.
gi 1034596369 1059 T 1059
Cdd:PRK11432 241 N 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
208-391 |
1.28e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 62.84 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLS--AILEemHLLEGSVGVQG-----------------SLAYVpQQAW--IVS 266
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGllAGLD--RPTSGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 267 GNIRENILMggaydkarylqvlhccslnrDLELLPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSD 332
Cdd:COG4181 105 LTALENVML--------------------PLELAGRRDARARARALLErvglghrldhypaqLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 333 RQIYLLDDPLSAVDAHVGKHI----FEecIKKTlRGKTVVLVTHQLQYLEFCGQIILLENGKI 391
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
208-390 |
1.40e-10 |
|
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: 60.54 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV--GVQGSLAYVPQqawivsgnirenilmggaydkaryl 285
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtwGSTVKIGYFEQ------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 286 qvlhccslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKtLRGk 365
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-YPG- 118
|
170 180
....*....|....*....|....*.
gi 1034596369 366 TVVLVTHQLQYL-EFCGQIILLENGK 390
Cdd:cd03221 119 TVILVSHDRYFLdQVATKIIELEDGK 144
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
826-1049 |
1.59e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.68 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 826 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI-------------GL 892
Cdd:PRK10619 10 DLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 893 EDLRSKLSVIPQdpvllsgtiRFNLDPFDRHTDQQIWDALERTFLTKAIS-----KFPKKLHTDVVENGG---NFSVGER 964
Cdd:PRK10619 88 RLLRTRLTMVFQ---------HFNLWSHMTVLENVMEAPIQVLGLSKQEAreravKYLAKVGIDERAQGKypvHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 965 QLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEV 1042
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQ 238
|
....*..
gi 1034596369 1043 LRKKPGS 1049
Cdd:PRK10619 239 LFGNPQS 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
825-1015 |
1.73e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 825 QDYHMKYrdNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL--VEP---MAGRILIDGVDICSIGLE--DLRS 897
Cdd:PRK14239 9 SDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDtvDLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 898 KLSVIPQDPVLLSGTIRFNLDPFDRHT---DQQIWD-ALERTFLTKAI-SKFPKKLHTDVVenggNFSVGERQLLCIARA 972
Cdd:PRK14239 87 EIGMVFQQPNPFPMSIYENVVYGLRLKgikDKQVLDeAVEKSLKGASIwDEVKDRLHDSAL----GLSGGQQQRVCIARV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 973 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH 1015
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
837-1038 |
1.84e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 62.16 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE-DLRSKLSVIpqDPVLLSGTIRf 915
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRLL- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 916 nldpfdRHTDQQIWDALERtflTKAISKFPKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDT 995
Cdd:cd03220 113 ------GLSRKEIDEKIDE---IIEFSELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034596369 996 LIQRTIREAFQGCTVLVIA-HRVTTVLN-CDHILVMGNGKVVEFD 1038
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
208-401 |
1.86e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 62.31 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQGS--------------LAYVPQQAWIVSG-NI 269
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAI---SGLLpprSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENILMGgAY---DKARYLQVLHccslnRDLELLPfgdmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDP- 341
Cdd:COG0410 96 EENLLLG-AYarrDRAEVRADLE-----RVYELFP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPs 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 342 --LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELM 401
Cdd:COG0410 165 lgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELL 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
215-397 |
2.01e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 215 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLayVPQQAWIVSG---------------NIRENILMGGay 279
Cdd:PRK13537 30 VQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP--VPSRARHARQrvgvvpqfdnldpdfTVRENLLVFG-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 dkaRYLQVLHCCSLNRDLELLPFGDMTEIGE-RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECI 358
Cdd:PRK13537 106 ---RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034596369 359 KKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KICENGTH 397
Cdd:PRK13537 182 RSLLaRGKTILLTTHFMEEAErLCDRLCVIEEGrKIAEGAPH 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
835-1049 |
2.11e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 835 TPTVL-HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP----MAGRILIDGVdicSIGLEDLRSKL-SVIPQDPvl 908
Cdd:PRK10418 14 AAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRKiATIMQNP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 lsgtiR--FN-LDPFDRH------------TDQQIWDALERTFLTKA---ISKFPKKLhtdvvenggnfSVGERQLLCIA 970
Cdd:PRK10418 89 -----RsaFNpLHTMHTHaretclalgkpaDDATLTAALEAVGLENAarvLKLYPFEM-----------SGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 971 RAVLRNSKIILIDEATASID----METDTLIQRTIREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRK 1045
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDvvaqARILDLLESIVQK--RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFN 230
|
....
gi 1034596369 1046 KPGS 1049
Cdd:PRK10418 231 APKH 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
208-400 |
2.18e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 61.93 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG---------------SLAYVPQQAwivsgN-- 268
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGedltdskkdinklrrKVGMVFQQF-----Nlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 ----IRENILMGGaydkaryLQVLHccsLNRD------LELLpfgdmteigER-GL---------NLSGGQKQRISLARA 328
Cdd:COG1126 90 phltVLENVTLAP-------IKVKK---MSKAeaeeraMELL---------ERvGLadkadaypaQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 329 VYSDRQIYLLDDPLSAVDAhvgkhifeECIK------KTL--RGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSE 399
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDP--------ELVGevldvmRDLakEGMTMVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEE 222
|
.
gi 1034596369 400 L 400
Cdd:COG1126 223 F 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
838-1043 |
2.29e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSVIPQ-DPVLLSGTIRFN 916
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPFDRH---TDQQIwDALERTFLTKAisKFPKKLHTDVVENGGnfsvGERQLLCIARAVLRNSKIILIDEATASIDMET 993
Cdd:PRK13536 135 LLVFGRYfgmSTREI-EAVIPSLLEFA--RLESKADARVSDLSG----GMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 994 DTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1043
Cdd:PRK13536 208 RHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
208-375 |
2.33e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIlEEMHLLEGSVGVQGSLAY---------------------VPQQAWIVS 266
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 267 GNIRENILMG----GAYDKARYLQVLHccslnRDLELLPFGDmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:PRK14239 100 MSIYENVVYGlrlkGIKDKQVLDEAVE-----KSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034596369 339 DDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 375
Cdd:PRK14239 173 DEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
817-1041 |
2.54e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 817 PQHGEIIFQ-----DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-----RLVepmAGRILIDG-- 884
Cdd:NF040905 251 PKIGEVVFEvknwtVYHPLHPERK--VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDGke 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 885 VDICSI------GL----EDlRSKLSVIpqdpvlLSGTIRFN--LDPFDRHTDQQIWDALERtflTKAISKFPKKLHT-- 950
Cdd:NF040905 326 VDVSTVsdaidaGLayvtED-RKGYGLN------LIDDIKRNitLANLGKVSRRGVIDENEE---IKVAEEYRKKMNIkt 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 951 -DVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDM----ETDTLIQRTireAFQGCTVLVIAHRVTTVLN-CD 1024
Cdd:NF040905 396 pSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVISSELPELLGmCD 472
|
250
....*....|....*...
gi 1034596369 1025 HILVMGNGKVV-EFDRPE 1041
Cdd:NF040905 473 RIYVMNEGRITgELPREE 490
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
203-391 |
2.81e-10 |
|
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: 60.52 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 203 SLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVP----QQAWI 264
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 265 VSGNIRENILMGgaydkarylqvlhccSLnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:cd03215 91 LDLSVAENIALS---------------SL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 345 VDahVG--KHIFEECIKKTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKI 391
Cdd:cd03215 135 VD--VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
833-1041 |
3.08e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.94 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 833 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA----GRILIDGVDICSIGLEDLR----SKLSVIPQ 904
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERELRrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DPvLLSgtirfnLDPFdrHT--DQ------------------QIWDALERTFLTKA---ISKFPKKLhtdvvenggnfSV 961
Cdd:COG4172 100 EP-MTS------LNPL--HTigKQiaevlrlhrglsgaaaraRALELLERVGIPDPerrLDAYPHQL-----------SG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 962 GERQLLCIARAVLRNSKIILIDEATasidmeT--DTLIQRTI--------REafQGCTVLVIAHRVTTVLN-CDHILVMG 1030
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPT------TalDVTVQAQIldllkdlqRE--LGMALLLITHDLGVVRRfADRVAVMR 231
|
250
....*....|....*...
gi 1034596369 1031 NGKVVE-------FDRPE 1041
Cdd:COG4172 232 QGEIVEqgptaelFAAPQ 249
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
211-373 |
3.79e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------SLAYV-PQQAWIVSGNIRENILMGGAY 279
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 DKARYLQVLHC-CSLN-RDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEEC 357
Cdd:PRK13539 101 LGGEELDIAAAlEAVGlAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAEL 169
|
170
....*....|....*..
gi 1034596369 358 IKKTL-RGKTVVLVTHQ 373
Cdd:PRK13539 170 IRAHLaQGGIVIAATHI 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
209-373 |
4.65e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 209 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-----NIRE 271
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTEltaleNLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGGAYDKARYLQVLHCCSLnRDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH--- 348
Cdd:PRK13538 98 YQRLHGPGDDEALWEALAQVGL-AGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgva 166
|
170 180
....*....|....*....|....*
gi 1034596369 349 VGKHIFEECIKktlRGKTVVLVTHQ 373
Cdd:PRK13538 167 RLEALLAQHAE---QGGMVILTTHQ 188
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
208-413 |
4.87e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLL-------EGSVGVQG---------SLA--------YVPQQAW 263
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTL-------MNILgcldkptSGTYRVAGqdvatldadALAqlrrehfgFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 IVS-----GNIRENILMGGAYDKARylqvlhccsLNRDLELLP-FGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYL 337
Cdd:PRK10535 97 LLShltaaQNVEVPAVYAGLERKQR---------LLRAQELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 338 LDDPLSAVDAHVGKHIFeeCIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 413
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRdrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNT 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
208-401 |
4.92e-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: 61.25 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEG-SVGVQG-------------SLAYV-PQQAWIVSGNIR-E 271
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggedvwelrkRIGLVsPALQLRFPRDETvL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGGAYD--------------KARYLqvlhccslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIY 336
Cdd:COG1119 99 DVVLSGFFDsiglyreptdeqreRAREL-----------LELL---GLAHLADRPFGtLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 337 LLDDPLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELM 401
Cdd:COG1119 165 ILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
200-373 |
5.32e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 63.61 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 200 EGNSLGPELhkiNLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHLLEG---SVGVQGSLAYVPQQAWIVSGNIRENIL-- 274
Cdd:TIGR00954 463 NGDVLIESL---SFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIyp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 -------MGGAYDK--ARYLQVLHCCS-LNRDLELLPFGDMTEIgerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:TIGR00954 539 dssedmkRRGLSDKdlEQILDNVQLTHiLEREGGWSAVQDWMDV------LSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 1034596369 345 VDAHVGKHIFEECIKKtlrGKTVVLVTHQ 373
Cdd:TIGR00954 613 VSVDVEGYMYRLCREF---GITLFSVSHR 638
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
208-403 |
5.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVqGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQV 287
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 288 lhccSLNRDLELLP--FGDMTEIGER---------GLN----------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:PRK13643 101 ----TVLKDVAFGPqnFGIPKEKAEKiaaeklemvGLAdefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 347 --AHVGKHIFEECIKKTlrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQK 403
Cdd:PRK13643 177 pkARIEMMQLFESIHQS--GQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
824-1035 |
6.30e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 59.99 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 824 FQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG-----VDICSIGL--ED-- 894
Cdd:cd03269 3 VENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiAARNRIGYlpEErg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 895 LRSKLSVIPQdpVLLSGTIRfNLDPfdRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 974
Cdd:cd03269 81 LYPKMKVIDQ--LVYLAQLK-GLKK--EEARRRIDEWLERLELSEYANKRVEEL-----------SKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 975 RNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
208-434 |
6.35e-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: 62.90 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLLEGS----------------------VGVQ-----------GS 254
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVL-------MHVLRGMdqyeptsgriiyhvalcekcgyVERPskvgepcpvcgGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 255 LAYVPQQAWIVSGNIRENILMGGA---------YDKARYLQ-VLHCC---------SLNRDLELLpfgDMTEIGER---- 311
Cdd:TIGR03269 89 LEPEEVDFWNLSDKLRRRIRKRIAimlqrtfalYGDDTVLDnVLEALeeigyegkeAVGRAVDLI---EMVQLSHRithi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 312 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQLQYLE-FCGQIILLE 387
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEdLSDKAIWLE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034596369 388 NGKICENGTHSELMQkkgKYAQLIQKMHKEATSDMLQDTAKIAEKPK 434
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
206-372 |
6.74e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.03 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQ----AWIvsgNIRENI 273
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvtgpgaDRGVVFQKdallPWL---NVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMG----GAyDKARYLQvlhccslnRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:COG4525 98 AFGlrlrGV-PKAERRA--------RAEELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180
....*....|....*....|....*..
gi 1034596369 349 VGKHIFE---ECIKKTlrGKTVVLVTH 372
Cdd:COG4525 169 TREQMQElllDVWQRT--GKGVFLITH 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
193-373 |
7.01e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 193 DALGPEEEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpQQAWIVSGNIREN 272
Cdd:cd03231 4 DELTCERDGRAL---FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGGAYD--KARY-----LQVLHC-CSLNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:cd03231 75 LLYLGHAPgiKTTLsvlenLRFWHAdHSDEQVEEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|
gi 1034596369 344 AVDAHVGKHIFEECIKKTLRGKTVVLVTHQ 373
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
201-375 |
7.23e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.95 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 201 GNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAI-----LEEMHLLEGSVGVQGSLAYVPQqawIVSGNIRENILM 275
Cdd:PRK14243 21 GSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPD---VDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 ----GGAYDKARYLQVLHCCSLNRDLellpfGDMTEIGER------------------GLNLSGGQKQRISLARAVYSDR 333
Cdd:PRK14243 96 vfqkPNPFPKSIYDNIAYGARINGYK-----GDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034596369 334 QIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 375
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
837-1047 |
7.70e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG-----RILIDGVDICSI-GLEDLRSKLSVIPQDPV--- 907
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNpfp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 ------LLSGTIRFNLDPFD--------RHTDQQIWDALErtfltKAISKFPKKLhtdvvenggnfSVGERQLLCIARAV 973
Cdd:PRK14271 115 msimdnVLAGVRAHKLVPRKefrgvaqaRLTEVGLWDAVK-----DRLSDSPFRL-----------SGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 974 LRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1047
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
822-1035 |
7.80e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRdNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsigLEDLRSKL-S 900
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 901 VIPQD-------PVLLSGTI---RFNLDPFDR----HTDQQIWDALERTFLTKAiskfpkkLHTDVvengGNFSVGERQL 966
Cdd:PRK15056 82 YVPQSeevdwsfPVLVEDVVmmgRYGHMGWLRrakkRDRQIVTAALARVDMVEF-------RHRQI----GELSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 967 LCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHIlVMGNGKVV 1035
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
842-1053 |
9.68e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIglEDLRSKLSVIPQDPVL-----LSGTIRFN 916
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALfphmtVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPfDRHTDQQIWDALERTFLTKAISKFPK-KLHtdvvenggNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDT 995
Cdd:PRK11607 116 LKQ-DKLPKAEIASRVNEMLGLVHMQEFAKrKPH--------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 996 LIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1053
Cdd:PRK11607 187 RMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
211-395 |
1.29e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 59.30 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAW----IVSGN--------IRENIlmgg 277
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlgFVSDStglydrltARENL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 278 aydkaRYLQVLHccSLNRDL------ELLPFGDMTEIGE-RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 350
Cdd:cd03266 100 -----EYFAGLY--GLKGDEltarleELADRLGMEELLDrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034596369 351 KHIFEecIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENG 395
Cdd:cd03266 173 RALRE--FIRQLRalGKCILFSTHIMQEVErLCDRVVVLHRGRVVYEG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
314-400 |
1.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 314 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKIC 392
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKII 244
|
....*....
gi 1034596369 393 ENG-THSEL 400
Cdd:PRK13651 245 KDGdTYDIL 253
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
821-1050 |
1.39e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.42 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 821 EIIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIdGVDICSIG-----L 892
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 893 EDLRSKLSVIPQDP--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFLTKAI-SKFPKKLhtdvvenggnfSVG 962
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETvekdICFgpmNFGVSEEDAKQKAREMIELVGLPEELlARSPFEL-----------SGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 963 ERQLLCIARAVLRNSKIILIDEATASID-------MEtdtLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemME---MFYKLHKE--KGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
|
250
....*....|....*.
gi 1034596369 1035 VEFDRPEVLRKKPGSL 1050
Cdd:PRK13634 225 FLQGTPREIFADPDEL 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
822-1041 |
1.47e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.23 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTPTVLHG---INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC----SIGLED 894
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 895 LRSKLSVIPQDP--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFL-TKAISKFPKKLhtdvvenggnfSVGER 964
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTvlkdVEFgpkNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFEL-----------SGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 965 QLLCIARAVLRNSKIILIDEATASIDMETdtliQRTIREAFQ-----GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 1038
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKdyqkaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
...
gi 1034596369 1039 RPE 1041
Cdd:PRK13641 228 SPK 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
208-391 |
1.60e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--SLAYVPQQAWIVSGN-IRENILMGgaydKARY 284
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDLtVLDTVLDG----DAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 285 LQVLHccSLNRDLELLPFGD-----MTEIGER------------------GL------------NLSGGQKQRISLARAV 329
Cdd:COG0488 90 RALEA--ELEELEAKLAEPDedlerLAELQEEfealggweaearaeeilsGLgfpeedldrpvsELSGGWRRRVALARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 330 YSDRQIYLLDDP-----LSAVDAhvgkhiFEECIKKtlRGKTVVLVTHQLQYL-EFCGQIILLENGKI 391
Cdd:COG0488 168 LSEPDLLLLDEPtnhldLESIEW------LEEFLKN--YPGTVLVVSHDRYFLdRVATRILELDRGKL 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
208-389 |
1.73e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 59.40 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVP-QQAWIVSGN--------IRENIlmgga 278
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRMVVFQNysllpwltVRENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 279 ydkarYLQVlhccslNRDLELLPFGDMTEIGERGLNL--------------SGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:TIGR01184 76 -----ALAV------DRVLPDLSKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034596369 345 VDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENG 389
Cdd:TIGR01184 145 LDALTRGNLQEELMQiWEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
206-538 |
1.77e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIREN 272
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILM-----GGAYDKARylqvlhccsLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:TIGR01257 1024 ILFyaqlkGRSWEEAQ---------LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 348 HVGKHIFEECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ--KKGKYAQLIQKMHK-EATSDML 423
Cdd:TIGR01257 1095 YSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGdRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVRKMKNiQSQRGGC 1173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 424 QDTAKIAEK---PKVESQALATSLEESLNGNAvpehqltqEEEMEegslswRVYHHYIQAAggyMVSCIiffFVVLIVFL 500
Cdd:TIGR01257 1174 EGTCSCTSKgfsTRCPARVDEITPEQVLDGDV--------NELMD------LVYHHVPEAK---LVECI---GQELIFLL 1233
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034596369 501 TIFSFwwlsywlEQGSGTNSSRESNGTMADLG----NIADNP 538
Cdd:TIGR01257 1234 PNKNF-------KQRAYASLFRELEETLADLGlssfGISDTP 1268
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
208-393 |
1.93e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLsAILE--------EMHLL---------EGSVGVQG-SLAYVPQQAWIV-SGN 268
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLL-AILAglddgssgEVSLVgqplhqmdeEARAKLRAkHVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENI----LMGGAYD---KARYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLLDDP 341
Cdd:PRK10584 105 ALENVelpaLLRGESSrqsRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 342 LSAVDAHVGKHIFEECIKKTLR-GKTVVLVTHQLQYLEFCGQIILLENGKICE 393
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
839-1035 |
2.07e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED---LRSKLSVIPQD---------- 905
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhhllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 906 -----PVLLSGTirfNLDPFDRHTDQqiwdALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKII 980
Cdd:PRK10908 98 dnvaiPLIIAGA---SGDDIRRRVSA----ALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 981 LIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKVV 1035
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
822-1043 |
2.15e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.20 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSV 901
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQ----DPVLlsgTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVvengGNFSVGERQLLCIARAVLRNS 977
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV----GELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1043
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
836-1041 |
2.20e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 836 PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGL----------EDlRSKLSVIP 903
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDairagimlcpED-RKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 904 ----QDPVLLSGtiRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKlHTDVvengGNFSVGERQLLCIARAVLRNSKI 979
Cdd:PRK11288 345 vhsvADNINISA--RRHHLRAGCLINNRWEAENADRFIRSLNIKTPSR-EQLI----MNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 980 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPE 1041
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELAREQ 482
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
835-1038 |
2.92e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 835 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGvdicsigleDLRskLSVIPQDPVLLS 910
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPK---------GLR--IGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 G-TIRFNLdpFDRHTDqqIWDALERtfLTKAISKFPK---------KLHTDVVENGG----------------------- 957
Cdd:COG0488 75 DlTVLDTV--LDGDAE--LRALEAE--LEELEAKLAEpdedlerlaELQEEFEALGGweaearaeeilsglgfpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 958 ---NFSVGERQLLCIARAVLRNSKIILIDEATASIDMET-----DTLIQrtireaFQGcTVLVIAH------RVttvlnC 1023
Cdd:COG0488 149 pvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN------YPG-TVLVVSHdryfldRV-----A 216
|
250
....*....|....*
gi 1034596369 1024 DHILVMGNGKVVEFD 1038
Cdd:COG0488 217 TRILELDRGKLTLYP 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
208-404 |
3.10e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileeMHL------LEGSVGVQGSLAYVPQQAWI---------------VS 266
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLL------LHLngiylpQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 267 GNIRENILMGGAYDKARYLQVLhccslNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVE-----RRVEEALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 346 DAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQKK 404
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
820-1034 |
4.42e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPT---VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRlVEPMA--GRILIDG--VDICS--- 889
Cdd:PRK13549 256 GEVILEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNpqq 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 890 -----IGL--EDlRSKLSVIPQDPVLLSGTIRfNLDPFDRHTdqQIWDALERTFLTKAISKFpkKLHTDVVENG-GNFSV 961
Cdd:PRK13549 335 aiaqgIAMvpED-RKRDGIVPVMGVGKNITLA-ALDRFTGGS--RIDDAAELKTILESIQRL--KVKTASPELAiARLSG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 962 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
578-749 |
4.55e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 58.94 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 578 NKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLlpiFSEQFLVL---SLMVIAVLLIVSVLSPYILLMGAIIMVIC 654
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNEL---FTSGLVTLigdLLLLIGILIAMFLLNWRLALISLLVLPLL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 655 FIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIM 734
Cdd:cd18544 155 LLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQE---YRKANLKSIKLFALFRPLV 231
|
170
....*....|....*
gi 1034596369 735 TNLVTLAVALFVAFG 749
Cdd:cd18544 232 ELLSSLALALVLWYG 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
837-1041 |
5.34e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.17 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvDICSIgLE---DLRSKLSVIpqDPVLLSGTI 913
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL-LElgaGFHPELTGR--ENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 R-FNLDPFDRHTDQQIWDAlertfltkAISKFpkkLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEATASIDme 992
Cdd:COG1134 116 LgLSRKEIDEKFDEIVEFA--------ELGDF---IDQPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD-- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 993 tdtliqrtirEAFQ-------------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1041
Cdd:COG1134 179 ----------AAFQkkclarirelresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPE 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
834-1020 |
5.48e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.12 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 834 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICS--IGLEDLRSKLSVIPQDP 906
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 907 VLLSGTI----RFNLDPFDRHTDQQIWDALERTFLTKAI-SKFPKKLHTDVVENGGnfsvGERQLLCIARAVLRNSKIIL 981
Cdd:PRK14258 98 NLFPMSVydnvAYGVKIVGWRPKLEIDDIVESALKDADLwDEIKHKIHKSALDLSG----GQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034596369 982 IDEATASID----METDTLIQR-TIREAFqgcTVLVIAHRVTTV 1020
Cdd:PRK14258 174 MDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQV 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
822-1046 |
5.94e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.64 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 894
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 895 LRSKLSVIPQDP-----------VLLSGTIRFNLDpFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGE 963
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtverEIIFGPKNFKMN-LDEVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 964 RQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 1040
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSP 230
|
....*.
gi 1034596369 1041 EVLRKK 1046
Cdd:PRK13646 231 KELFKD 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
842-1044 |
6.37e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 58.96 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDicsigLEDLRSKLSVIP---------QDPVL---L 909
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV-----LQDSARGIFLPPhrrrigyvfQEARLfphL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 910 S--GTIRFNLDPFDRHTDQQIWDA----------LERtfltkaiskFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 977
Cdd:COG4148 93 SvrGNLLYGRKRAPRAERRISFDEvvellgighlLDR---------RPATL-----------SGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 978 KIILIDEATASIDMETDT----LIQRtIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP-EVLR 1044
Cdd:COG4148 153 RLLLMDEPLAALDLARKAeilpYLER-LRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLaEVLS 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
837-1036 |
6.63e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiGLEDLRSKLSVI-PQDPVLLSGTIRF 915
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 916 NLDpFDRH----TDQQIWDALERTFLtKAISKFPkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDM 991
Cdd:PRK13539 93 NLE-FWAAflggEELDIAAALEAVGL-APLAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 992 ETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNCdHILVMGNGKVVE 1036
Cdd:PRK13539 161 AAVALFAELIRAhLAQGGIVIAATHIPLGLPGA-RELDLGPFAAED 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
837-1015 |
7.84e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 56.73 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 916
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPFDR-HTDQQIWDALERTFLTkAISKFPkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET-D 994
Cdd:cd03231 94 LRFWHAdHSDEQVEEALARVGLN-GFEDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvA 162
|
170 180
....*....|....*....|.
gi 1034596369 995 TLIQRTIREAFQGCTVLVIAH 1015
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
208-410 |
7.87e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSaileemHL------LEGSVGV----------QGSLAYVPQQAWIV------ 265
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQ------HLngllqpTSGTVTIgervitagkkNKKLKPLRKKVGIVfqfpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 266 ---SGNIRENILMG---------GAYDKARYLqvLHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSD 332
Cdd:PRK13634 97 qlfEETVEKDICFGpmnfgvseeDAKQKAREM--IELVGLPEElLARSPF-----------ELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 333 RQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQL----QYLEfcgQIILLENGKICENGTHSELMQKKG 405
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMmemFYKLHKE--KGLTTVLVTHSMedaaRYAD---QIVVMHKGTVFLQGTPREIFADPD 238
|
....*
gi 1034596369 406 KYAQL 410
Cdd:PRK13634 239 ELEAI 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
838-1036 |
7.88e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--------VDICSIGLedLRSKLSVIPQD---- 905
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 906 PVLlsgTIRFNL--DPF------DRHTDQQIWDALERTFLTKAISKFPkkLHtdvvenggnFSVGERQLLCIARAVLRNS 977
Cdd:PRK11124 95 PHL---TVQQNLieAPCrvlglsKDQALARAEKLLERLRLKPYADRFP--LH---------LSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
17-108 |
8.04e-09 |
|
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: 57.95 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 17 DQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKE------RKLLEK-CGLVQSLTSItLFIIPTVATAVWvlihtsL 89
Cdd:cd18598 173 DARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKElkalkgRKYLDAlCVYFWATTPV-LISILTFATYVL------M 245
|
90
....*....|....*....
gi 1034596369 90 KLKLTASMAFSMLASLNLL 108
Cdd:cd18598 246 GNTLTAAKVFTSLALFNML 264
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
208-400 |
9.20e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.77 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL----------------------EEMHLLEGSVGV--QGSLAYV-PQQA 262
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVglespsqgnvswrgeplaklnrAQRKAFRRDIQMvfQDSISAVnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 263 --WIVSGNIRENILMGGAYDKARYLQVLHCCSLnrDLELLpfgdmteiGERGLNLSGGQKQRISLARAVYSDRQIYLLDD 340
Cdd:PRK10419 108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDL--DDSVL--------DKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 341 PLSAVDAHVGKHIFEecIKKTLR---GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSEL 400
Cdd:PRK10419 178 AVSNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVErFCQRVMVMDNGQIVETQPVGDK 239
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
549-749 |
1.01e-08 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 57.82 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 549 LNALLLICVGVCSS----GIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLP 616
Cdd:cd18552 35 LEALLLVPLAIIGLfllrGLASylqtylmaYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 617 IFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVF-KRLENYSR------SPLFSHILNSLQG 689
Cdd:cd18552 115 SALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL-------PIRRIgKRLRKISRrsqesmGDLTSVLQETLSG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 690 LSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 749
Cdd:cd18552 188 IRVVKAFGAEDYEIKRFRKANE---RLRRLSMKIARARALSSPLMELLGAIAIALVLWYG 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
837-1033 |
1.11e-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: 54.76 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLvepMAGRILIDGVDICSIGledlRSKLSVIPQdpvlLSGtirfn 916
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTL----LKL---IAGELEPDEGIVTWGS----TVKIGYFEQ----LSG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 ldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASIDMETDTL 996
Cdd:cd03221 74 ---------------------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 997 IQRTIREaFQGcTVLVIAH------RVttvlnCDHILVMGNGK 1033
Cdd:cd03221 109 LEEALKE-YPG-TVILVSHdryfldQV-----ATKIIELEDGK 144
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
206-403 |
1.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMHLLEGSVGVQGsLAYVPQQAWivsgNIRE----------N 272
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVW----DIREkvgivfqnpdN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGGAY--DKARYLQvlhccslNRDLellPFGDMTEIGERGL--------------NLSGGQKQRISLARAVYSDRQIY 336
Cdd:PRK13640 96 QFVGATVgdDVAFGLE-------NRAV---PRPEMIKIVRDVLadvgmldyidsepaNLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 337 LLDDPLSAVDAHvGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 403
Cdd:PRK13640 166 ILDESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
850-1035 |
1.39e-08 |
|
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: 56.15 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 850 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGV---DIC-SIGLEDLRSKLSVIPQDPVLLSG-TIRFNL------- 917
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPHlNVRENLafglkrk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 918 -DPFDRHTDQQIWDALErtfLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTL 996
Cdd:cd03297 104 rNREDRISVDELLDLLG---LDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034596369 997 IQ---RTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVV 1035
Cdd:cd03297 170 LLpelKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
198-401 |
1.51e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.12 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 198 EEEGNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 277
Cdd:PRK10070 36 EKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 278 AYDKARYLQVLHCCSLNRDLELLPFGDMTE-----IGERGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAGINAEERREkaldaLRQVGLEnyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 344 AVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 401
Cdd:PRK10070 194 ALDPLIRTEMQDELVKlQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
208-432 |
1.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.33 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLS-----AILEEMHLLEGSVGVQGSLAYVPQ---------------QAWIVSG 267
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQltnglIISETGQTIVGDYAIPANLKKIKEvkrlrkeiglvfqfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 268 NIRENILMG----GAYDKARYLQV---LHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLD 339
Cdd:PRK13645 107 TIEKDIAFGpvnlGENKQEAYKKVpelLKLVQLPEDyVKRSPF-----------ELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 340 DPLSAVDAHVGK---HIFEECIKKtlRGKTVVLVTHQL-QYLEFCGQIILLENGKICENG------THSELMQK----KG 405
Cdd:PRK13645 176 EPTGGLDPKGEEdfiNLFERLNKE--YKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGspfeifSNQELLTKieidPP 253
|
250 260
....*....|....*....|....*..
gi 1034596369 406 KYAQLIQKMhKEATSDMLQDTAKIAEK 432
Cdd:PRK13645 254 KLYQLMYKL-KNKGIDLLNKNIRTIEE 279
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
297-400 |
1.64e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 297 LELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLR-GKTVVLVTHQL- 374
Cdd:PRK13631 170 LERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMe 237
|
90 100
....*....|....*....|....*.
gi 1034596369 375 QYLEFCGQIILLENGKICENGTHSEL 400
Cdd:PRK13631 238 HVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
841-1047 |
1.83e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.54 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 841 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICsiGLED----------------LRSKLSVIPQ 904
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGhqiarmgvvrtfqhvrLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DPV---------LLSGTirFNLDPFDRHTDQQIWDA---LERTFLTKAISKfpkklhtdvveNGGNFSVGERQLLCIARA 972
Cdd:PRK11300 101 LLVaqhqqlktgLFSGL--LKTPAFRRAESEALDRAatwLERVGLLEHANR-----------QAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 973 VLRNSKIILIDEATASID-METDTLIQ--RTIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1047
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
957-1033 |
2.00e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 957 GNFSVGERQLLCIARAVLRNSKIILIDEAT-ASIDMETDTLIqRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1033
Cdd:PRK10762 140 GELSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
830-1039 |
2.15e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 830 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE--PMAGRILIDGVDicsigledlrsklsvIPQDPV 907
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ---------------FGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LlsgtirfnLDPFDRHTDqqIWDALER----------TFLTKaiskfPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 977
Cdd:COG2401 102 L--------IDAIGRKGD--FKDAVELlnavglsdavLWLRR-----FKEL-----------STGQKFRFRLALLLAERP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHR--VTTVLNCDHILVMGNGKVVEFDR 1039
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHydVIDDLQPDLLIFVGYGGVPEEKR 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
208-410 |
2.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.71 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------SLAYVPQQAWIV---------SGN 268
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkYIRPVRKRIGMVfqfpesqlfEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENILMGGA-------YDKARYLQVLHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDD 340
Cdd:PRK13646 103 VEREIIFGPKnfkmnldEVKNYAHRLLMDLGFSRDvMSQSPF-----------QMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 341 PLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQL----QYLEfcgQIILLENGKICENGTHSELMQKKGKYAQL 410
Cdd:PRK13646 172 PTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnevaRYAD---EVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
208-374 |
2.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAiLEEMHLLEGSVGVQGSLAYVPQQAWIVSGNI------------RENILM 275
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsmvhpKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 GGAYDKARYlqVLHCCSLNRDLEL-------LPFGDM-----TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:PRK14258 102 MSVYDNVAY--GVKIVGWRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190
....*....|....*....|....*....|..
gi 1034596369 344 AVDAHVGKHIFEECIKKTLRGK-TVVLVTHQL 374
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
839-1040 |
3.02e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDPVllsG---- 911
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY---Gslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 --TIRFNL-DPFDRHTD-------QQIWDALERTFL-TKAISKFPkklHTdvvenggnFSVGERQLLCIARAVLRNSKII 980
Cdd:PRK11308 108 rkKVGQILeEPLLINTSlsaaerrEKALAMMAKVGLrPEHYDRYP---HM--------FSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 981 LIDEATASIDMEtdtlIQRTIREAFQ------GCTVLVIAHRVTTVlncDHI----LVMGNGKVVE-------FDRP 1040
Cdd:PRK11308 177 VADEPVSALDVS----VQAQVLNLMMdlqqelGLSYVFISHDLSVV---EHIadevMVMYLGRCVEkgtkeqiFNNP 246
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
190-417 |
3.13e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 190 RPRDALGPEEEGNSLGPeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIvSGNI 269
Cdd:PRK13546 23 RMKDALIPKHKNKTFFA-LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 R--ENI-----LMGGAYDKARYLQVlhccslnrdlELLPFGDMTE-IGERGLNLSGGQKQRISLARAVYSDRQIYLLDDP 341
Cdd:PRK13546 101 TgiENIefkmlCMGFKRKEIKAMTP----------KIIEFSELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 342 LSavdahVGKHIF-EECIKKTL----RGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMH 415
Cdd:PRK13546 171 LS-----VGDQTFaQKCLDKIYefkeQNKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKS 245
|
..
gi 1034596369 416 KE 417
Cdd:PRK13546 246 KA 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
839-1036 |
3.23e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGV--------DICSIGLEDLRSKLSVIPQDPV--- 907
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttAALAAGVAIIYQELHLVPEMTVaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 908 LLSGTI--RFNLdpFDRHTDQQiwDALERTfltkaiskfpKKLHTDVVENG--GNFSVGERQLLCIARAVLRNSKIILID 983
Cdd:PRK11288 100 LYLGQLphKGGI--VNRRLLNY--EAREQL----------EHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 984 EATASIDM-ETDTLIqRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK11288 166 EPTSSLSArEIEQLF-RVIRElRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
837-1035 |
3.40e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK-LSVIPQDPVLLSG- 911
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 TIRFNLdpFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENG---GNFSVGERQLLCIARAVLRNSKIILIDEATAS 988
Cdd:TIGR02633 94 SVAENI--FLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTrpvGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 989 I-DMETDTLIQrTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1035
Cdd:TIGR02633 172 LtEKETEILLD-IIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
845-1029 |
3.48e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.49 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 845 TIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDpvLLSGTIRfnldpfdrht 924
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTVRD--LLSSITK---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 925 dqqiwDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREa 1004
Cdd:cd03237 88 -----DFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR- 160
|
170 180
....*....|....*....|....*
gi 1034596369 1005 fqgctvlVIAHRVTTVLNCDHILVM 1029
Cdd:cd03237 161 -------FAENNEKTAFVVEHDIIM 178
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
211-403 |
3.57e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAI-----LEEMHLLEGSVGVQGSLAYVPQQAWIvsgNIRENILMGGAY-DKARY 284
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPI---EVRREVGMVFQYpNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 285 LQVLHCCSLNRDLELL--PFGDMTEIGERGL------------------NLSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALkkaalwdevkdrlndypsNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 345 VDAhVGKHIFEECIKKTLRGKTVVLVTHQ-------LQYLEFCGQIILLENG---KICENGTHsELMQK 403
Cdd:PRK14267 180 IDP-VGTAKIEELLFELKKEYTIVLVTHSpaqaarvSDYVAFLYLGKLIEVGptrKVFENPEH-ELTEK 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
212-402 |
4.03e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 212 NLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--LAYVPQQAwIVSG-----------NIRENILMG-- 276
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRR-PVSMlfqennlfshlTVAQNIGLGln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 -----GAYDKARYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:PRK10771 98 pglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 352 HIF----EECIKKTLrgkTVVLVTHQlqyLEFCGQI----ILLENGKICENGTHSELMQ 402
Cdd:PRK10771 167 EMLtlvsQVCQERQL---TLLMVSHS---LEDAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
206-395 |
4.34e-08 |
|
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: 55.03 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILeemHLLEGSVGVQGslaYVPqqaWIVSGNIRENI--LMGGAYD 280
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLL---QPTSGEVRVAG---LVP---WKRRKKFLRRIgvVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 281 KARYLQVLHCCSLNRDLELLP----------FGDMTEIGE------RglNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPparfkkrldeLSELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 345 VDAhVGKHIFEECIKK--TLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENG 395
Cdd:cd03267 184 LDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEaLARRVLVIDKGRLLYDG 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
211-373 |
4.57e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQgslayVPQQAWIVSGNIRENILMGGAYDKAryLQVLHC 290
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDA--VELLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 291 CSLNrD--LELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD---AHVGKHIFEECIKKtlRGK 365
Cdd:COG2401 122 VGLS-DavLWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR--AGI 188
|
....*...
gi 1034596369 366 TVVLVTHQ 373
Cdd:COG2401 189 TLVVATHH 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
838-1041 |
5.63e-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: 56.73 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLV---EPMAGRIlIDGVDIC-SIGLEDLRSKlsVIPQDPVLLSGTI 913
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRI-IYHVALCeKCGYVERPSK--VGEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RFNLD------PFDRHTDQQIWDALERTF--------LTKAISKFPK-------------------KLHTDVVENGGNFS 960
Cdd:TIGR03269 91 PEEVDfwnlsdKLRRRIRKRIAIMLQRTFalygddtvLDNVLEALEEigyegkeavgravdliemvQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 961 VGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHrVTTVLN--CDHILVMGNGKVVE 1036
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSH-WPEVIEdlSDKAIWLENGEIKE 249
|
....*
gi 1034596369 1037 FDRPE 1041
Cdd:TIGR03269 250 EGTPD 254
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
830-1051 |
5.74e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 830 KYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrSKLSVIPQDPVL- 908
Cdd:PRK10851 10 KSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 ----LSGTIRFNLDPFDRHT-------DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 977
Cdd:PRK10851 87 rhmtVFDNIAFGLTVLPRRErpnaaaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIR---EAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLF 1051
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRF 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
842-1034 |
6.31e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLLSGTIRFN 916
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssgLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 LDPFdRHTDQQIWdaLERTFLTKAISKFPKKLH---TDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 993
Cdd:PRK15439 362 VCAL-THNRRGFW--IKPARENAVLERYRRALNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 994 DTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:PRK15439 439 RNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
839-1047 |
7.98e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA-----GRILIDGVDICSIGLE--DLRSKLSVIPQDPVLLSG 911
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 912 TIRFNL------DPFDRHTDQQIWDALERTFLTKAISKfpkKLHtdvvENGGNFSVGERQLLCIARAVLRNSKIILIDEA 985
Cdd:PRK14243 106 SIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKD---KLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 986 TASIDMETDTLIQRTIREAFQGCTVLVIAH------RV---TTVLNCDHILVMG-NGKVVEFDRPEVLRKKP 1047
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVsdmTAFFNVELTEGGGrYGYLVEFDRTEKIFNSP 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
837-1036 |
8.21e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLS------------VIP- 903
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD-EEARAKLRakhvgfvfqsfmLIPt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 904 -------QDPVLLSGTirfnldpFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRN 976
Cdd:PRK10584 103 lnalenvELPALLRGE-------SSRQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 977 SKIILIDEATASIDMETDTLIQRTI----REafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLfslnRE--HGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
211-400 |
8.32e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.81 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEM---HLLEG------------SVG-VQGSLAYVPQQawivsgNIREN 272
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIagLEDItsgDLFIGekrmndvppaerGVGmVFQSYALYPHL------SVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG----GAyDKARYLQvlhccSLNRDLELLPFGDMTEigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA- 347
Cdd:PRK11000 96 MSFGlklaGA-KKEEINQ-----RVNQVAEVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAa 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 348 -HVGKHIFEECIKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:PRK11000 168 lRVQMRIEISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
845-1015 |
1.24e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 845 TIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicsigledlrSKLSVIPQ----DPvllSGTIRFNLDpf 920
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQyikpDY---DGTVEDLLR-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 921 drhtdqQIWDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 1000
Cdd:PRK13409 423 ------SITDDLGSSYYKSEIIK-PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170
....*....|....*..
gi 1034596369 1001 IREAF--QGCTVLVIAH 1015
Cdd:PRK13409 496 IRRIAeeREATALVVDH 512
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
206-410 |
1.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMhllEGSVGVQGSLaYVPQQAWivsgNIRENILMG------ 276
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAE---SGQIIIDGDL-LTEENVW----DIRHKIGMVfqnpdn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 ---GAY---DKARYLQ---VLHCCSLNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:PRK13650 93 qfvGATvedDVAFGLEnkgIPHEEMKERVNEALELVGMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 347 AHvGKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 410
Cdd:PRK13650 173 PE-GRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
316-395 |
1.31e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 316 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLRGKtvvlvtHQLQYL----------EFCGQIIL 385
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQK------HQLAYLfishdlhvvrALCHQVIV 498
|
90
....*....|
gi 1034596369 386 LENGKICENG 395
Cdd:PRK15134 499 LRQGEVVEQG 508
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
208-386 |
1.38e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENIL 274
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 M-----GGAYDKARYLqvlhccslnRDLEllPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:PRK10247 103 FpwqirNQQPDPAIFL---------DDLE--RFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034596369 349 vGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQIILL 386
Cdd:PRK10247 172 -NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
208-404 |
1.46e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.45 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------------SLAYVPQQAWIVSGN 268
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENILMG----GAYD---KARYLQVLHCCSLNRDL-ELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDD 340
Cdd:PRK13641 103 VLKDVEFGpknfGFSEdeaKEKALKWLKKVGLSEDLiSKSPF-----------ELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 341 PLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQKK 404
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
837-1041 |
1.50e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL-------- 908
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditvqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 LSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKklhtdvvENGGNFSVGERQLLCIARAVLRNSKIILIDEATAS 988
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 989 IDMETDT----LIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1041
Cdd:PRK10253 174 LDISHQIdlleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPK 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
199-375 |
1.67e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 199 EEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLLEG-SVGVQGSLAYVPQQAWIVSGNIR------- 270
Cdd:PRK11629 16 QEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLL-------HLLGGlDTPTSGDVIFNGQPMSKLSSAAKaelrnqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 -----------------ENILMGGAYDKARYLQVLhccslNRDLELL-PFGDMTEIGERGLNLSGGQKQRISLARAVYSD 332
Cdd:PRK11629 89 lgfiyqfhhllpdftalENVAMPLLIGKKKPAEIN-----SRALEMLaAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034596369 333 RQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVL-VTHQLQ 375
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLQ 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
838-1015 |
1.74e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI---CSIGLEDLRS-KLSVIPQ--------- 904
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklSSAAKAELRNqKLGFIYQfhhllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 ------DPVLLSGTIRfnldpfdRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 978
Cdd:PRK11629 104 alenvaMPLLIGKKKP-------AEINSRALEMLAAVGLEHRANHRPSEL-----------SGGERQRVAIARALVNNPR 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034596369 979 IILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAH 1015
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTH 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
838-1036 |
2.28e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.16 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrsklSVIPQDPVLLS-----GT 912
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwrnvqDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 913 IRFNLD------PFDRHTDQQiwdALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEAT 986
Cdd:PRK11248 91 VAFGLQlagvekMQRLEIAHQ---MLKKVGLEGAEKRYIWQL-----------SGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 987 ASIDMET----DTLIQRTIREafQGCTVLVIAHRVTTVLNCDHILVM---GNGKVVE 1036
Cdd:PRK11248 157 GALDAFTreqmQTLLLKLWQE--TGKQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
839-1036 |
2.71e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.01 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI---DGVDICSIGLED------LRSKLSVIPQDP--- 906
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrrlLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 907 ----VLLSGTIRFNL-DPFDRH---TDQQIWDALERTFLTKA-ISKFPkklhtdvvengGNFSVGERQLLCIARAVLRNS 977
Cdd:PRK11701 102 lrmqVSAGGNIGERLmAVGARHygdIRATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 978 KIILIDEATASIDMETDT----LIQRTIREafQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE 1036
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQArlldLLRGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
208-405 |
2.77e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.14 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhllegsvgvqGSLAYVpqqawIVSGNIR---ENILMGGAYDKARy 284
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-------------GHPKYE-----VTEGEILfkgEDITDLPPEERAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 285 lqvlhcCSLnrdleLLPFGDMTEIGE-------RGLN--LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE 355
Cdd:cd03217 77 ------LGI-----FLAFQYPPEIPGvknadflRYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 356 EcIKKTLR-GKTVVLVTHQLQYLEFC--GQIILLENGKICENGThSELMQ---KKG 405
Cdd:cd03217 146 V-INKLREeGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD-KELALeieKKG 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
851-1038 |
3.23e-07 |
|
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: 54.17 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 851 VVGIVGRTGSGKSSLgmalFRLV----EPMAGRILI-DGVdicsigledlrsKLSVIPQdpvllsgtIRFNLDPfDRHTD 925
Cdd:TIGR03719 350 IVGVIGPNGAGKSTL----FRMItgqeQPDSGTIEIgETV------------KLAYVDQ--------SRDALDP-NKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 926 QQIWDALE------RTFLTKA-ISKFPKKlHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETdtliQ 998
Cdd:TIGR03719 405 EEISGGLDiiklgkREIPSRAyVGRFNFK-GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET----L 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 999 RTIREA---FQGCTVlVIAH------RVTTvlncdHILVM-GNGKVVEFD 1038
Cdd:TIGR03719 480 RALEEAllnFAGCAV-VISHdrwfldRIAT-----HILAFeGDSHVEWFE 523
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
315-401 |
3.59e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 52.92 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQYLE-FCGQIILLENGK 390
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIinlMLE-LQEKL-GISYIYVSQHLGIVKhISDKVLVMHQGE 227
|
90
....*....|.
gi 1034596369 391 ICENGTHSELM 401
Cdd:COG4167 228 VVEYGKTAEVF 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
211-402 |
4.20e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAIL--------------EEMHLLEGSVGVQGSLAYVPQQAWI-----VSGN--- 268
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVgivprdagniiiddEDISLLPLHARARRGIGYLPQEASIfrrlsVYDNlma 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 ---IRENILMGGAYDKARYL-QVLHCCSLNRDLellpfgdmteigerGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:PRK10895 102 vlqIRDDLSAEQREDRANELmEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 345 VDAhvgkhIFEECIKKTL-----RGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQ 402
Cdd:PRK10895 168 VDP-----ISVIDIKRIIehlrdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
830-1053 |
5.26e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.03 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 830 KYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGVDICSIGLEDlRSKLSVIPQD 905
Cdd:PRK09452 22 KSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-RHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 906 PVLLSGTIRFNLD--------PFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 977
Cdd:PRK09452 96 ALFPHMTVFENVAfglrmqktPAAE-ITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 978 KIILIDEATASID--------METDTLiQRTIreafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPG 1048
Cdd:PRK09452 164 KVLLLDESLSALDyklrkqmqNELKAL-QRKL-----GITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
....*
gi 1034596369 1049 SLFAA 1053
Cdd:PRK09452 238 NLFVA 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
825-1045 |
5.27e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.50 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 825 QDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 904
Cdd:PRK13652 7 RDLCYSYSGSK-EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 DP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLR 975
Cdd:PRK13652 86 NPddQIFSPTVEqdiafgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 976 NSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE-------FDRPEVLRK 1045
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAygtveeiFLQPDLLAR 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
206-402 |
6.48e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.32 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGsLAYVPQQAWivsgNIRENILM---------G 276
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVW----DVRRQVGMvfqnpdnqfV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 GAY---DKARYL---QVLHCCSLNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhV 349
Cdd:PRK13635 96 GATvqdDVAFGLeniGVPREEMVERVDQALRQVGMEDFLNREpHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP-R 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 350 GKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQ 402
Cdd:PRK13635 175 GRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
842-1051 |
7.66e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFD 921
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 922 RHTDQQIWDalERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTI 1001
Cdd:TIGR01257 1028 AQLKGRSWE--EAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 1002 REAFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEFDRPEVLRKKPGSLF 1051
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKNCFGTGF 1155
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
205-402 |
7.81e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 205 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMH----------LLEGSVGVQGSL-----AYV---PQQAW--- 263
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqtagrvLLDGKPVAPCALrgrkiATImqnPRSAFnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 -IVSGNIRENIL-MGGAYDKARYLQVLHCCSLN---RDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:PRK10418 96 hTMHTHARETCLaLGKPADDATLTAALEAVGLEnaaRVLKLYPF-----------EMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 339 DDPLSAVDAHVGKHIFE--ECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ 402
Cdd:PRK10418 165 DEPTTDLDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLAdDVAVMSHGRIVEQGDVETLFN 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
838-1047 |
7.86e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 838 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlRSKLSVIPQ----DPVLLSGTI 913
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQklylDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RF-NLDPFDRHTDqqIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASIDME 992
Cdd:PRK09544 88 RFlRLRPGTKKED--ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 993 TDT----LIQRTIREAfqGCTVLVIAHRVTTVL-NCDHILVMgNGKVVEFDRPEVLRKKP 1047
Cdd:PRK09544 155 GQValydLIDQLRREL--DCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
550-708 |
8.20e-07 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 52.06 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 550 NALLLICVGVCSSGIF------------TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPI 617
Cdd:cd18570 39 NLLNIISIGLILLYLFqsllsyirsyllLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 618 FSEQFLVLSLMVIAVLLIVSVLSPY----ILLMGAIIMVICFIYYMMFKKAIGvfKRLENYSRspLFSHILNSLQGLSSI 693
Cdd:cd18570 118 TTISLFLDLLMVIISGIILFFYNWKlfliTLLIIPLYILIILLFNKPFKKKNR--EVMESNAE--LNSYLIESLKGIETI 193
|
170
....*....|....*
gi 1034596369 694 HVYGKTEDFISQFKR 708
Cdd:cd18570 194 KSLNAEEQFLKKIEK 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
822-1040 |
8.61e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.04 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 894
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 895 LRSKLSVIPQDP--VLLSGT----IRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVvenggnfSVGERQLLC 968
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETvlkdVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFEL-------SGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 969 IARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 1040
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
208-417 |
9.46e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.62 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMhllEGSVGVQG--------SLAYVPQQAWIVSGN-------- 268
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPT---SGEVLIKGepikydkkSLLEVRKTVGIVFQNpddqlfap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 -IRENILMGgaydkarylqvlhccSLNRDLellpfgDMTEIGER--------GL---------NLSGGQKQRISLARAVY 330
Cdd:PRK13639 95 tVEEDVAFG---------------PLNLGL------SKEEVEKRvkealkavGMegfenkpphHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 331 SDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKG---- 405
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDIEtirk 233
|
250
....*....|....*...
gi 1034596369 406 ------KYAQLIQKMHKE 417
Cdd:PRK13639 234 anlrlpRVAHLIEILNKE 251
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-400 |
1.02e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 393
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*..
gi 1034596369 394 NGTHSEL 400
Cdd:PRK14271 243 EGPTEQL 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
842-1047 |
1.05e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 842 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-P---MAGRILIDGVDICSIGLEDLR----SKLSVIPQDPVLL---S 910
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSlnpC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 911 GTIRFnldpfdrhtdqQIWDALE-------RTFLTKAI---------------SKFPKKLhtdvvenggnfSVGERQLLC 968
Cdd:PRK11022 106 YTVGF-----------QIMEAIKvhqggnkKTRRQRAIdllnqvgipdpasrlDVYPHQL-----------SGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 969 IARAVLRNSKIILIDEATASIDMEtdtlIQRTIREAF------QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1041
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAH 239
|
....*.
gi 1034596369 1042 VLRKKP 1047
Cdd:PRK11022 240 DIFRAP 245
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
208-384 |
1.07e-06 |
|
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: 50.01 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEmhllEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYdkarylqv 287
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 288 lhcCSLNRDLEllpfgdmteigerglNLSGGQKQRISLARAVYSD--RQIYLLDDPLSAVDaHVGKHIFEECIKKTL-RG 364
Cdd:cd03238 79 ---LTLGQKLS---------------TLSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLG 139
|
170 180
....*....|....*....|
gi 1034596369 365 KTVVLVTHQLQYLEFCGQII 384
Cdd:cd03238 140 NTVILIEHNLDVLSSADWII 159
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
817-1030 |
1.17e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 817 PQHGEIIFQDYHMKYrDNTPTV-------LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdics 889
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 890 igledlRSKLSVIPQDPVLLSGTIRfnldpfdrhtDQQIW-----DALERTFLTKAISKFPKKLH-TDVVENGGNF---- 959
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLR----------DQIIYpdsseDMKRRGLSDKDLEQILDNVQlTHILEREGGWsavq 577
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 960 ------SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAfqGCTVLVIAHRVTTVLNCDHILVMG 1030
Cdd:TIGR00954 578 dwmdvlSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
531-751 |
1.22e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 51.41 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 531 LGNIADNPQLSFYQLVYGLNALLLICVGVCSS-------GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 603
Cdd:cd18557 19 IGRLIDTIIKGGDLDVLNELALILLAIYLLQSvftfvryYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 604 FAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLF--- 680
Cdd:cd18557 99 LSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALAkag 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 681 SHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS 751
Cdd:cd18557 176 QVAEESLSNIRTVRSFSAEEKEIRRYS---EALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGY 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
208-424 |
1.50e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaiLEEMHLLE---GSVGVQG-------------SLAYVPQQAWIVSGNIRE 271
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLL---LTFMRMVEvcgGEIRVNGreigayglrelrrQFSMIPQDPVLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NIlmgGAYDKARYLQVLhccslnRDLELLPF---------GDMTEIGERGLNLSGGQKQRISLARAVYS-DRQIYLLDDP 341
Cdd:PTZ00243 1403 NV---DPFLEASSAEVW------AALELVGLrervaseseGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEA 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 342 LSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSEL-MQKKGKYAQLIQKMHKEATS 420
Cdd:PTZ00243 1474 TANIDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEALGRSEAK 1552
|
....
gi 1034596369 421 DMLQ 424
Cdd:PTZ00243 1553 RFLQ 1556
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
270-428 |
2.11e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 270 RENILMGGaydkaRYLQVLHCCSLNRDLELLPFGDMTEI-GERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 348
Cdd:NF000106 104 RENLYMIG-----R*LDLSRKDARARADELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 349 VGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSDMLQDTA 427
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIA 258
|
.
gi 1034596369 428 K 428
Cdd:NF000106 259 Q 259
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
208-390 |
3.13e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILE------EMHLLEGSVGVQG-------SLAYVPQQAWIVSG-NIR 270
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPhgtwdgEIYWSGSPLKASNirdteraGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMGG---------AYDkaryLQVLHCCSLNRDLELLPFGDMTEIGERGlnlsGGQKQRISLARAVYSDRQIYLLDDP 341
Cdd:TIGR02633 97 ENIFLGNeitlpggrmAYN----AMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 342 LSAVDAHVGKHIFEecIKKTLRGKTV--VLVTHQLQYLE-FCGQIILLENGK 390
Cdd:TIGR02633 169 SSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKaVCDTICVIRDGQ 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
211-403 |
3.23e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLS--AILEEMHllEGSVGVQG------------------SLAYVPQQAwiVSGNIR 270
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRlvAGLEKPT--EGQIFIDGedvthrsiqqrdicmvfqSYALFPHMS--LGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMGGAYDKARYLQVlhccslNRDLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:PRK11432 101 YGLKMLGVPKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 350 GKHIFEEC--IKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSELMQK 403
Cdd:PRK11432 172 RRSMREKIreLQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
209-379 |
3.33e-06 |
|
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: 48.12 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 209 HKINLVV-----SKGMMLGVCGNTGSGKSSLLSAILeemhLLEGSVGVQGSLAYVPQQAWIVsgnirenilmggAYDKAR 283
Cdd:cd03227 7 FPSYFVPndvtfGEGSLTIITGPNGSGKSTILDAIG----LALGGAQSATRRRSGVKAGCIV------------AAVSAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 284 YLQVLHCcslnrdlellpfgdmteigerglnLSGGQKQRISLARAV----YSDRQIYLLDDPLSAVDAHVGKHIFEECIK 359
Cdd:cd03227 71 LIFTRLQ------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170 180
....*....|....*....|
gi 1034596369 360 KTLRGKTVVLVTHQLQYLEF 379
Cdd:cd03227 127 HLVKGAQVIVITHLPELAEL 146
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
208-402 |
3.64e-06 |
|
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: 49.46 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------------SLAYVPQQAWIVSG-NIREN 272
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILM---GGAYDKARYLQVLHccSLNRDLELLPFGDmteigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:cd03218 96 ILAvleIRGLSKKEREEKLE--ELLEEFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 350 GKHIFEecIKKTLRGKTV-VLVT-HQL-QYLEFCGQIILLENGKICENGTHSELMQ 402
Cdd:cd03218 169 VQDIQK--IIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
198-391 |
3.68e-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: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 198 EEEGNSLGPelhkINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLLEGsvgvqgsLaYVPQqawivSGNIR------- 270
Cdd:COG4615 342 GDEGFTLGP----IDLTIRRGELVFIVGGNGSGKSTL-------AKLLTG-------L-YRPE-----SGEILldgqpvt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 -ENI-------------------LMGGAY----DKARYLqvlhccslnrdLELLPFGDMTEIgERG----LNLSGGQKQR 322
Cdd:COG4615 398 aDNReayrqlfsavfsdfhlfdrLLGLDGeadpARAREL-----------LERLELDHKVSV-EDGrfstTDLSQGQRKR 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 323 ISLARAVYSDRQIYLLD------DPlsavdahVGKHIF-EECI---KKtlRGKTVVLVTHQLQYLEFCGQIILLENGKI 391
Cdd:COG4615 466 LALLVALLEDRPILVFDewaadqDP-------EFRRVFyTELLpelKA--RGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
198-403 |
4.23e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 198 EEEGNSLgPELHKINLVVSKGMMLGVCGNTGSGKSSllsaILEEMHLL----EGSVGVQGSLAYVPQQAWivsgNIRENI 273
Cdd:PRK13633 17 NEESTEK-LALDDVNLEVKKGEFLVILGRNGSGKST----IAKHMNALlipsEGKVYVDGLDTSDEENLW----DIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 274 LMggaydkarylqVLHccslNRDLELLP--------FG------DMTEIGERGLN-----------------LSGGQKQR 322
Cdd:PRK13633 88 GM-----------VFQ----NPDNQIVAtiveedvaFGpenlgiPPEEIRERVDEslkkvgmyeyrrhaphlLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 323 ISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSEL 400
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDP-SGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 1034596369 401 MQK 403
Cdd:PRK13633 232 FKE 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
198-393 |
4.52e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 198 EEEGNSLGPelhkINLVVSKGMMLGVCGNTGSGKSSLlsaileEMhLLEGsvgvqgslAYVPQQAWI------VSGNIRE 271
Cdd:PRK10522 333 QDNGFSVGP----INLTIKRGELLFLIGGNGSGKSTL------AM-LLTG--------LYQPQSGEIlldgkpVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NI----------------LMGG---AYDKARYLQVLHCCSLNRDLELlpfgdmtEIGE-RGLNLSGGQKQRISLARAVYS 331
Cdd:PRK10522 394 DYrklfsavftdfhlfdqLLGPegkPANPALVEKWLERLKMAHKLEL-------EDGRiSNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 332 DRQIYLLDDPLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICE 393
Cdd:PRK10522 467 ERDILLLDEWAADQDPHF-RREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
849-1041 |
4.75e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 849 HEVVGIVGRTGSGKSSLGMALFRLVEPMAGRIlidgvdicsigledlrsklsvipqdpvllsgtIRFNLDPFDRHTDQQI 928
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 929 WdalertfltkaiskfpkklHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIR------ 1002
Cdd:smart00382 50 L-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034596369 1003 -EAFQGCTVLVIAHRVTTVLncDHILVMGNGKVVEFDRPE 1041
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
843-1017 |
4.76e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.81 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 843 NLTIRGHEVVGIVGRTGSGKSSL--GMALFrlVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLLSG-TIRFN--- 916
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLlnLIAGF--LTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 917 -LDPFDRHTDQQ---IWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID-- 990
Cdd:PRK10771 95 gLNPGLKLNAAQrekLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*....
gi 1034596369 991 --METDTLIQRTIREafQGCTVLVIAHRV 1017
Cdd:PRK10771 164 lrQEMLTLVSQVCQE--RQLTLLMVSHSL 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
820-1036 |
5.02e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 820 GEIIFQDYHMKYRDNTPtvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC-SIGLEDLRSK 898
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 899 LSVIPQD-------------------PVLLSGTIRFNLDPFDRHTDQQIWDAlERTFLtkAIskfpkKLHTdVVENGGNF 959
Cdd:PRK09700 340 MAYITESrrdngffpnfsiaqnmaisRSLKDGGYKGAMGLFHEVDEQRTAEN-QRELL--AL-----KCHS-VNQNITEL 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 960 SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1036
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
206-380 |
5.18e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-----LAYVPQQAWIV---SG-----NIREN 272
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdLCTYQKQLCFVghrSGinpylTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILmggaYD---KARYLQVLHCCSLNRDLELLPFgdmteigERGLnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:PRK13540 95 CL----YDihfSPGAVGITELCRLFSLEHLIDY-------PCGL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034596369 350 GKHIFEECIKKTLRGKTVVLVTHQ------LQYLEFC 380
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQdlplnkADYEEYH 199
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
829-1047 |
5.18e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 829 MKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGVDICSI---GLEDLRSKLSV 901
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMsrsRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 902 IPQdpvllSGTIRFNLDPFdrhtDQQIWDALERTFLTKAIskfpkkLHTDV---VENGG----------NFSVGERQLLC 968
Cdd:PRK11831 89 LFQ-----SGALFTDMNVF----DNVAYPLREHTQLPAPL------LHSTVmmkLEAVGlrgaaklmpsELSGGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 969 IARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRK 1045
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233
|
..
gi 1034596369 1046 KP 1047
Cdd:PRK11831 234 NP 235
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
531-749 |
6.26e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 49.33 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 531 LGNIAD---NPQLSFYQLVYglNALLLICVGVCSsGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGR 599
Cdd:cd18541 22 IGRAIDaltAGTLTASQLLR--YALLILLLALLI-GIFRflwrylifGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 600 LLNCFAGDLEQLDQLL-P--IFSEQFLVLSLMVIAVLLIVSV-LSPYILLMgAIIMVICFIYY--MMFKKaigvFKRL-E 672
Cdd:cd18541 99 LMARATNDLNAVRMALgPgiLYLVDALFLGVLVLVMMFTISPkLTLIALLP-LPLLALLVYRLgkKIHKR----FRKVqE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 673 NYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 749
Cdd:cd18541 174 AFSD--LSDRVQESFSGIRVIKAFVQEEAEIERFDKLNE---EYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYG 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
225-391 |
8.60e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.10 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 225 GNTGSGKSSLLSAI------------LEEMHLLEGSVGV-----QGSLAYVPQQA-----WIVSGNIRENIlmgGAYDKA 282
Cdd:PRK11144 31 GRSGAGKTSLINAIsgltrpqkgrivLNGRVLFDAEKGIclppeKRRIGYVFQDArlfphYKVRGNLRYGM---AKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 283 RYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI--FEECIKK 360
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLERLAR 176
|
170 180 190
....*....|....*....|....*....|...
gi 1034596369 361 TLrgKTVVL-VTHQLQ-YLEFCGQIILLENGKI 391
Cdd:PRK11144 177 EI--NIPILyVSHSLDeILRLADRVVVLEQGKV 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
211-400 |
1.22e-05 |
|
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: 48.51 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGS-----------------------LAYVPQQA----- 262
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAI---LGLLPPPGITSGEilfdgedllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 263 ------WIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELL---PFgdmteigerglNLSGGQKQRISLARAVYSDR 333
Cdd:COG0444 101 pvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 334 QIYLLDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 400
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQIlnlLKD-LQRE-LGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
208-391 |
1.26e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.16 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQ---AWI-------VSG-----NIRE 271
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvfqdpMMGtapsmTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMggAY---------------DKARYLQVLhcCSLNRDLEllpfgDM--TEIGerglNLSGGQKQRISLARAVYSDRQ 334
Cdd:COG1101 102 NLAL--AYrrgkrrglrrgltkkRRELFRELL--ATLGLGLE-----NRldTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 335 IYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENGKI 391
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
211-401 |
1.34e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQ----AWIVSGNIREN 272
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITESrrdnGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILM---------GGAY------------DKARYLQVLHCCSLNRDlellpfgdmteIGErglnLSGGQKQRISLARAVYS 331
Cdd:PRK09700 362 MAIsrslkdggyKGAMglfhevdeqrtaENQRELLALKCHSVNQN-----------ITE----LSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 332 DRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKI------CENGTHSELM 401
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLtqiltnRDDMSEEEIM 503
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
206-414 |
1.54e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMH---LLEGSVGVQGSLAYVPQQAWIVSGNiRENILMGGAY 279
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQSgeiKIDGITISKENLKEIRKKIGIIFQN-PDNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 --DKARYLQvlhccslNRdleLLPFGDMTEIGE--------------RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 343
Cdd:PRK13632 102 edDIAFGLE-------NK---KVPPKKMKDIIDdlakkvgmedyldkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 344 AVDAHvGKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKgkyaQLIQKM 414
Cdd:PRK13632 172 MLDPK-GKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK----EILEKA 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
211-401 |
1.58e-05 |
|
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: 47.43 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 211 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQAWIVSG-NIRENILM 275
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 GGAYDKARYLQVLHCCSLNRDL-----ELLpfgDMTEIGER-----GlNLSGGQKQRISLARAVYSDRQIYLLDDP---L 342
Cdd:cd03219 99 AAQARTGSGLLLARARREEREAreraeELL---ERVGLADLadrpaG-ELSYGQQRRLEIARALATDPKLLLLDEPaagL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 343 SAVDAHVGKHIFEEcIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELM 401
Cdd:cd03219 175 NPEETEELAELIRE-LRE--RGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
832-1041 |
1.84e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.89 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 832 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL-FRLVEPM--AGRILIDGVdicSIGLEDLRSKLSVIPQDPVL 908
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 909 L-SGTIRFNLD-----PFDRHTD-----QQIWDALERTFLTKAiskfpKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 977
Cdd:TIGR00955 111 IpTLTVREHLMfqahlRMPRRVTkkekrERVDEVLQALGLRKC-----ANTRIGVPGRVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 978 KIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNC--DHILVMGNGKVVEFDRPE 1041
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPD 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
315-402 |
2.30e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTL---RGKTVVLVTHQLQ---YLefCGQIILLEN 388
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLqreHGLAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 1034596369 389 GKICENGTHSELMQ 402
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
839-1058 |
2.80e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 839 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLLSGTI 913
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RFN-----LDPFDRHTDQqIWDALERTFLTKAISKFPKKlhTDVVENG-GNFSVGERQLLCIARAVLRNSKIILIDEATA 987
Cdd:PRK10762 348 KENmsltaLRYFSRAGGS-LKHADEQQAVSDFIRLFNIK--TPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 988 SIDM----ETDTLIQRTIREafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPEVLRKKpgslfaaLMATA 1058
Cdd:PRK10762 425 GVDVgakkEIYQLINQFKAE---GLSIILVSSEMPEVLGmSDRILVMHEGRISgEFTREQATQEK-------LMAAA 491
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
581-749 |
3.03e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.18 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 581 FNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVIcfIYYMM 660
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPL--IIAGT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 661 FKkaigvF-KRLE-NYSR-----SPLFSHILNSLQGLSSIHVYGkTEDFisQFKRLTDAQNNYLllflsSTRWMALRLEI 733
Cdd:cd18565 172 YW-----FqRRIEpRYRAvreavGDLNARLENNLSGIAVIKAFT-AEDF--ERERVADASEEYR-----DANWRAIRLRA 238
|
170 180
....*....|....*....|..
gi 1034596369 734 M----TNLVTLA--VALFVAFG 749
Cdd:cd18565 239 AffpvIRLVAGAgfVATFVVGG 260
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
205-403 |
3.44e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.05 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 205 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHL-LEGSVGVQGS----------LAYVPQQAWIV-----SGN 268
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQ-LLNGLHVpTQGSVRVDDTlitstsknkdIKQIRKKVGLVfqfpeSQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 IRENILMGGAYD-----------KARYLQVLHCCSLNRDL-ELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIY 336
Cdd:PRK13649 99 FEETVLKDVAFGpqnfgvsqeeaEALAREKLALVGISESLfEKNPF-----------ELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 337 LLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQK 403
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
208-400 |
3.51e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.72 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS---------------LAYVPQQAWIVSGNIREN 272
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMG-------GAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 346 DAHVGKHI--FEECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 400
Cdd:PRK13652 169 DPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-400 |
3.78e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTH-QLQYLEFCGQIILLENGKICE 393
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 1034596369 394 NGTHSEL 400
Cdd:PRK14247 226 WGPTREV 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
208-396 |
3.99e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSL--AYVPQQAWI-------VS-------GNIRE 271
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYLdttlpltVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 272 NILMGGAYDKARYLqvlhccsLNRDLEllpfgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD--AHV 349
Cdd:PRK09544 100 DILPALKRVQAGHL-------IDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034596369 350 GKHIFEECIKKTLrGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 396
Cdd:PRK09544 158 ALYDLIDQLRREL-DCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGT 203
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
551-772 |
4.16e-05 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 46.62 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 551 ALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVI 630
Cdd:cd18548 49 ALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 631 AVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLN-----SLQGLSSIHVYGKtEDFi 703
Cdd:cd18548 129 GAIIMAFRINPKLaLILLVAIPILALVVFLIMKKAIPLFKKVqKKLDR-------LNrvvreNLTGIRVIRAFNR-EDY- 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 704 sQFKRLTDAQNNYLLLFLSSTRWMALRLEIMT---NLVTLAVALFVAFGISSTPYSF-KVMA-VNIVLQLASSF 772
Cdd:cd18548 200 -EEERFDKANDDLTDTSLKAGRLMALLNPLMMlimNLAIVAILWFGGHLINAGSLQVgDLVAfINYLMQILMSL 272
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1-112 |
4.87e-05 |
|
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: 46.48 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEVSdqriRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATA 80
Cdd:pfam00664 165 LRKLSRKEQKAVAKAS----SVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
90 100 110
....*....|....*....|....*....|....
gi 1034596369 81 V--WVLIHTSLKLKLTASMAFSMLASLNLLRLSV 112
Cdd:pfam00664 241 LalWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
208-403 |
4.87e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 46.28 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------LAYVPQQAWIVSGNiRENILMGG--AY 279
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnFEKLRKHIGIVFQN-PDNQFVGSivKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 280 DKARYLQvlhccslNrdlELLPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:PRK13648 104 DVAFGLE-------N---HAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 346 DAHVGKHIFeECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 403
Cdd:PRK13648 174 DPDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
551-750 |
5.45e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 46.27 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 551 ALLLICVGVcSSGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQF 622
Cdd:cd18542 42 ALLILGVAL-LRGVFRylqgylaeKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 623 LVLSLMVIAVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLNS-LQ-GLSSIHV--- 695
Cdd:cd18542 121 VRAVLLFIGALIIMFSINWKLtLISLAIIPFIALFSYVFFKKVRPAFEEIrEQEGE-------LNTvLQeNLTGVRVvka 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 696 YGKtEDF-ISQFkrltDAQN-NYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 750
Cdd:cd18542 194 FAR-EDYeIEKF----DKENeEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGG 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
851-1038 |
5.68e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 851 VVGIVGRTGSGKSSLgmalFRLV----EPMAGRILI-DGVDICSI-----GLEDLRSKLSVIP--QDPVLLSGTI----- 913
Cdd:PRK11819 352 IVGIIGPNGAGKSTL----FKMItgqeQPDSGTIKIgETVKLAYVdqsrdALDPNKTVWEEISggLDIIKVGNREipsra 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 ---RFNLdpfdRHTDQQiwdalertfltkaiskfpKKLhtdvvengGNFSVGERQLLCIARAVLRNSKIILIDEATASID 990
Cdd:PRK11819 428 yvgRFNF----KGGDQQ------------------KKV--------GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 991 MET-----DTLiqrtirEAFQGCTVlVIAH------RVTTvlncdHILVM-GNGKVVEFD 1038
Cdd:PRK11819 478 VETlraleEAL------LEFPGCAV-VISHdrwfldRIAT-----HILAFeGDSQVEWFE 525
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
315-403 |
5.79e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 391
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
90
....*....|..
gi 1034596369 392 CENGTHSELMQK 403
Cdd:PRK11650 214 EQIGTPVEVYEK 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
209-415 |
6.62e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 209 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAwIVSGNIRENILM 275
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNA-TTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 276 GgaydKARYLQVLHCCSLNRDLELLPFGDMTEIGERGL------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahV 349
Cdd:PRK10253 103 A----RGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLadqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--I 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 350 GKHI-FEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQkkgkyAQLIQKMH 415
Cdd:PRK10253 177 SHQIdLLELLSELNRekGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT-----AELIERIY 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
184-371 |
6.64e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 184 ASEGMTRPRDALgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAW 263
Cdd:PRK13543 13 AAHALAFSRNEE----------PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 IVS-----GNIRENIlmgGAYDKARYLQVLHCCSLNRdlelLPFGDMTEIGERGL------NLSGGQKQRISLARAVYSD 332
Cdd:PRK13543 83 FMAylghlPGLKADL---STLENLHFLCGLHGRRAKQ----MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034596369 333 RQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGKTVVLVT 371
Cdd:PRK13543 156 APLWLLDEPYANLDLE-GITLVNRMISAHLRGGGAALVT 193
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
822-1040 |
7.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 822 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 894
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 895 LRSKLSVIPQDP--VLLSGT----IRFNLDPFDRHTDQQIWDALERTFLTkAISK--FPKklhtdvveNGGNFSVGERQL 966
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETvlkdVAFGPQNFGVSQEEAEALAREKLALV-GISEslFEK--------NPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 967 LCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 1040
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
208-399 |
8.14e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.81 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQAWIV---------SGNIR 270
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKVGLVfqypeyqlfEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 271 ENILMG----GAYDKARYLQVlhccslNRDLEL--LPFGDMTEigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 344
Cdd:PRK13637 103 KDIAFGpinlGLSEEEIENRV------KRAMNIvgLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 345 VDAHVGKHIFEECikKTLRGK---TVVLVTHQLQYL-EFCGQIILLENGKICENGTHSE 399
Cdd:PRK13637 175 LDPKGRDEILNKI--KELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
313-399 |
9.77e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 313 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-------AHVGKHIFEEcikktlRGKTVVLVTHQLQYLEFCGQIIL 385
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKTALVVEHDLAVLDYLSDRIH 143
|
90
....*....|....
gi 1034596369 386 LENGKICENGTHSE 399
Cdd:cd03222 144 VFEGEPGVYGIASQ 157
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
198-368 |
1.25e-04 |
|
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: 44.18 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 198 EEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 277
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL---ANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 278 AYDkarylqvLHCCSLNRDlELLPF------GDMTeigeRGlnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 351
Cdd:cd03233 90 EED-------VHFPTLTVR-ETLDFalrckgNEFV----RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180
....*....|....*....|
gi 1034596369 352 HIFeECIK---KTLRGKTVV 368
Cdd:cd03233 156 EIL-KCIRtmaDVLKTTTFV 174
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
208-404 |
1.38e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.22 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIvsgNIRENIlmGGAYDKARylQV 287
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLM---KLRESV--GMVFQDPD--NQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 288 LHCCSLNRDLEL------LPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 347
Cdd:PRK13636 95 LFSASVYQDVSFgavnlkLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 348 hVGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKK 404
Cdd:PRK13636 175 -MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
208-373 |
1.55e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMH--LLEGSVGVQGSlaYVPQQAWIVSGNIRENILMggaYDKARYL 285
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNR--KPTKQILKRTGFVTQDDIL---YPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 286 QVLHCCSLNRDLELLPFGDMTE-----IGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILvaesvISELGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*..
gi 1034596369 347 AHVGKHIFEECIKKTLRGKTVVLVTHQ 373
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
837-1035 |
1.61e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-RLVEPMA-------GRILIDGVDICSIGLEDLRSKLSVIPQ---- 904
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 905 ------DPVLLSGtiRFnldPFDR------HTDQQI-WDALERTFLTKAISKfpkklhtDVVenggNFSVGERQLLCIAR 971
Cdd:PRK13547 95 afafsaREIVLLG--RY---PHARragaltHRDGEIaWQALALAGATALVGR-------DVT----TLSGGELARVQFAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596369 972 AV---------LRNSKIILIDEATASIDME-----TDTlIQRTIREAFQGctVLVIAHRVT-TVLNCDHILVMGNGKVV 1035
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAhqhrlLDT-VRRLARDWNLG--VLAIVHDPNlAARHADRIAMLADGAIV 234
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
570-750 |
2.01e-04 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 44.71 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 570 RKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSeQFL-------VLSLMVIAVLLIVSVLSpy 642
Cdd:cd18584 66 ARVKAELRRRLLARLLALGPALLRRQSSGELATLL---TEGVDALDGYFA-RYLpqlvlaaIVPLLILVAVFPLDWVS-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 643 illmgAIIMVICF---IYYMMFkkaIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAq 713
Cdd:cd18584 140 -----ALILLVTApliPLFMIL---IGKAaqaasrRQWAALSR--LSGHFLDRLRGLPTLKLFGRARAQAARIARASED- 208
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034596369 714 nnylllFLSSTrwMA-LRLEIMTNLV-----TLAVALfVAFGI 750
Cdd:cd18584 209 ------YRRRT--MKvLRVAFLSSAVleffaTLSIAL-VAVYI 242
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
214-379 |
2.74e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 214 VVSKGMMLGVCGNTGSGKS---SLLS-----------------AILE-----EMH-----LLEGSVGVQGSLAYVPQQAW 263
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTtavKILSgelipnlgdyeeepswdEVLKrfrgtELQnyfkkLYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 IVSGNIREnILMG----GAYDkarylqvlhccslnrdlELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:PRK13409 175 VFKGKVRE-LLKKvderGKLD-----------------EVVERLGLENILDRDIsELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 339 DDPLSAVDahvgkhIFE-----ECIKKTLRGKTVVLVTHQLQYLEF 379
Cdd:PRK13409 237 DEPTSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDLAVLDY 276
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
840-1015 |
3.62e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.87 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 840 HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSVIPQDP---VLLSGT--IR 914
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPgikTELTALenLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 915 FNLDPFDRHTDQQIWDALERTFLTKaiskfpkklhtdvVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME 992
Cdd:PRK13538 97 FYQRLHGPGDDEALWEALAQVGLAG-------------FEDvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180
....*....|....*....|....
gi 1034596369 993 -TDTLIQRTIREAFQGCTVLVIAH 1015
Cdd:PRK13538 164 gVARLEALLAQHAEQGGMVILTTH 187
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
316-349 |
3.92e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 3.92e-04
10 20 30
....*....|....*....|....*....|....
gi 1034596369 316 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 349
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
206-417 |
3.93e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.46 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMhllEGSVGVQGS--------LAYVPQQAWIVSGNIRENIL 274
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLRPQ---KGAVLWQGKpldyskrgLLALRQQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 275 MGGA-YDKA---RYLQVLHCCSLNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhV 349
Cdd:PRK13638 92 YTDIdSDIAfslRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP-A 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596369 350 GKHIFEECIKKTL-RGKTVVLVTHQLQYL-EFCGQIILLENGKICENG------THSELMQKKGKYAQLIQKMHKE 417
Cdd:PRK13638 171 GRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAGLTQPWLVKLHTQ 246
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
598-774 |
4.10e-04 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 43.62 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 598 GRLLNCFAGDLEQLDQL-LPIFSEqFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-----VICFIYYMMfKKAIGVFKRl 671
Cdd:cd18585 92 GDLLNRIVADIDTLDNLyLRVLSP-PVVALLVILATILFLAFFSPALALILLAGLllagvVIPLLFYRL-GKKIGQQLV- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 672 enYSRSPLFSHILNSLQGLSSIHVYGKTEdfiSQFKRLTDAQNNYL--------LLFLSSTrWMALRLEIMTNLVTLAVA 743
Cdd:cd18585 169 --QLRAELRTELVDGLQGMAELLIFGALE---RQRQQLEQLSDALIkeqrrlarLSGLSQA-LMILLSGLTVWLVLWLGA 242
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034596369 744 LFVAFGISSTPY----SFKVMAV-NIVLQLASSFQA 774
Cdd:cd18585 243 PLVQNGALDGALlamlVFAVLASfEAVAPLPLAFQY 278
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
208-414 |
4.10e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.24 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILE----EMhLLEGSV------------GVqgslAYVPQQAWIVSG- 267
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLmkiLSGVYQpdsgEI-LLDGEPvrfrsprdaqaaGI----AIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 268 NIRENILMG------GAYDK----ARYLQVLHCCSLNRDLEllpfgdmTEIGErglnLSGGQKQRISLARAVYSDRQIYL 337
Cdd:COG1129 95 SVAENIFLGreprrgGLIDWramrRRARELLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 338 LDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELmqkkgKYAQLIQKM 414
Cdd:COG1129 164 LDEPTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL-----TEDELVRLM 236
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
825-1036 |
4.32e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 825 QDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF--RLVEPMAGRILIDGVDICSIGLEDlRSKLSVI 902
Cdd:PRK09580 5 KDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 903 P--QDPVLLSGT-----IRFNLDPFDRHTDQQIWDALE-RTFLTKAIS--KFPKKLHTDVVENGgnFSVGERQLLCIARA 972
Cdd:PRK09580 82 MafQYPVEIPGVsnqffLQTALNAVRSYRGQEPLDRFDfQDLMEEKIAllKMPEDLLTRSVNVG--FSGGEKKRNDILQM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 973 VLRNSKIILIDEATASIDMETDTLIQR---TIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1036
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
206-348 |
4.39e-04 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 42.81 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 206 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhlleGSVGVQ-GSLAYVPQQAWI--VSGNIREnIL------MG 276
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIY-------GNYLPDsGSILVRHDGGWVdlAQASPRE-ILalrrrtIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 277 ------------GAYD----KARYLQVLHCCSLNRDLELLpfgDMTEIGERGLNL-----SGGQKQRISLARAVYSDRQI 335
Cdd:COG4778 97 yvsqflrviprvSALDvvaePLLERGVDREEARARARELL---ARLNLPERLWDLppatfSGGEQQRVNIARGFIADPPL 173
|
170
....*....|...
gi 1034596369 336 YLLDDPLSAVDAH 348
Cdd:COG4778 174 LLLDEPTASLDAA 186
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
541-751 |
4.84e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 43.34 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 541 SFYQLVYGLNALLL--ICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAgDLEQLDQ----- 613
Cdd:cd18566 40 TLQVLVIGVVIAILleSLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREfltgq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 614 -LLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGAIIMVICFIYYMMfKKAIGvfKRLENYSRSplFSHILNSLQGLSS 692
Cdd:cd18566 119 aLLALLDLPFVLIFLGLIWYLGGKLVLVP-LVLLGLFVLVAILLGPIL-RRALK--ERSRADERR--QNFLIETLTGIHT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 693 IHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRwMALRLEIMTNLVT-LAVALFVAFGIS 751
Cdd:cd18566 193 IKAMAMEPQMLRRYERL---QANAAYAGFKVAK-INAVAQTLGQLFSqVSMVAVVAFGAL 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
315-435 |
6.73e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLR-GKTVVLVTHQLQYL-EFCGQIILLENGKIC 392
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVaEAAHKIIVMYAGQVV 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034596369 393 ENGTHSELMQK-KGKYAQLIQKmhkeATSDMLQDTAKIAEKPKV 435
Cdd:PRK11022 234 ETGKAHDIFRApRHPYTQALLR----ALPEFAQDKARLASLPGV 273
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
564-750 |
7.26e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 42.88 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 564 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNcFAGDLEQLDQLLpifSEQFLVL---SLMVIAVLLIVSVLS 640
Cdd:cd18555 65 IIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLF-RANSNVYIRQIL---SNQVISLiidLLLLVIYLIYMLYYS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 641 PYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLtdaQNNYLLLF 720
Cdd:cd18555 141 PLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENL---FKKQLKAF 217
|
170 180 190
....*....|....*....|....*....|
gi 1034596369 721 LSSTRWMALRLEIMTNLVTLAVALFVAFGI 750
Cdd:cd18555 218 KKKERLSNILNSISSSIQFIAPLLILWIGA 247
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
536-750 |
7.31e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 42.84 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 536 DNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLL 615
Cdd:cd18545 35 DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 616 -----PIFSEQFLVlsLMVIAVLLIVSV-LSpyiLLMGAIIMVICFIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQG 689
Cdd:cd18545 115 sngliNLIPDLLTL--VGIVIIMFSLNVrLA---LVTLAVLPLLVLVVFLLRRRARKAWQRVRK-KISNLNAYLHESISG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596369 690 LSSIHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 750
Cdd:cd18545 189 IRVIQSFAREDENEEIFDEL---NRENRKANMRAVRLNALFWPLVELISALGTALVYWYGG 246
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
574-749 |
8.47e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 42.65 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 574 TALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVI 653
Cdd:cd18561 69 QHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 654 CFIYYMMFKKAIGvfKRLENY--SRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnylllFLSSTRWM---- 727
Cdd:cd18561 149 IPLSPALWDRLAK--DTGRRHwaAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAED-------LRQATMKVlavs 219
|
170 180
....*....|....*....|..
gi 1034596369 728 ALRLEIMTNLVTLAVALFVAFG 749
Cdd:cd18561 220 LLSSGIMGLATALGTALALGVG 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
315-401 |
8.63e-04 |
|
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: 43.25 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKI 391
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKI 506
|
90
....*....|
gi 1034596369 392 CENGTHSELM 401
Cdd:TIGR03269 507 VKIGDPEEIV 516
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1-126 |
8.81e-04 |
|
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: 42.59 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 1 MTRMAVKAQHHTSEvsDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKC----GLVQSLTSITLFIIPT 76
Cdd:cd18559 159 ASSRQLKRLESVSK--DPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIvylrALAVRLWCVGPCIVLF 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1034596369 77 VATAVWVLIHTSlkLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSK 126
Cdd:cd18559 237 ASFFAYVSRHSL--AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
960-1037 |
9.29e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 960 SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIrEAFQGcTVLVIAH-RV---TTVLNCdhILVMGNGKVV 1035
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVTEC--WIFEGNGKIG 517
|
..
gi 1034596369 1036 EF 1037
Cdd:PRK11147 518 RY 519
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
315-404 |
1.27e-03 |
|
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: 42.50 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 393
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKG 483
|
90
....*....|.
gi 1034596369 394 NGTHSELMQKK 404
Cdd:TIGR02633 484 DFVNHALTQEQ 494
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
534-657 |
1.49e-03 |
|
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: 41.76 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 534 IADNPQLSFYQLVYGLnALLLICVGVCS---SGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQ 610
Cdd:cd18572 27 VADGSREAFYRAVLLL-LLLSVLSGLFSglrGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQK 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034596369 611 LDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VICFIY 657
Cdd:cd18572 106 VSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVpVIALIT 153
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
282-384 |
1.54e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 282 ARYLQVLHccslnrDLELlpfgDMTEIGERGLNLSGGQKQRISLARAVY---SDRQIYLLDDPLSAVDAHVGKHIFEECI 358
Cdd:cd03271 147 ARKLQTLC------DVGL----GYIKLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQ 216
|
90 100
....*....|....*....|....*.
gi 1034596369 359 KKTLRGKTVVLVTHQLQYLEFCGQII 384
Cdd:cd03271 217 RLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
291-459 |
1.57e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 291 CSLNrdLELLPFGdmteigeRGL-NLSGGQKQRISLARAVYSDRQ---IYLLDDPLSAVDAHVGKHIFEECIKKTLRGKT 366
Cdd:PRK00635 794 CSLG--LDYLPLG-------RPLsSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHT 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 367 VVLVTHQLQYLEFCGQIILL------ENGKICENGTHSELMQKKGKYAQLIQKMHKEAtsdmlQDTAKIAEKPKVESQAL 440
Cdd:PRK00635 865 VVIIEHNMHVVKVADYVLELgpeggnLGGYLLASCSPEELIHLHTPTAKALRPYLSSP-----QELPYLPDPSPKPPVPA 939
|
170 180
....*....|....*....|....*
gi 1034596369 441 ATSLEESLNGN------AVPEHQLT 459
Cdd:PRK00635 940 DITIKNAYQHNlkhidlSLPRNALT 964
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
316-425 |
1.73e-03 |
|
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: 42.69 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 316 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICEN 394
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEaLCTRLAIMVKGAFQCL 2151
|
90 100 110
....*....|....*....|....*....|.
gi 1034596369 395 GTHSELMQKKGKYAQLIQKMhKEATSDMLQD 425
Cdd:TIGR01257 2152 GTIQHLKSKFGDGYIVTMKI-KSPKDDLLPD 2181
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
531-749 |
1.85e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 41.70 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 531 LGNIADNPQLSFYQLVYGLNALLLICV----GVCSSG---IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 603
Cdd:cd18576 19 AGQLIDAALGGGDTASLNQIALLLLGLfllqAVFSFFriyLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 604 FAGDLEQLDQ----LLPIFSEQFLVLslmVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVFKRLENYSR--- 676
Cdd:cd18576 99 LSNDVTQIQDtlttTLAEFLRQILTL---IGGVVLLFFISWKLTLLMLATVPVVVLV-------AVLFGRRIRKLSKkvq 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 677 ---SPLFSHILNSLQGLSSIHVYGKtEDF-ISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 749
Cdd:cd18576 169 delAEANTIVEETLQGIRVVKAFTR-EDYeIERYRKALER---VVKLALKRARIRALFSSFIIFLLFGAIVAVLWYG 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
208-390 |
2.10e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQAWIV-SGNIREN 272
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELNLVlQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 273 ILMGgaydkaRY----LQVLHCcSLNRDLELLpFGDM---TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 345
Cdd:PRK10982 94 MWLG------RYptkgMFVDQD-KMYRDTKAI-FDELdidIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034596369 346 DAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGK 390
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
957-1044 |
2.10e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 957 GNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1034
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
90
....*....|....*.
gi 1034596369 1035 V------EFDRPEVLR 1044
Cdd:PRK10982 470 AgivdtkTTTQNEILR 485
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
313-374 |
2.18e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596369 313 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlrGKTVVLVTHQL 374
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNRV---GVTVLMATHDI 197
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
821-880 |
2.27e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.23 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596369 821 EIIFQDYHMKYRDNTPT---VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRI 880
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
837-1039 |
2.67e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 837 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP--MAGRILIDGVDICsiglEDLRSKLSVIPQDPVLLSG-TI 913
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPT----KQILKRTGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 914 RFNLdpfdrhtdqqIWDALERtfLTKAISKFPKKLHTDVV---------EN---GGNF----SVGERQLLCIARAVLRNS 977
Cdd:PLN03211 158 RETL----------VFCSLLR--LPKSLTKQEKILVAESViselgltkcENtiiGNSFirgiSGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 978 KIILIDEATASIDMETD-TLIQRTIREAFQGCTVLVIAH----RVTTVLncDHILVMGNGKVVEFDR 1039
Cdd:PLN03211 226 SLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGK 290
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
214-374 |
2.98e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.69 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 214 VVSKGMMLGVCGNTGSGKS---SLLS-----------------AILE-----EMH-----LLEGSVGVqgslAYVPQQ-- 261
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKStalKILSgelkpnlgdydeepswdEVLKrfrgtELQdyfkkLANGEIKV----AHKPQYvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 262 --AWIVSGNIREniLMGGAYDKARYLQVLhccslnrdlELLpfgDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLL 338
Cdd:COG1245 171 liPKVFKGTVRE--LLEKVDERGKLDELA---------EKL---GLENILDRDIsELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034596369 339 DDPLSAVDahvgkhIFE-----ECIKKTLR-GKTVVLVTHQL 374
Cdd:COG1245 237 DEPSSYLD------IYQrlnvaRLIRELAEeGKYVLVVEHDL 272
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
851-871 |
3.13e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.90 E-value: 3.13e-03
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
208-346 |
3.29e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 208 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQqawivsG---N-- 268
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------GlgkNly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 269 ----IRENI-----LMG-GAYDKARYLQvlhccSLNRDLELLPFGDmteigeR--GlNLSGGQKQRISLARAVYSDRQIY 336
Cdd:NF033858 91 ptlsVFENLdffgrLFGqDAAERRRRID-----ELLRATGLAPFAD------RpaG-KLSGGMKQKLGLCCALIHDPDLL 158
|
170
....*....|
gi 1034596369 337 LLDDPLSAVD 346
Cdd:NF033858 159 ILDEPTTGVD 168
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
315-346 |
3.47e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 40.87 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|..
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 346
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
576-712 |
4.12e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 40.57 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 576 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VIC 654
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVpLVV 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596369 655 FIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA 712
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWR-RWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE 214
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
576-749 |
4.58e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 40.48 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 576 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICF 655
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 656 IYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMT 735
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVN 237
|
170
....*....|....
gi 1034596369 736 NLVTLAVALFVAFG 749
Cdd:cd18554 238 TITDLAPLLVIGFA 251
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
310-403 |
4.64e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 310 ERGLN-LSGGQKQRISLARAVYSDRQ--IYLLDDP---LSAVDAHvgKHIfeECIKKtLR--GKTVVLVTHQLQYLEFCG 381
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIgiTYILDEPsigLHPQDTH--KLI--NVIKK-LRdqGNTVLLVEHDEQMISLAD 545
|
90 100
....*....|....*....|....*...
gi 1034596369 382 QIILLE------NGKICENGTHSELMQK 403
Cdd:PRK00635 546 RIIDIGpgagifGGEVLFNGSPREFLAK 573
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
316-391 |
4.83e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596369 316 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTlrgKTVVLVTHQLQYLE-FCGQIILLENGKI 391
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNtVVTDILHLHGQKL 419
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
551-749 |
6.63e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 39.78 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 551 ALLLICVGVCSSGIFTKVTRKAST----ALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLV-- 624
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGErllyDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVsl 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 625 LSLMVIAVLLIvsVLSPYILLMGAIIMVICFIyymmfkkAIGVFKRLEN--YSR-----SPLFSHILNSLQGLSSIHVYG 697
Cdd:cd18546 125 LTLVGIAVVLL--VLDPRLALVALAALPPLAL-------ATRWFRRRSSraYRRareriAAVNADLQETLAGIRVVQAFR 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034596369 698 KTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 749
Cdd:cd18546 196 RERRNAERFAELSDD---YRDARLRAQRLVAIYFPGVELLGNLATAAVLLVG 244
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
204-242 |
8.13e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 39.69 E-value: 8.13e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1034596369 204 LGPELHKINLVvSKGMMLgVCGNTGSGKSSLLSAILEEM 242
Cdd:COG2805 113 LPPVLKELAEL-PRGLVL-VTGPTGSGKSTTLAAMIDYI 149
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
315-401 |
8.45e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.39 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 315 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGK 390
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINlmlELQEK--QGISYIYVTQHLGMMKhISDQVLVMHQGE 227
|
90
....*....|.
gi 1034596369 391 ICENGTHSELM 401
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
201-389 |
9.23e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 201 GNSLGP--ELHKINLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHL-LEGSVGVQG--------SLAY------VPQQAW 263
Cdd:PRK09700 12 GKSFGPvhALKSVNLTVYPGEIHALLGENGAGKSTLMK-VLSGIHEpTKGTITINNinynkldhKLAAqlgigiIYQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596369 264 IVSG-NIRENILMGG--------------AYDKARYLQVLHCCSLNRDLEllpfgdmteigERGLNLSGGQKQRISLARA 328
Cdd:PRK09700 91 VIDElTVLENLYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596369 329 VYSDRQIYLLDDPLSAVDAHVGKHIFeeCIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENG 389
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLF--LIMNQLRkeGTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| |
