|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
85-1333 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 730.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRrgiEKASVLLVMLRFQRTRLI 164
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK---PKPWLLRALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 165 FDALLGICFCIASVLGPILIiPKILEySEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFE 244
Cdd:PLN03130 305 LGGFFKIGNDLSQFVGPLLL-NLLLE-SMQNGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 245 KLIQF--KSVIHITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYTAFIAILCYLLVFPL 316
Cdd:PLN03130 383 KSLRLthEGRKKFTSGKITNLMTTDAEALqqicqqLHTLWSAPFRIIIAMVLL------YQQLGVASLIGSLMLVLMFPI 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 317 AVFM-TRMavkaQHHTSE---VSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:PLN03130 457 QTFIiSKM----QKLTKEglqRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 393 IPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPS- 471
Cdd:PLN03130 533 IPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGl 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 472 KALVFEEATLSWQQTcpgivngaleLERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKS 551
Cdd:PLN03130 613 PAISIKNGYFSWDSK----------AER-------------------------PTLSNINLDVPVGSLVAIVGSTGEGKT 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 552 SLLSAILEEMHLLE-GSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGER 630
Cdd:PLN03130 658 SLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGER 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:PLN03130 738 GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 711 CENGTHSELMqKKGKyaqLIQK-MHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQ-------LTQEEE 782
Cdd:PLN03130 818 KEEGTYEELS-NNGP---LFQKlMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKskegksvLIKQEE 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 783 MEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGtnssrESNGTMadlgniadnpqlsFY 862
Cdd:PLN03130 894 RETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPL-------------FY 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 863 QLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFL 942
Cdd:PLN03130 956 NLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFL 1035
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 943 --VLSLMVIAVLL-IVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTE 1019
Cdd:PLN03130 1036 gqIFQLLSTFVLIgIVSTISLWAIMPLLVLFYGAYLYYQSTAREV---KRLDSITRSPVYAQFGEALNGLSTIRAY-KAY 1111
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1020 DFISQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS--STPYSFKV---MAVNIVLQLASSFQA 1093
Cdd:PLN03130 1112 DRMAEINgRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGraENQAAFAStmgLLLSYALNITSLLTA 1191
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1094 TARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGI 1173
Cdd:PLN03130 1192 VLRLASLAENSLNAVERVGTYIDL-PSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGI 1270
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1174 VGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALER 1253
Cdd:PLN03130 1271 VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLER 1350
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1254 TFLTKAI-------------------------------------ILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIA 1295
Cdd:PLN03130 1351 AHLKDVIrrnslgldaevseagenfsvgqrqllslarallrrskILVlDEATAAVDVRTDALIQKTIREEFKSCTMLIIA 1430
|
1290 1300 1310
....*....|....*....|....*....|....*...
gi 21729876 1296 HRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1333
Cdd:PLN03130 1431 HRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
74-1333 |
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: 724.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 74 FRPKPRF-------PAPQPLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRRGI 146
Cdd:TIGR00957 185 FSDKSPLfsetnhdPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 147 EKASVL-----------------------LVMLRFQRTR--LIFDALLG-------ICFCIASVLGPILII-PKILE--- 190
Cdd:TIGR00957 265 QPVSAVygkkdpskpkgssqldaneeveaLIVKSPHKPRkpSLFKVLYKtfgpyflMSFCFKAIHDLMMFIgPQILSlli 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 191 -YSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEKLIQFKSVIHITS--GEAISFFTGD 267
Cdd:TIGR00957 345 rFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 268 VNYLFEGVCYgpLVLITCASL-VICSIssYFI---IGYTAFIAILCYLLVFPL--AVFMTRMAVKAQHHTSEvsDQRIRV 341
Cdd:TIGR00957 425 AQRFMDLATY--INMIWSAPLqVILAL--YFLwlnLGPSVLAGVAVMVLMVPLnaVMAMKTKTYQVAHMKSK--DNRIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 342 TSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVAT--AVWVLIHTSLKLKLTASMAFS 419
Cdd:TIGR00957 499 MNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVAliTFAVYVTVDENNILDAEKAFV 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 420 MLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQES---PVFYVQTLQD-PSKALVFEEATLSWQQTCPgivngal 495
Cdd:TIGR00957 579 SLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEElepDSIERRTIKPgEGNSITVHNATFTWARDLP------- 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 496 elernghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLA 575
Cdd:TIGR00957 652 -----------------------------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 576 YVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIY 655
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 656 LLDDPLSAVDAHVGKHIFEECI--KKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI--- 730
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLrty 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 731 ----QKMHKEATSDMLQdTAKIAEKPKVESQALAT-----------SLEESLNGNAVPEH----------------QLTQ 779
Cdd:TIGR00957 863 apdeQQGHLEDSWTALV-SGEGKEAKLIENGMLVTdvvgkqlqrqlSASSSDSGDQSRHHgssaelqkaeakeetwKLME 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 780 EEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVfLTIFSFWWLSYWleqgsgtnssreSNGTMADLGNIADNPQL 859
Cdd:TIGR00957 942 ADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHV-SALASNYWLSLW------------TDDPMVNGTQNNTSLRL 1008
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 860 SFYQLVYGLN--ALLLICVGVCSSGIFtkvtrkASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIF 937
Cdd:TIGR00957 1009 SVYGALGILQgfAVFGYSMAVSIGGIQ------ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPV 1082
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 938 SEQFLVLSLMVIAVLLIVSVLSPyilLMGAIIMVICFIYYMMFKKAIGV---FKRLENYSRSPLFSHILNSLQGLSSIHV 1014
Cdd:TIGR00957 1083 IKMFMGSLFNVIGALIVILLATP---IAAVIIPPLGLLYFFVQRFYVASsrqLKRLESVSRSPVYSHFNETLLGVSVIRA 1159
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1015 YGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQAT 1094
Cdd:TIGR00957 1160 FEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWL 1239
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1095 ARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIV 1174
Cdd:TIGR00957 1240 VRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIV 1318
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1175 GRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALE-- 1252
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALEla 1398
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1253 -----------------------------------RTFLTKAIILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAH 1296
Cdd:TIGR00957 1399 hlktfvsalpdkldhecaeggenlsvgqrqlvclaRALLRKTKILVlDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
|
1370 1380 1390
....*....|....*....|....*....|....*..
gi 21729876 1297 RVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1333
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
85-1336 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 681.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEvSRRgiEKASVLLVMLRFQRTRLI 164
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE-SRR--PKPWLLRALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 165 FDALLGICFCIASVLGPIL---IIPKILEYSEEQLGnVVHGVGLCFALFLSECVKSLSFSSSWiinqRTAIRFRAAVSSF 241
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVIlshLLQSMQEGDPAWVG-YVYAFLIFFGVTFGVLCESQYFQNVG----RVGFRLRSTLVAA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 242 AFEKLIQF--KSVIHITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYTAFIAILCYLLV 313
Cdd:PLN03232 380 IFHKSLRLthEARKNFASGKVTNMITTDANALqqiaeqLHGLWSAPFRIIVSMVLL------YQQLGVASLFGSLILFLL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 314 FPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFII 393
Cdd:PLN03232 454 IPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSI 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 394 PTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQT-LQDPSK 472
Cdd:PLN03232 534 PVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPpLQPGAP 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 473 ALVFEEATLSWQqtcpgivngaLELERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSS 552
Cdd:PLN03232 614 AISIKNGYFSWD----------SKTSK-------------------------PTLSDINLEIPVGSLVAIVGGTGEGKTS 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 553 LLSAILEEM-HLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERG 631
Cdd:PLN03232 659 LISAMLGELsHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERG 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 632 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKIC 711
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 712 ENGTHSELMQKKGKYAQLIQKMHK-EATSDMLQDTAKIAEK-PKVE---SQALATSLEESLNGNAVpehqLTQEEEMEEG 786
Cdd:PLN03232 819 EEGTFAELSKSGSLFKKLMENAGKmDATQEVNTNDENILKLgPTVTidvSERNLGSTKQGKRGRSV----LVKQEERETG 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 787 SLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSResngtmadlgniadnpqlSFYQLVY 866
Cdd:PLN03232 895 IISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSP------------------GFYIVVY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 867 GLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ----LLPIFSEQFL 942
Cdd:PLN03232 957 ALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRnvanLMNMFMNQLW 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 943 VLsLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTEDFI 1022
Cdd:PLN03232 1037 QL-LSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREV---RRLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRM 1111
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1023 SQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTP-----YSFKVMAVNIVLQLASSFQATAR 1096
Cdd:PLN03232 1112 AKINgKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLSGVLR 1191
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1097 IGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGR 1176
Cdd:PLN03232 1192 QASKAENSLNSVERVGNYIDL-PSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGR 1270
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1177 TGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFL 1256
Cdd:PLN03232 1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHI 1350
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1257 TKA--------------------------------------IILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRV 1298
Cdd:PLN03232 1351 KDVidrnpfgldaevseggenfsvgqrqllslarallrrskILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRL 1430
|
1290 1300 1310
....*....|....*....|....*....|....*...
gi 21729876 1299 TTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 1336
Cdd:PLN03232 1431 NTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
183-1336 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 616.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 183 LIIPKILE----YSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEK--LIQFKSVIH-- 254
Cdd:PTZ00243 261 LTLPVLLKyfvkFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKcfTISSKSLAQpd 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 255 ITSGEAISFFTGDVNYLFEGVCY------GPLVLITCASLVicsissYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQ 328
Cdd:PTZ00243 341 MNTGRIINMMSTDVERINSFMQYcmylwsSPMVLLLSILLL------SRLVGWCALMAVAVLLVTLPLNGAIMKHQMAAR 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 329 HHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSL 408
Cdd:PTZ00243 415 RKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 409 KLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFlqESPVFYVQTLQDPSK--------------AL 474
Cdd:PTZ00243 495 GHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFL--ECDNATCSTVQDMEEywreqrehstacqlAA 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 475 VFEEAT-----------------------LSW----------QQTCPGIVNGALE----LERNGHASEGMTRPRDALGPE 517
Cdd:PTZ00243 573 VLENVDvtafvpvklprapkvktsllsraLRMlcceqcrptkRHPSPSVVVEDTDygspSSASRHIVEGGTGGGHEATPT 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 518 EEGNSLGPE--------------LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWI 583
Cdd:PTZ00243 653 SERSAKTPKmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWI 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 584 VSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 664 VDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK---KGKYAQLIQKMH-KEATS 739
Cdd:PTZ00243 813 LDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyATLAAELKENKDsKEGDA 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 740 DMLQDTAKIAE------KPKVESQALATSLEESLNGNAVpEHQLTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFV 813
Cdd:PTZ00243 893 DAEVAEVDAAPggavdhEPPVAKQEGNAEGGDGAALDAA-AGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATF 971
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 814 VLIVFLTIFSFWWLSYWleqgsGTNSSRESNGTmadlgniadnpqlsfYQLVYglnaLLLICVGVCSSGIFTKVT----R 889
Cdd:PTZ00243 972 AVTELVTVSSGVWLSMW-----STRSFKLSAAT---------------YLYVY----LGIVLLGTFSVPLRFFLSyeamR 1027
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 890 KASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLmgAII 969
Cdd:PTZ00243 1028 RGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLV--ALV 1105
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 970 MViCFIYY--MMFKKAIG-VFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWM 1046
Cdd:PTZ00243 1106 PC-GYLYYrlMQFYNSANrEIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWL 1184
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1047 ALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQAT----ARIGLETEAQFTAVERILQYMKMCVSEA 1122
Cdd:PTZ00243 1185 GVRVEFLSNIVVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATlnwlVRQVATVEADMNSVERLLYYTDEVPHED 1264
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1123 PLHM-----------------------EGTSCPQGWP---QHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGR 1176
Cdd:PTZ00243 1265 MPELdeevdalerrtgmaadvtgtvviEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGR 1344
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1177 TGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALE---- 1252
Cdd:PTZ00243 1345 TGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALElvgl 1424
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1253 ---------------------------------RTFLTK--AIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHR 1297
Cdd:PTZ00243 1425 rervasesegidsrvleggsnysvgqrqlmcmaRALLKKgsGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHR 1504
|
1290 1300 1310
....*....|....*....|....*....|....*....
gi 21729876 1298 VTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 1336
Cdd:PTZ00243 1505 LHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
85-1319 |
5.89e-147 |
|
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: 484.03 E-value: 5.89e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRRGiEKASVLLVMLRFQRTRLI 164
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK-KNPKLLNALRRCFFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 165 FDALLGICFCIASVLGPILIIPKILEY----SEEQLGNVVHGVGLCFaLFLsecVKSLSFSSSWIINQRTAIRFRAAVSS 240
Cdd:TIGR01271 84 FYGILLYFGEATKAVQPLLLGRIIASYdpfnAPEREIAYYLALGLCL-LFI---VRTLLLHPAIFGLHHLGMQMRIALFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 241 FAFEKLIQFKSVI--HITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAiLCYLLVfpLAV 318
Cdd:TIGR01271 160 LIYKKTLKLSSRVldKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCG-LGFLIL--LAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 319 F---MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI--I 393
Cdd:TIGR01271 237 FqacLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFsgF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 394 PTVATAV--WVLIHTSLKLKLTASMAFSMLASLNLLRLsvffVPIAVKGLTNSKSAVMRFKKFFLQESpvFYVQTLQDPS 471
Cdd:TIGR01271 317 FVVFLSVvpYALIKGIILRRIFTTISYCIVLRMTVTRQ----FPGAIQTWYDSLGAITKIQDFLCKEE--YKTLEYNLTT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 472 KALVFEEATLSWQQtcpGIvnGAL-ELERNGHASEGMTRPRDALGPEEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGK 550
Cdd:TIGR01271 391 TEVEMVNVTASWDE---GI--GELfEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 551 SSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGER 630
Cdd:TIGR01271 466 SSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:TIGR01271 546 GITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVC 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 711 CENGTHSELMQKKGKYAQLI------QKMHKEATSDMLQDT---------------------------AKIAEKPK---- 753
Cdd:TIGR01271 626 YFYGTFSELQAKRPDFSSLLlgleafDNFSAERRNSILTETlrrvsidgdstvfsgpetikqsfkqppPEFAEKRKqsii 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 754 ---------------VESQALATSLEESLNG------NAVPE-------------------------------------- 774
Cdd:TIGR01271 706 lnpiasarkfsfvqmGPQKAQATTIEDAVREpserkfSLVPEdeqgeeslprgnqyhhglqhqaqrrqsvlqlmthsnrg 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 775 ----HQLT--------------------------------------QEEEMEE----------GSLSWRVYHHYIQAAGG 802
Cdd:TIGR01271 786 enrrEQLQtsfrkkssitqqnelaseldiysrrlskdsvyeiseeiNEEDLKEcfaderenvfETTTWNTYLRYITTNRN 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 803 yMVSCIIFFFVvliVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQL----SFYQLVYglnalllICVGV 878
Cdd:TIGR01271 866 -LVFVLIFCLV---IFLAEVAASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIitptSAYYIFY-------IYVGT 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 879 CSS----GIF-------TKVTrkASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 947
Cdd:TIGR01271 935 ADSvlalGFFrglplvhTLLT--VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLI 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 948 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 1027
Cdd:TIGR01271 1013 VLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHK 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1028 LTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAlFVAFGISSTpysfKVMAVNIVLQLA----SSFQATARIGLETEA 1103
Cdd:TIGR01271 1093 ALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVT-FIAIGTNQD----GEGEVGIILTLAmnilSTLQWAVNSSIDVDG 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1104 QFTAVERILQYMKMCVSEAP-------------LHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEV 1170
Cdd:TIGR01271 1168 LMRSVSRVFKFIDLPQEEPRpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQR 1247
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1171 VGIVGRTGSGKSSLGMALFRLVEpMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDA 1250
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKV 1326
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1251 -------------------------------------LERTFLTKA-IILIDEATASIDMETDTLIQRTIREAFQGCTVL 1292
Cdd:TIGR01271 1327 aeevglksvieqfpdkldfvlvdggyvlsnghkqlmcLARSILSKAkILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
|
1450 1460
....*....|....*....|....*..
gi 21729876 1293 VIAHRVTTVLNCDHILVMGNGKVVEFD 1319
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
802-1115 |
2.40e-131 |
|
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: 406.56 E-value: 2.40e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 802 GYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 881
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDN-STVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 882 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 961
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 962 ILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLS 1041
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1042 STRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
165-451 |
3.92e-112 |
|
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: 353.79 E-value: 3.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 165 FDALLGICFCIASVLGPILIIPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFE 244
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 245 KLIQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRMA 324
Cdd:cd18592 81 KILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 325 VKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLI 404
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 21729876 405 HTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRF 451
Cdd:cd18592 241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
517-709 |
7.64e-103 |
|
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: 325.19 E-value: 7.64e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 517 EEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 596
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 597 AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC 676
Cdd:cd03250 91 PFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC 170
|
170 180 190
....*....|....*....|....*....|....
gi 21729876 677 IKKTLR-GKTVVLVTHQLQYLEFCGQIILLENGK 709
Cdd:cd03250 171 ILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1139-1321 |
9.21e-94 |
|
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: 300.95 E-value: 9.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALE-------------------------------------RTFLTKA-I 1260
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALErvglkefveslpggldtvveeggenlsvgqrqllclaRALLRKSkI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1261 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 1321
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
789-1335 |
2.73e-85 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 290.53 E-value: 2.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 789 SWRVYHHYIQAAGGYMVSCII-FFFVVLIVFLTIFSFWWLSYWLEQGSgtnssreSNGTMADLGNIAdnpqlsfyqLVYG 867
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILaLLLLLLSALLELLLPLLLGRIIDALL-------AGGDLSALLLLL---------LLLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 868 LNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 947
Cdd:COG1132 69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 948 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 1027
Cdd:COG1132 149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1028 LTDaqnNYLLLFLSSTRWMAL---RLEIMTNLVTLAVALFVAFGISS---TPYSFkVMAVNIVLQLASSFQATARIGLET 1101
Cdd:COG1132 229 ANE---ELRRANLRAARLSALffpLMELLGNLGLALVLLVGGLLVLSgslTVGDL-VAFILYLLRLFGPLRQLANVLNQL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1102 EAQFTAVERILQYMkmcvSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGK 1181
Cdd:COG1132 305 QRALASAERIFELL----DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1182 SSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALE-------- 1252
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKaaqahefi 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1253 -----------------------------RTFLTKAIILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVL 1302
Cdd:COG1132 460 ealpdgydtvvgergvnlsggqrqriaiaRALLKDPPILIlDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
|
570 580 590
....*....|....*....|....*....|...
gi 21729876 1303 NCDHILVMGNGKVVEFDRPEVLRKKPGsLFAAL 1335
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGG-LYARL 571
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1135-1321 |
1.64e-83 |
|
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: 271.59 E-value: 1.64e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1135 WPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL 1214
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1215 RSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALE-------------------RTFLTKA-IILIDEATASIDMET 1274
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRvsegglnlsqgqrqllclaRALLKRPrVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 1275 DTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 1321
Cdd:cd03369 161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
806-1115 |
1.80e-71 |
|
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: 240.87 E-value: 1.80e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 806 SCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTnssresngtmadlgniaDNPQLSFYQLVY-GLNALLLICVGVCSSGIF 884
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSS-----------------PNSSSGYYLGVYaALLVLASVLLVLLRWLLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 885 TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILL 964
Cdd:cd18580 64 VLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 965 MGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 1044
Cdd:cd18580 144 VLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1045 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18580 224 WLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
883-1337 |
1.34e-69 |
|
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: 248.98 E-value: 1.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 883 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYI 962
Cdd:COG2274 219 LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 963 LLMGAIIMVICFIYYMMFKKAIG--VFKRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLlfl 1040
Cdd:COG2274 298 ALVVLLLIPLYVLLGLLFQPRLRrlSREESEASAK--RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARF--- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1041 sSTRWMALRLEIMTNLVT-LAVALFVAFGisstpySFKVM----------AVNIVL-QLASSFQATARIGLETEAQFTAV 1108
Cdd:COG2274 373 -KLRRLSNLLSTLSGLLQqLATVALLWLG------AYLVIdgqltlgqliAFNILSgRFLAPVAQLIGLLQRFQDAKIAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1109 ERILQYMKMcVSEAPLHMEGTSCPQGwpqHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL 1188
Cdd:COG2274 446 ERLDDILDL-PPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1189 FRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALE--------------- 1252
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARlaglhdfiealpmgy 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1253 ----------------------RTFLTK-AIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILV 1309
Cdd:COG2274 602 dtvvgeggsnlsggqrqrlaiaRALLRNpRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
490 500
....*....|....*....|....*...
gi 21729876 1310 MGNGKVVEFDRPEVLRKKPGsLFAALMA 1337
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKG-LYAELVQ 708
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
152-731 |
3.99e-62 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 223.50 E-value: 3.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 152 LLVMLRFQRTRLIFDALLGICFCIASVLGPILIIPKILEYSEEQ-LGNVVHGVGLCFALFLSECVksLSFSSSWIINqRT 230
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGdLSALLLLLLLLLGLALLRAL--LSYLQRYLLA-RL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 231 AIRFRAAVSSFAFEKLIQF--KSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYT-AFIAI 307
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLplSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRlALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 308 LCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKP----FAKIIEDLRRKERKLLEKCGLVQ 383
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 384 SLTSITLFIipTVATAVWVLIHTSLKLKLTASMAFSMLASLNLL-----RLSVFFVpiavkGLTNSKSAVMRFKKFFLQE 458
Cdd:COG1132 249 PLMELLGNL--GLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLfgplrQLANVLN-----QLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 459 SPVfyvqtlQDPSKALVFEEatlswqqtcpgiVNGALELERNGHAsegmtrprdalGPEEEgnslgPELHKINLVVSKGM 538
Cdd:COG1132 322 PEI------PDPPGAVPLPP------------VRGEIEFENVSFS-----------YPGDR-----PVLKDISLTIPPGE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 539 MLGVCGNTGSGKSSLLSAILEEMHLLEGSV---GV----------QGSLAYVPQQAWIVSGNIRENILMG--GAyDKARY 603
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidGVdirdltleslRRQIGVVPQDTFLFSGTIRENIRYGrpDA-TDEEV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 604 LQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRG 683
Cdd:COG1132 447 EEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKG 525
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 21729876 684 KTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:COG1132 526 RTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
806-1114 |
1.97e-61 |
|
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: 212.95 E-value: 1.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 806 SCIIFFFVVLIVFLT----IFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 881
Cdd:cd18601 1 GVFVFILLVLLNIAAqvlyVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 882 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 961
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 962 ILLmGAIIMVICFI----YYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLL 1037
Cdd:cd18601 161 VLI-PVIPLVILFLflrrYYLKTSREV---KRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1038 LFLSSTRWMALRLEIMTnLVTLAVALFVAFGISSTPYSFKV-MAVNIVLQLASSFQATARIGLETEAQFTAVERILQY 1114
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, ... |
808-1115 |
4.99e-60 |
|
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: 208.10 E-value: 4.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 808 IIFFFVVLIVFLTIFSFWWLSYWLEQgsgtnssresngtmADLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSEWSDD--------------PALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILlmgA 967
Cdd:cd18603 69 CVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFL---V 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 968 IIMVICFIYYMMFKKAIGV---FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 1044
Cdd:cd18603 146 VIIPLAILYFFIQRFYVATsrqLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1045 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
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 ... |
808-1115 |
6.45e-60 |
|
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: 207.71 E-value: 6.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 808 IIFFFVVLIVFLTIFSFWWLSYWLEqgsgtNSSRESNGtmadlgniadnpqlsFYQLVY-GLNALLLICVgVCSSGIFTK 886
Cdd:cd18606 3 LLLLLLILSQFAQVFTNLWLSFWTE-----DFFGLSQG---------------FYIGIYaGLGVLQAIFL-FLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 887 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMg 966
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 967 AIIMVICFIYYMMFKKAIGV-FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRW 1045
Cdd:cd18606 141 LPPLLVLYYFIANYYRASSReLKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRW 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1046 MALRLEIMTNLVTLAVALFVAFGISS-TPYSFKVmAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSiSPSSTGL-VLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1141-1314 |
9.64e-58 |
|
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: 196.84 E-value: 9.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDPVLLSGTIRFNLdpfdrhtdQQIwdALERTFLTKA-IILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVT 1299
Cdd:cd03228 81 VPQDPFLFSGTIRENIlsg--gqrQRI--AIARALLRDPpILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLS 156
|
170
....*....|....*
gi 21729876 1300 TVLNCDHILVMGNGK 1314
Cdd:cd03228 157 TIRDADRIIVLDDGR 171
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
808-1115 |
2.86e-57 |
|
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: 200.39 E-value: 2.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 808 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTmadlgniadnpqLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVS------------VLYYLGIYALISLLSVLLGTLRYLLFFFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGA 967
Cdd:cd18604 71 SLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 968 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMA 1047
Cdd:cd18604 151 VLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLS 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1048 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18604 231 VRIDLLGALFSFATAALLVYGPGIDA-GLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1139-1338 |
1.75e-56 |
|
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: 196.67 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALE-------------------------------------RTFLTKAII 1261
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEiaqlknmvkslpggldavvteggenfsvgqrqlfclaRAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1262 LI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALMAT 1338
Cdd:cd03288 178 LImDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRT 255
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
167-450 |
2.34e-56 |
|
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: 197.32 E-value: 2.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 167 ALLGICFCIASVLGPILIIpKILEY-SEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEK 245
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLG-LLISYlSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 246 L--IQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRM 323
Cdd:cd18579 82 AlrLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 324 AVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVL 403
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 21729876 404 IHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
525-708 |
8.72e-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: 8.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV-----------------GVQGSLAYVPQQAWIVSGN 587
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21729876 668 VGKHIFEECIKKTLRG--KTVVLVTHQLQYLEFCGQIILLENG 708
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
525-730 |
1.27e-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: 189.30 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYL 604
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 605 QVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGK 684
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 685 TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 730
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
117-731 |
2.80e-51 |
|
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: 193.90 E-value: 2.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 117 IPPLSVHDASDKNVQRLHRLWEeevsrrgiekasvllvMLRFQRTRLIFDALLGICFCIASVLGPIL---IIPKILEYSE 193
Cdd:COG2274 128 LEPTPEFDKRGEKPFGLRWFLR----------------LLRRYRRLLLQVLLASLLINLLALATPLFtqvVIDRVLPNQD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 194 EQLGNVVhGVGLcFALFLSECVksLSFSSSWIINqRTAIRFRAAVSSFAFEKLI-----QFKSVihiTSGEAIS------ 262
Cdd:COG2274 192 LSTLWVL-AIGL-LLALLFEGL--LRLLRSYLLL-RLGQRIDLRLSSRFFRHLLrlplsFFESR---SVGDLASrfrdve 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 263 ----FFTGDvnyLFEGVCYGPLVLITCAslVICSISSYFIIgyTAFIAILCYLLVFplaVFMTRMAVKAQHHTSEVSDQR 338
Cdd:COG2274 264 sireFLTGS---LLTALLDLLFVLIFLI--VLFFYSPPLAL--VVLLLIPLYVLLG---LLFQPRLRRLSREESEASAKR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 339 IRVTSEVLTCIKLIKMY--------TWEKPFAKIIeDLRRKERKLLekcgLVQSLTSITLFIIPTVATaVWVLIHTSLKL 410
Cdd:COG2274 334 QSLLVETLRGIETIKALgaesrfrrRWENLLAKYL-NARFKLRRLS----NLLSTLSGLLQQLATVAL-LWLGAYLVIDG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 411 KLTASM--AFSMLASLnllrlsvFFVPIA--VKGLTN---SKSAVMRFKKFFLQESpvfyvqtlqdpskalvfeEATLSW 483
Cdd:COG2274 408 QLTLGQliAFNILSGR-------FLAPVAqlIGLLQRfqdAKIALERLDDILDLPP------------------EREEGR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 484 QQTCPGIVNGALELER-----NGHASegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL 558
Cdd:COG2274 463 SKLSLPRLKGDIELENvsfryPGDSP--------------------PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 559 EEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRENILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDM 624
Cdd:COG2274 523 GLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYD 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 625 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 704
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL-ENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
650 660
....*....|....*....|....*..
gi 21729876 705 LENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
807-1115 |
6.84e-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: 176.64 E-value: 6.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 807 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADlgniaDNPQLSFYQLVYGLNALLLICVGVCSSGIFTK 886
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSL-----EDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 887 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 966
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 967 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqNNYLLLFLSST-RW 1045
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDR-NNTAFLFLNTAnRW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1046 MALRLEIMTNLVTLA---VALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18602 236 LGIRLDYLGAVIVFLaalSSLTAALAGYISP-SLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
524-724 |
1.36e-48 |
|
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: 183.04 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:COG4988 430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 670 KHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKG 724
Cdd:COG4988 510 AEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1139-1329 |
2.59e-47 |
|
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: 169.33 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1139 GEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWD--------------------------------------ALERTFLTKAI 1260
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeaakeagahdfimklpngydtvlgenggnlsqgerqllAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1261 ILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1329
Cdd:cd03254 160 ILIlDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1141-1335 |
4.33e-47 |
|
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: 168.95 E-value: 4.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDPVLLSGTIRFNLdpfdRH-----TDQQIWDALE-------------------------------------RTFLTK 1258
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKaaqihdkimrfpdgydtivgerglklsggekqrvaiaRAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1259 AIILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAAL 1335
Cdd:cd03253 156 PPILLlDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEM 232
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
808-1115 |
1.47e-46 |
|
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: 169.63 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 808 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18605 3 LILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFIND-------------SFNFFLTVYGFLAGLNSLFTLLRAFLFAYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLmga 967
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 968 IIMVICFIYYMM---FKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQF-KRLTDAQNNYLLLfLSST 1043
Cdd:cd18605 147 LLLPLAFIYYRIqryYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYlEKLENNQRAQLAS-QAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 1044 RWMALRLEIMTNLVTLAVALFVAFGIS---STPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
871-1317 |
5.73e-44 |
|
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: 169.51 E-value: 5.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 871 LLLICVGVC---SSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLpifSEQFLVL--- 944
Cdd:TIGR02203 62 GLAVLRGICsfvSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA---TDAFIVLvre 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 945 SLMVIA---VLLIVS-VLSPYILLMGAIIMVICFIYYmmfkkaigvfKRLENYSRsplfsHILNS-----------LQGL 1009
Cdd:TIGR02203 139 TLTVIGlfiVLLYYSwQLTLIVVVMLPVLSILMRRVS----------KRLRRISK-----EIQNSmgqvttvaeetLQGY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1010 SSIHVYGKTEdfiSQFKRLtDAQNNYLLLFlsstrwmALRLEIMTNL--------------VTLAVALFVAFGISSTPYS 1075
Cdd:TIGR02203 204 RVVKLFGGQA---YETRRF-DAVSNRNRRL-------AMKMTSAGSIsspitqliaslalaVVLFIALFQAQAGSLTAGD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1076 FKVMAVNIvLQLASSFQATARIGLETEAQFTAVERILQYmkmcVSEAPLHMEGTSCPQgwPQHGEIIFQDYHMKYRDNTP 1155
Cdd:TIGR02203 273 FTAFITAM-IALIRPLKSLTNVNAPMQRGLAAAESLFTL----LDSPPEKDTGTRAIE--RARGDVEFRNVTFRYPGRDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 1235
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1236 L--------------------------DPFDRHTDQQIWD-------------ALERTFLTKAIILI-DEATASIDMETD 1275
Cdd:TIGR02203 426 IaygrteqadraeieralaaayaqdfvDKLPLGLDTPIGEngvllsggqrqrlAIARALLKDAPILIlDEATSALDNESE 505
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21729876 1276 TLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1317
Cdd:TIGR02203 506 RLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
280-731 |
7.55e-44 |
|
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: 169.18 E-value: 7.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 280 LVLITCASLVICSISsyFIIGYTAFIAILCYLLVFPLaVFMTRMAVKAQHHTSEVSDQRIRVTsEVLTCIKLIKMY---- 355
Cdd:COG4987 140 LLVILAAVAFLAFFS--PALALVLALGLLLAGLLLPL-LAARLGRRAGRRLAAARAALRARLT-DLLQGAAELAAYgald 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 356 TWEKPFAKIIEDLRRKERKL--LEkcGLVQSLTSITLFIipTVATAVWVLIHtslkLKLTASMAFSMLASLNLLRLSVF- 432
Cdd:COG4987 216 RALARLDAAEARLAAAQRRLarLS--ALAQALLQLAAGL--AVVAVLWLAAP----LVAAGALSGPLLALLVLAALALFe 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 433 -FVPI--AVKGLTNSKSAVMRfkkfflqespvfyVQTLQDPSKALVFEEATLSWQQTcpgivnGALELERNGHASEGMTR 509
Cdd:COG4987 288 aLAPLpaAAQHLGRVRAAARR-------------LNELLDAPPAVTEPAEPAPAPGG------PSLELEDVSFRYPGAGR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 510 PRdalgpeeegnslgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAY 576
Cdd:COG4987 349 PV---------------LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 577 VPQQAWIVSGNIRENILMG--GAYDkARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQI 654
Cdd:COG4987 414 VPQRPHLFDTTLRENLRLArpDATD-EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPI 492
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 655 YLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:COG4987 493 LLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1141-1317 |
2.81e-42 |
|
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: 155.08 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALE-------------------------------------RTFLTKAII 1261
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARaanahefimelpegydtvigergvklsggqrqriaiaRALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1262 LI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1317
Cdd:cd03251 160 LIlDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1138-1317 |
3.10e-41 |
|
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: 161.91 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1138 HGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK 1217
Cdd:COG5265 355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1218 LSVIPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALE-------------------------------------RTFLTK 1258
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNI-AYGRPdaSEEEVEAAARaaqihdfieslpdgydtrvgerglklsggekqrvaiaRTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1259 AIILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1317
Cdd:COG5265 513 PPILIfDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
165-450 |
1.54e-40 |
|
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: 152.26 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 165 FDALLGICFCIASVLGPILIiPKILEYSEEQ-LGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAF 243
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFL-NRLLRYLEDPgEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 244 EKLIQFKSVIHITS---------------------GEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYT 302
Cdd:cd18596 80 EKALRRRDKSGSSKsseskkkdkeededekssasvGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 303 AFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLV 382
Cdd:cd18596 160 ALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 383 QSLTSITLFIIPTVATAVWVLIHTSL-KLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDR 308
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
168-450 |
2.84e-40 |
|
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: 151.07 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 168 LLGICFCIASVLGPiLIIPKILEYSEE-----QLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFA 242
Cdd:cd18597 4 LLKLLADVLQVLSP-LLLKYLINFVEDaylggPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 243 FEKLIQF--KSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFM 320
Cdd:cd18597 83 YRKSLRLsgKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 321 TRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAV 400
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 21729876 401 WVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKR 292
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1141-1336 |
1.84e-39 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 146.92 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSGTIRFN--LDPFDRHTD--------------------------------------QQIwdALERTFLTK 1258
Cdd:cd03249 80 GLVSQEPVLFDGTIAENirYGKPDATDEeveeaakkanihdfimslpdgydtlvgergsqlsggqkQRI--AIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1259 -AIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALM 1336
Cdd:cd03249 158 pKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG-VYAKLV 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
525-724 |
2.69e-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: 146.22 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:cd03254 97 IRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21729876 671 HIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKG 724
Cdd:cd03254 177 LI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
525-729 |
5.35e-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: 145.45 E-value: 5.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMG--GAyDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 669
Cdd:cd03251 96 IAYGrpGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ES 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 670 KHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:cd03251 174 ERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1141-1337 |
1.74e-38 |
|
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: 144.17 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDPVLLSGTIRFNL---DP-FDRH------------------------------------TDQQIwdALERTFLTKAI 1260
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDPgMSMErvieaaklagahdfiselpegydtivgeqgaglsggQRQRI--AIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1261 ILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAALMA 1337
Cdd:cd03252 159 ILIfDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQ 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
525-732 |
1.99e-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: 140.83 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMG--GAYDKARYLQVLHCCsLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03253 95 IRYGrpDATDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 670 KHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:cd03253 174 REIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1139-1319 |
1.59e-36 |
|
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: 139.60 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEpMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDA-------------------------------------LERTFLTKA-I 1260
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVaeevglksvieqfpgqldfvlvdggcvlshghkqlmcLARSVLSKAkI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1261 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFD 1319
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
521-714 |
2.09e-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: 137.34 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 521 NSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGN 587
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:cd03245 94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 667 HVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENG 714
Cdd:cd03245 174 NSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
531-732 |
3.55e-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: 3.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 531 NLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENILMGGa 597
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIRYGK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 598 yDKARYLQVLHCCSL-NRD--LELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfE 674
Cdd:cd03249 102 -PDATDEEVEEAAKKaNIHdfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV-Q 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 675 ECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:cd03249 180 EALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
520-709 |
6.82e-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: 6.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 520 GNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG 586
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 587 NIRENILmggaydkarylqvlhccslnrdlellpfgdmteigerglnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:cd03228 91 TIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21729876 667 HVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGK 709
Cdd:cd03228 130 ETEALIL-EALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
327-740 |
1.29e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.08 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 327 AQHHTSEVSDQrirvTSEVLTCIKLIKMYTWEK----PFAKIIEDLRRKERKLLEkcglVQSLTSITLFIIPTVAT--AV 400
Cdd:PRK10789 168 AQAAFSSLNDR----TQESLTSIRMIKAFGLEDrqsaLFAADAEDTGKKNMRVAR----IDARFDPTIYIAIGMANllAI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 401 ----WVLIHTSLKL-KLTASMAFSMLASLNLLRLSVFFvPIAVKGltnskSAVMRFKKFFLQESPVfyvqtLQDPSKALV 475
Cdd:PRK10789 240 gggsWMVVNGSLTLgQLTSFVMYLGLMIWPMLALAWMF-NIVERG-----SAAYSRIRAMLAEAPV-----VKDGSEPVP 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 476 FEEATLSWqqtcpgivngalelernghASEGMTRPRdalgpeeegnSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLS 555
Cdd:PRK10789 309 EGRGELDV-------------------NIRQFTYPQ----------TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 556 AILEEMHLLEGSVGVQ-------------GSLAYVPQQAWIVSGNIRENILMGG-AYDKARYLQVLHCCSLNRDLELLPF 621
Cdd:PRK10789 360 LIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 622 GDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQ 701
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASE 518
|
410 420 430
....*....|....*....|....*....|....*....
gi 21729876 702 IILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSD 740
Cdd:PRK10789 519 ILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALD 557
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
523-715 |
1.64e-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: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 523 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahvg 669
Cdd:cd03244 96 SNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD---- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21729876 670 kHIFEECIKKTLR----GKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:cd03244 172 -PETDALIQKTIReafkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
524-732 |
1.74e-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: 132.61 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 524 GPE-LHKINLVVSKGMMLGVCGNTGSGKSSLlSAILEEMHLLE-GSVGVQG-------------SLAYVPQQAWIVSGNI 588
Cdd:cd03252 14 GPViLDNISLRIKPGEVVGIVGRSGSGKSTL-TKLIQRFYVPEnGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaH 667
Cdd:cd03252 93 RDNIALADpGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-Y 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 668 VGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:cd03252 172 ESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
900-1335 |
4.42e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 139.71 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 900 FNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQL----LPIFSEQFLvlSLMVIAVLLIVSVlspYI-LLMGAIIMVICF 974
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTL---LRGTDALfglwLEFMREHLA--TLVALVVLLPLAL---FMnWRLSLVLVVLGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 975 IYYMM----FKKAIGVFKRLENYsRSPLFSHILNSLQGLSSIHVYGKTEDFISQFK----RLTDAQNNYL--------LL 1038
Cdd:PRK13657 168 VYTLIttlvMRKTKDGQAAVEEH-YHDLFAHVSDAIGNVSVVQSYNRIEAETQALRdiadNLLAAQMPVLswwalasvLN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1039 FLSSTRWMALRLEIMTNLVT---LAVALFVAFgisstpYSFKVMAVNIVLQLAS----SFQATARIgleteAQFTAVERI 1111
Cdd:PRK13657 247 RAASTITMLAILVLGAALVQkgqLRVGEVVAF------VGFATLLIGRLDQVVAfinqVFMAAPKL-----EEFFEVEDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1112 LQYmkmcVSEAPlhmeGTSCPQGWpqHGEIIFQDYHMKYrDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 1191
Cdd:PRK13657 316 VPD----VRDPP----GAIDLGRV--KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1192 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL-----DPfdrhTDQQIWDALE-------------- 1252
Cdd:PRK13657 385 FDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAEraqahdfierkpdg 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1253 -----------------------RTFLTKAIILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHIL 1308
Cdd:PRK13657 461 ydtvvgergrqlsggerqrlaiaRALLKDPPILIlDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
|
490 500 510
....*....|....*....|....*....|
gi 21729876 1309 VMGNGKVVE---FDrpEVLRKkpGSLFAAL 1335
Cdd:PRK13657 541 VFDNGRVVEsgsFD--ELVAR--GGRFAAL 566
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
524-705 |
9.32e-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: 137.80 E-value: 9.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:TIGR02857 415 NIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 21729876 670 KHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILL 705
Cdd:TIGR02857 495 AEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
888-1310 |
1.37e-33 |
|
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: 137.42 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 967
Cdd:TIGR02857 72 AAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA---LEGVEALDGYFARYLPQLVLAVIVPLAILAAVFP-QDWISG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 968 IIMVICFIYYMMFKKAIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEdfiSQFKRLTDAQNNYL----- 1036
Cdd:TIGR02857 148 LILLLTAPLIPIFMILIGWAaqaaarKQWAALSR--LSGHFLDRLRGLPTLKLFGRAK---AQAAAIRRSSEEYRertmr 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1037 ---LLFLSStrwmaLRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVL---------QLASSFQATAriglETEAQ 1104
Cdd:TIGR02857 223 vlrIAFLSS-----AVLELFATLSVALVAVYIGFRLLAGDLDLATGLFVLLLapefylplrQLGAQYHARA----DGVAA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1105 FTAVERILQymkmcVSEAPLHMEGtscPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSL 1184
Cdd:TIGR02857 294 AEALFAVLD-----AAPRPLAGKA---PVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1185 GMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN---------------------LDPFDR-- 1241
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENirlarpdasdaeirealeragLDEFVAal 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1242 --HTDQQIWD-------------ALERTFL-TKAIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCD 1305
Cdd:TIGR02857 445 pqGLDTPIGEggaglsggqaqrlALARAFLrDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
....*
gi 21729876 1306 HILVM 1310
Cdd:TIGR02857 525 RIVVL 529
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
207-451 |
2.49e-33 |
|
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: 130.83 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 207 FALFLSECVKSLSFSSSWII--NQRTAIRFRAAVSSFAFEKLIQFKSVI--HITSGEAISFFTGDVNYLFEGVCYGPLVL 282
Cdd:cd18594 41 YALGLSLCAFLRVLLHHPYFfgLHRYGMQLRIALSSLIYKKTLKLSSSAlsKITTGHIVNLLSNDVQKFDEVLVYLHFLW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 283 ITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFA 362
Cdd:cd18594 121 IAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 363 KIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSV-FFVPIAVKGL 441
Cdd:cd18594 201 KLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLLNALRMTItRFFPESIQTL 280
|
250
....*....|
gi 21729876 442 TNSKSAVMRF 451
Cdd:cd18594 281 SESRVSLKRI 290
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1149-1315 |
1.03e-32 |
|
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: 125.02 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1149 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLL 1228
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1229 SGTIRFNLdpFDRHTDQQIwdALERTFLTK-AIILIDEATASIDMETDTLIQRTIREA-FQGCTVLVIAHRVTTVLNCDH 1306
Cdd:cd03246 89 SGSIAENI--LSGGQRQRL--GLARALYGNpRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADR 164
|
....*....
gi 21729876 1307 ILVMGNGKV 1315
Cdd:cd03246 165 ILVLEDGRV 173
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
233-729 |
2.87e-32 |
|
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: 134.06 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 233 RFRAAVSSFAFEKLIQFKSVIHIT--SGEAISFFTGDVNYLFEGVcyGPLVLITCASLVICsISSYFIIGYTAFIAILCY 310
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFDKnrSGEVVSRLTTDTTLLQSVI--GSSLSMALRNALMC-IGGLIMMFITSPKLTSLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 311 LLVFPLAVF--------MTRMAVKAQHHTSEVSDqrirVTSEVLTCIKLIKMYTWE----KPFAKIIEDLRRKERKLLEK 378
Cdd:TIGR02204 165 LLAVPLVLLpillfgrrVRKLSRESQDRIADAGS----YAGETLGAIRTVQAFGHEdaerSRFGGAVEKAYEAARQRIRT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 379 CGLvqsLTSITLFII-PTVATAVWVLIHTSLKLKLTASmafsmlaslnllRLSVF-FVPIAVKGLTNSKSAVmrfkkffl 456
Cdd:TIGR02204 241 RAL---LTAIVIVLVfGAIVGVLWVGAHDVIAGKMSAG------------TLGQFvFYAVMVAGSIGTLSEV-------- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 457 qespvfyVQTLQDPSKA------LVFEEATLS---WQQTCPGIVNGALELERNGHASEGmtRPRDalgpeeegnslgPEL 527
Cdd:TIGR02204 298 -------WGELQRAAGAaerlieLLQAEPDIKapaHPKTLPVPLRGEIEFEQVNFAYPA--RPDQ------------PAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 528 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRENILM 594
Cdd:TIGR02204 357 DGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVMENIRY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 GGAydKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKH 671
Cdd:TIGR02204 437 GRP--DATDEEVEAAARAAHAHEFisaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE-SEQ 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 672 IFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:TIGR02204 514 LVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1139-1316 |
2.96e-32 |
|
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: 125.39 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSGTIRFNL---DPFdrHTDQQIWDALERTFLTK------------------------------------- 1258
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDfvnkhpngldlqigergrglsggqrqavalarallnd 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1259 -AIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRvTTVLN-CDHILVMGNGKVV 1316
Cdd:cd03245 159 pPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR-PSLLDlVDRIIVMDSGRIV 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
523-731 |
3.37e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 133.82 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 523 LGPelhkINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLlEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:PRK11174 366 AGP----LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK11174 441 DNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 669 GKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:PRK11174 521 EQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
527-711 |
5.64e-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: 124.57 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQA---WIVSGNIRENILMG 595
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRsidRDFPISVRDVVLMG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 gaydkaRYLQVLHCCSLNRD-----LELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03235 95 ------LYGHKGLFRRLSKAdkakvDEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21729876 670 KHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKIC 711
Cdd:cd03235 169 EDIYE--LLRELRreGMTILVVTHDLgLVLEYFDRVLLLNRTVVA 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
917-1317 |
7.20e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 132.64 E-value: 7.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 917 GRLLNCFAGDLEQLDQL-LPIFSEqfLVLSLMVIAVLLI-VSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRLENY 993
Cdd:PRK11160 117 GDLLNRLVADVDTLDHLyLRLISP--LVAALVVILVLTIgLSFFDLTLaLTLGGILLLLLLLLPLLFYRLGKKPGQDLTH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 994 SRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQnnylllflssTRWMAlRLEIMTNLVTLAVALFVAFGisstp 1073
Cdd:PRK11160 195 LRAQYRVQLTEWLQGQAELTLFGAEDRYR---QQLEQTE----------QQWLA-AQRRQANLTGLSQALMILAN----- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1074 ysfkVMAVNIVLQLASS-----FQATARIGLETEAQFTAVERIL------QYMKMCVS-----------EAPLHMEGTSC 1131
Cdd:PRK11160 256 ----GLTVVLMLWLAAGgvggnAQPGALIALFVFAALAAFEALMpvagafQHLGQVIAsarrineiteqKPEVTFPTTST 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1132 PQgwPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 1211
Cdd:PRK11160 332 AA--ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1212 EDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTK------------------------------ 1258
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKlleddkglnawlgeggrqlsggeqrrlgia 487
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 1259 -------AIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1317
Cdd:PRK11160 488 rallhdaPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
167-438 |
1.22e-31 |
|
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: 126.05 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 167 ALLGICFCIASVLGPIlIIPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEKL 246
Cdd:cd18595 3 ALLKLLSDILLFASPQ-LLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 247 IQFKSVI--HITSGEAISFFTGDVNYLFEGVCY------GPLVLItcaslvICSISSYFIIGYTAFIAILCYLLVFPLAV 318
Cdd:cd18595 82 LRLSNSArkKSTVGEIVNLMSVDAQRIQDLVPYlnmlwsAPLQII------LALYFLWQTLGPSVLAGLGVMILLIPLNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 319 FMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIP---T 395
Cdd:cd18595 156 VLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPflvS 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 21729876 396 VAT-AVWVLIhtSLKLKLTASMAFSMLASLNLLRLSVFFVPIAV 438
Cdd:cd18595 236 LATfATYVLS--DPDNVLDAEKAFVSLSLFNILRFPLSMLPMVI 277
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1141-1317 |
5.19e-31 |
|
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: 120.50 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSV 1220
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDPVLLSGTIRFNL-DPFDRHTDQQIwdALERTFLTKA-IILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRV 1298
Cdd:cd03247 80 LNQRPYLFDTTLRNNLgRRFSGGERQRL--ALARILLQDApIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHL 157
|
170
....*....|....*....
gi 21729876 1299 TTVLNCDHILVMGNGKVVE 1317
Cdd:cd03247 158 TGIEHMDKILFLENGKIIM 176
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
525-731 |
8.82e-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: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLlSAILEEMHLLE-GSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTL-TKLLQRLYTPQhGQVLVDGvdlaiadpawlrrQMGVVLQENVLFSRSIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGGAydKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:TIGR01846 550 NIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 668 vGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:TIGR01846 628 -SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQ 690
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
789-1115 |
9.18e-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: 124.53 E-value: 9.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 789 SWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMAdlgnIADNPQLSFYQL-VYG 867
Cdd:cd18600 2 TWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYA----VIVTFTSSYYVFyIYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 868 LNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 947
Cdd:cd18600 78 GVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 948 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 1027
Cdd:cd18600 158 VIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1028 LTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAlFVAFGISstpySFKVMAVNIVLQLA----SSFQATARIGLETEA 1103
Cdd:cd18600 238 ALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVT-FISIGTT----GDGEGRVGIILTLAmnimSTLQWAVNTSIDVDS 312
|
330
....*....|..
gi 21729876 1104 QFTAVERILQYM 1115
Cdd:cd18600 313 LMRSVSRIFKFI 324
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
901-1317 |
2.14e-30 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 128.30 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 901 NKVFRCPMSFFDTIPIGRLLNCFAGDLEQL-DQLLPIFSEQFLVLSL---MVIAVLLI---VSVLSPYILLMGAIIMVIc 973
Cdd:PRK10790 106 DAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLYVTVVATVLRSAALigaMLVAMFSLdwrMALVAIMIFPAVLVVMVI- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 974 fiyYMMFKKAIgvFKRLenysRSPL------FSHILNslqGLSSIHVYGKTEDFisqFKRLTDAQNNYLLlflssTRWMA 1047
Cdd:PRK10790 185 ---YQRYSTPI--VRRV----RAYLadindgFNEVIN---GMSVIQQFRQQARF---GERMGEASRSHYM-----ARMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1048 LRLE--IMTNLVTLAVA-----LFVAFGISSTP-------YSFkvmaVNIVLQLASSF-QATARIGLETEAqFTAVERIL 1112
Cdd:PRK10790 245 LRLDgfLLRPLLSLFSAlilcgLLMLFGFSASGtievgvlYAF----ISYLGRLNEPLiELTTQQSMLQQA-VVAGERVF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1113 QYMkmcvsEAPLHMEGTScpqGWP-QHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 1191
Cdd:PRK10790 320 ELM-----DGPRQQYGND---DRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1192 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLdPFDRH-TDQQIWDALERTFL-------------- 1256
Cdd:PRK10790 391 YPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRDiSEEQVWQALETVQLaelarslpdglytp 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1257 ------------------------TKAIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGN 1312
Cdd:PRK10790 470 lgeqgnnlsvgqkqllalarvlvqTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549
|
....*
gi 21729876 1313 GKVVE 1317
Cdd:PRK10790 550 GQAVE 554
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
807-1087 |
3.11e-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: 121.60 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 807 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTK 886
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ--------------ALNVYSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 887 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 966
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 967 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWM 1046
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 21729876 1047 ALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQL 1087
Cdd:pfam00664 228 FGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
525-730 |
6.49e-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: 127.93 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMGgAYDKARYLQVLHCCSL---NRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:TIGR01193 568 LLLG-AKENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 669 GKHIFEECIKktLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 730
Cdd:TIGR01193 647 EKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
527-721 |
1.49e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQAWIVSG---NIRENILMG 595
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAEVDWDfpiTVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 --------GAYDKARYLQVLHCcslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDLADRPIGeLSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 667 HvGKHIFEECIKKtLR--GKTVVLVTHQLQYL-EFCGQIILLENGKICEnGTHSELMQ 721
Cdd:COG1121 173 A-TEEALYELLRE-LRreGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
525-732 |
5.16e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 124.17 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMG--GAYDkARYLQVLHCCSLNRDLELLPfGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:PRK11160 434 LLLAapNASD-EALIEVLQQVGLEKLLEDDK-GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 670 KHIFEeCIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:PRK11160 512 RQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQR 573
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
885-1337 |
5.65e-29 |
|
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: 125.06 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 885 TKVTRKASTALHNKLFNKVFRCPMSFFDTipigRllncFAGDLE---QL-DQLLPIFSEQFL--VLSLMVIAVLLIVSVL 958
Cdd:TIGR03796 219 RRLEIKLAVGMSARFLWHILRLPVRFFAQ----R----HAGDIAsrvQLnDQVAEFLSGQLAttALDAVMLVFYALLMLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 959 spYILLMGAIIMVICFIYYMMFKKaigVFKRLENYSRS------PLFSHILNSLQGLSSIHVYGKTEDFisqFKRLTDAQ 1032
Cdd:TIGR03796 291 --YDPVLTLIGIAFAAINVLALQL---VSRRRVDANRRlqqdagKLTGVAISGLQSIETLKASGLESDF---FSRWAGYQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1033 NNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGisstpySFKVMAVNIVL-------QLASSFQA--TARIGL---- 1099
Cdd:TIGR03796 363 AKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVG------GLRVMEGQLTIgmlvafqSLMSSFLEpvNNLVGFggtl 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1100 -ETEAQFTAVERILQYMKMCVSEAPLHMEGTSCPQgWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTG 1178
Cdd:TIGR03796 437 qELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPP-RRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSG 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1179 SGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHT----------DQQIW 1248
Cdd:TIGR03796 516 SGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIpdadlvrackDAAIH 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1249 DA--------------------------LE--RTFLTKAIILI-DEATASIDMETDTLIQRTIREafQGCTVLVIAHRVT 1299
Cdd:TIGR03796 596 DVitsrpggydaelaegganlsggqrqrLEiaRALVRNPSILIlDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLS 673
|
490 500 510
....*....|....*....|....*....|....*...
gi 21729876 1300 TVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMA 1337
Cdd:TIGR03796 674 TIRDCDEIIVLERGKVVQRGTHEELWAVGG-AYARLIR 710
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1150-1314 |
9.66e-29 |
|
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: 113.11 E-value: 9.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1150 YRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQdpvlLS 1229
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----LS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1230 GTIRfnldpfdrhtdQQIwdALERTFLTKA-IILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDH 1306
Cdd:cd00267 83 GGQR-----------QRV--ALARALLLNPdLLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADR 149
|
....*...
gi 21729876 1307 ILVMGNGK 1314
Cdd:cd00267 150 VIVLKDGK 157
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
879-1329 |
1.03e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 124.06 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 879 CSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVL 958
Cdd:TIGR00958 220 LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 959 SPYILLMGAIIMVICFIYYMMFKKAI-GVFKRLENySRSPLFSHILNSLQGLSSIHVYG-------KTEDFISQFKRLTD 1030
Cdd:TIGR00958 300 SPRLTMVTLINLPLVFLAEKVFGKRYqLLSEELQE-AVAKANQVAEEALSGMRTVRSFAaeegeasRFKEALEETLQLNK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1031 AQNNYLLLFLSSTRWMALRLE----------IMTNLVTlaVALFVAFGIsstpYSFKV-MAVNIVLQLASSFQATArigl 1099
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQvlvlyyggqlVLTGKVS--SGNLVSFLL----YQEQLgEAVRVLSYVYSGMMQAV---- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1100 eteaqfTAVERILQYM--KMCVSE----APLHMEGTscpqgwpqhgeIIFQDYHMKY--RDNTPtVLHGINLTIRGHEVV 1171
Cdd:TIGR00958 449 ------GASEKVFEYLdrKPNIPLtgtlAPLNLEGL-----------IEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1172 GIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL--------------- 1236
Cdd:TIGR00958 511 ALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIaygltdtpdeeimaa 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1237 ------------DPFDRHTD-----------QQIWDALERTFLTKAIILI-DEATASIDMETDTLIQRTirEAFQGCTVL 1292
Cdd:TIGR00958 591 akaanahdfimeFPNGYDTEvgekgsqlsggQKQRIAIARALVRKPRVLIlDEATSALDAECEQLLQES--RSRASRTVL 668
|
490 500 510
....*....|....*....|....*....|....*..
gi 21729876 1293 VIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1329
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
174-450 |
5.42e-28 |
|
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: 115.40 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 174 CIASVLGPILIIpKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSW--IINQRTAIRFRAAVSSFAFEKLIQF-- 249
Cdd:cd18593 10 EAIRVVQPIFLG-KLIRYFEGNGSSISLTEAYLYAGGVSLCSFLFIITHHPyfFGMQRIGMRLRVACSSLIYRKALRLsq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 250 KSVIHITSGEAISFFTGDVNYLFEGV---CY---GPLVLItcASLVICsissYFIIGYTAFIAILCYLLVFPLAVFMTRM 323
Cdd:cd18593 89 AALGKTTVGQIVNLLSNDVNRFDQAVlflHYlwvAPLQLI--AVIYIL----WFEIGWSCLAGLAVLLILIPLQSFFGKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 324 AVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVL 403
Cdd:cd18593 163 FSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 21729876 404 IHTSLKLKLTASMAFSMLASLNLLRLSV-FFVPIAVKGLTNSKSAVMR 450
Cdd:cd18593 243 AYILLGNILTAERVFVTMALYNAVRLTMtLFFPFAIQFGSELSVSIRR 290
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
175-450 |
2.40e-27 |
|
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: 113.87 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 175 IASVLGPiLIIPKILEY--------SEEQLGNVVHGVG----------LCFALFLSECVKSLSFSSSWIINQRTAIRFRA 236
Cdd:cd18591 11 LLGFVGP-LCISGIVDYveentyssSNSTDKLSVSYVTveeffsngyvLAVILFLALLLQATFSQASYHIVIREGIRLKT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 237 AVSSFAFEKLIQFKSV----IHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLL 312
Cdd:cd18591 90 ALQAMIYEKALRLSSWnlssGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 313 VFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:cd18591 170 MTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 393 IPTVATAVWVLIHTSLKLK-LTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18591 250 SPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1136-1315 |
4.98e-27 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 110.64 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1136 PQH--GEIIFQDYHMKYRDNTPT-VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 1212
Cdd:cd03248 5 PDHlkGIVKFQNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1213 DLRSKLSVIPQDPVLLSGTIRFNLD------PFDR--------HTDQQIWD------------------------ALERT 1254
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAyglqscSFECvkeaaqkaHAHSFISElasgydtevgekgsqlsggqkqrvAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1255 FLTKAIILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1315
Cdd:cd03248 165 LIRNPQVLIlDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
527-710 |
1.05e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.14 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALadLDPPT--SGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 I-----LMGGAYDKARYLQVLHccSLNRDLELLpfgDmTEIGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:COG4619 94 LpfpfqLRERKFDRERALELLE--RLGLPPDIL---D-KPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 667 HvGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:COG4619 164 E-NTRRVEELLREYLAeeGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
525-730 |
3.68e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.97 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:TIGR00958 575 IAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 671 HIFEEcikKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 730
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 ... |
203-722 |
5.90e-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: 114.37 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 203 VGLCFALFLSECVKS--LSFSSSWIINQRTAIRFRAAV----------SSFAFEKLIQFKSVIhiTSGEAISFFtgDVNY 270
Cdd:TIGR01842 53 LGLYLFLGLLDALRSfvLVRIGEKLDGALNQPIFAASFsatlrrgsgdGLQALRDLDQLRQFL--TGPGLFAFF--DAPW 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 271 LfegvcygPLVLITCaslvicsissYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRV------TSE 344
Cdd:TIGR01842 129 M-------PIYLLVC----------FLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLadsalrNAE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 345 VLTCIKLIKMYT--WEKPFAKIIEdlrrKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIhtSLKLKLTASMafsMLA 422
Cdd:TIGR01842 192 VIEAMGMMGNLTkrWGRFHSKYLS----AQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYL--AIDGEITPGM---MIA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 423 SLNLL--RLSVFFVPIAV-KGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPskalvfeeatlswqqtcpgivNGALELER 499
Cdd:TIGR01842 263 GSILVgrALAPIDGAIGGwKQFSGARQAYKRLNELLANYPSRDPAMPLPEP---------------------EGHLSVEN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 500 nghasegmtrpRDALGPEEEGnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------- 572
Cdd:TIGR01842 322 -----------VTIVPPGGKK----PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwd 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 573 ------SLAYVPQQAWIVSGNIRENILMGGayDKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRIS 643
Cdd:TIGR01842 387 retfgkHIGYLPQDVELFPGTVAENIARFG--ENADPEKIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 644 LARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKT-LRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDE-EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
527-720 |
8.95e-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: 105.13 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAwIVSGNI--REN 591
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEP-PAPFGLtvREL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMG--------GAYDKARYLQVLHCcslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:COG1120 96 VALGryphlglfGRPSAEDREAVEEA------LERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 663 AVDAHvgkHIFE--ECIKK--TLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 720
Cdd:COG1120 167 HLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1161-1343 |
8.95e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.09 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFD 1240
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1241 RH-TDQQIWDALERTF--------------------------------LTKAII------LIDEATASIDMETDTLIQRT 1281
Cdd:PRK11174 448 PDaSDEQLQQALENAWvseflpllpqgldtpigdqaaglsvgqaqrlaLARALLqpcqllLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1282 IREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMATATSSL 1343
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG-LFATLLAHRQEEI 588
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
525-729 |
9.55e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 9.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------SLAYVPQQAWIVSGN-------IREN 591
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdyTLASLRNQVALVSQNvhlfndtIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 IlmggAY---DKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK11176 437 I----AYartEQYSREQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 666 AHVgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:PRK11176 513 TES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
527-729 |
9.95e-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: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLL-------EGSVGV---------QGSL----AYVPQQawIVSG 586
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLA-------RLLfrfydvtSGRILIdgqdirdvtQASLraaiGIVPQD--TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 587 N--IRENILMG--GAyDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:COG5265 445 NdtIAYNIAYGrpDA-SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 663 AVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:COG5265 524 ALDSRTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
230-693 |
3.46e-24 |
|
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: 108.60 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 230 TAIRFRAAVSSFAFEKL--IQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAI 307
Cdd:TIGR02868 80 AALRSLGALRVRVYERLarQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 308 LCYLLVFPLAV-FMTRMAVKAQHHT-----SEVSDQrirvTSEVLTCIKLIKMYTWEKPFAKIIED----LRRKERKLLE 377
Cdd:TIGR02868 160 AAGLLLAGFVApLVSLRAARAAEQAlarlrGELAAQ----LTDALDGAAELVASGALPAALAQVEEadreLTRAERRAAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 378 KCGLVQSLTSitLFIIPTVATAVWVLIHTSLklklTASMAFSMLASLNLLRLSVF----FVPIAVKGLTNSKSAVMRFKK 453
Cdd:TIGR02868 236 ATALGAALTL--LAAGLAVLGALWAGGPAVA----DGRLAPVTLAVLVLLPLAAFeafaALPAAAQQLTRVRAAAERIVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 454 FFLQESPVFYVQTLQDpsKALVFEEATLswqqtcpgivngalELErngHASEGmtRPRDAlgpeeegnslgPELHKINLV 533
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAA--GAVGLGKPTL--------------ELR---DLSAG--YPGAP-----------PVLDGVSLD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 534 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENILMG-GAYD 599
Cdd:TIGR02868 358 LPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLArPDAT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 600 KARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKK 679
Cdd:TIGR02868 438 DEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLA 516
|
490
....*....|....
gi 21729876 680 TLRGKTVVLVTHQL 693
Cdd:TIGR02868 517 ALSGRTVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
525-722 |
4.90e-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: 108.30 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 IlmggaydkARYLQV-------------LHccslnrDLEL-LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:COG4618 426 I--------ARFGDAdpekvvaaaklagVH------EMILrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 658 DDPLSAVDAhVGKHIFEECI---KKtlRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:COG4618 492 DEPNSNLDD-EGEAALAAAIralKA--RGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1151-1318 |
6.81e-24 |
|
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: 101.81 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1151 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 1227
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1228 lsgtirfNLDPfdRHT-DQQIWDALE-------------------------RTFLTK----------------------- 1258
Cdd:cd03257 94 -------SLNP--RMTiGEQIAEPLRihgklskkearkeavllllvgvglpEEVLNRyphelsggqrqrvaiaralalnp 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1259 AIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1318
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
527-725 |
7.94e-24 |
|
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: 101.86 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSGN-IRENIL 593
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRLtVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 594 M-GGAYDKARYLQVLHCCSLNRDLELLPFGDMteigeRGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHI 672
Cdd:COG4555 97 YfAELYGLFDEELKKRIEELIELLGLEEFLDR-----RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 673 FEECIKKtLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKGK 725
Cdd:COG4555 171 LREILRA-LKkeGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1141-1334 |
8.66e-24 |
|
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: 107.30 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSIGLEDLRSK 1217
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1218 LSVIPQDP--VLLSGTIRF-------NLDPFDRHTDQQIWDALERTFLTK---------------------------AII 1261
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDqiaealeNLGLSRAEARARVLELLEAVGLERrldryphqlsggqrqrvaiamalaldpDLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 1262 LIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1334
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
523-715 |
2.23e-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: 99.41 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 523 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMGGAYDKARYLQVLhccslnrdlellpfgdmtEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVg 669
Cdd:cd03369 100 SNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 670 KHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:cd03369 161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
527-710 |
2.55e-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: 98.28 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpqqawivsgnirENILMGGAYDKARYL-- 604
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-----------------KDLASLSPKELARKIay 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 605 --QVLHCCslnrdlellpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHVGKHIFEECI 677
Cdd:cd03214 78 vpQALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLAR 145
|
170 180 190
....*....|....*....|....*....|....
gi 21729876 678 KktlRGKTVVLVTHQL-QYLEFCGQIILLENGKI 710
Cdd:cd03214 146 E---RGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1151-1322 |
6.25e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 104.60 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1151 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 1227
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1228 -------LSGTIRFNLDPFDRHTDQQIWDA---------LERTFLTK-------------AI---------ILI-DEATA 1268
Cdd:COG1123 354 slnprmtVGDIIAEPLRLHGLLSRAERRERvaellervgLPPDLADRyphelsggqrqrvAIaralalepkLLIlDEPTS 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1269 SIDMetdtLIQRTIREAFQ------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1322
Cdd:COG1123 434 ALDV----SVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1139-1329 |
9.62e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.33 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSGTIRFNL--DPFDRHTDQQIWDALE-------------------------------------RTFLTKA 1259
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARmayamdfinkmdngldtvigengvllsggqrqriaiaRALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1260 IILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1329
Cdd:PRK11176 500 PILIlDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
527-709 |
1.03e-22 |
|
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: 97.55 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIRENI- 592
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVRENLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 ----LMGGAYDKARYLQVLHCCSLnRDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHv 668
Cdd:COG4133 98 fwaaLYGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21729876 669 GKHIFEECIKKTL-RGKTVVLVTHQLQYLEFCgQIILLENGK 709
Cdd:COG4133 166 GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1157-1326 |
1.45e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 103.67 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL 1236
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1237 DPFDRHTDQQIWDA-------------------------------------LERTFLTK-AIILIDEATASIDMETDTLI 1278
Cdd:COG4618 427 ARFGDADPEKVVAAaklagvhemilrlpdgydtrigeggarlsggqrqrigLARALYGDpRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21729876 1279 QRTIREA-FQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEF-DRPEVLRK 1326
Cdd:COG4618 507 AAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
527-722 |
1.59e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.83 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIRENI- 592
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMGGAYD------KARYLQVLhccslnRDLELLPFGDmTEIGerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:COG1131 96 FFARLYGlprkeaRERIDELL------ELFGLTDAAD-RKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 667 hVGKHIFEECIKK-TLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQK 722
Cdd:COG1131 165 -EARRELWELLRElAAEGKTVLLSTHYLEEAErLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
505-731 |
2.01e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 103.64 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 505 EGMTRPRDALGPEEEGNSLG---------------PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVG 569
Cdd:PRK10790 320 ELMDGPRQQYGNDDRPLQSGrididnvsfayrddnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 570 VQG-------------SLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSG 636
Cdd:PRK10790 400 LDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 637 GQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifEECIKKTLRG----KTVVLVTHQLQYLEFCGQIILLENGKICE 712
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAIQQALAAvrehTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
250
....*....|....*....
gi 21729876 713 NGTHSELMQKKGKYAQLIQ 731
Cdd:PRK10790 555 QGTHQQLLAAQGRYWQMYQ 573
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
525-710 |
3.08e-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: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIREN 591
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILmggaydkarylqvlhccslnrdlellpfgdmteigerglnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKH 671
Cdd:cd03246 96 IL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21729876 672 IFEECIKKT-LRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:cd03246 134 ALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
524-709 |
4.15e-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: 94.23 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAWivsgniRENILMggaydkar 602
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEEL------RRRIGY-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 603 ylqvLHCcslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL- 681
Cdd:cd00267 78 ----VPQ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLRELAe 128
|
170 180
....*....|....*....|....*....
gi 21729876 682 RGKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:cd00267 129 EGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
527-714 |
9.15e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 93.92 E-value: 9.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------------LAYVPQQAWIVSGNIRENIlm 594
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTLRNNL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 ggaydkarylqvlhccslnrdlellpfgdmteigerGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFe 674
Cdd:cd03247 96 ------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21729876 675 ECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENG 714
Cdd:cd03247 139 SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
527-710 |
1.64e-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: 94.48 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhLL----EGSVGVQG-----------------SLAYVPQQ-AWIV 584
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG----GLdrptSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 585 SGNIRENILMGgaydkARYLQVLHCCSLNRDLELLpfgDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:cd03255 96 DLTALENVELP-----LLLAGVPKKERRERAEELL---ERVGLGDR-LNhypseLSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21729876 660 PLSAVDAHVGKHIFEEcIKKT--LRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:cd03255 167 PTGNLDSETGKEVMEL-LRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1156-1314 |
2.22e-21 |
|
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: 92.64 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLLSG-TI 1232
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1233 RFNLdPFDRHTDQQIWDALERTFLTKA-IILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHIL 1308
Cdd:cd03229 94 LENI-ALGLSGGQQQRVALARALAMDPdVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVV 172
|
....*.
gi 21729876 1309 VMGNGK 1314
Cdd:cd03229 173 VLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
527-709 |
2.78e-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: 93.69 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSL-------------AYVPQ----QawIVSGNIR 589
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrkvGLVFQnpddQ--FFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENIL-----MGGAYDKARylqvlhccslNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:cd03225 95 EEVAfglenLGLPEEEIE----------ERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21729876 664 VDAHVGKHIFEecIKKTLR--GKTVVLVTHQLQYL-EFCGQIILLENGK 709
Cdd:cd03225 165 LDPAGRRELLE--LLKKLKaeGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
527-710 |
3.63e-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: 93.69 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsAILEEMHLLE-GSVGVQGS-------------LAYVPQQAWIVSGNIRENI 592
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVV-ALLENFYQPQgGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMGgaydkarylqvLHCCSLNRDLEL------------LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:cd03248 109 AYG-----------LQSCSFECVKEAaqkahahsfiseLASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21729876 661 LSAVDAHvGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:cd03248 178 TSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1158-1268 |
4.73e-21 |
|
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: 90.78 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIRFNL 1236
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1237 -------DPFDRHTDQQIWDALE------------------------------RTFLTKA-IILIDEATA 1268
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEklglgdladrpvgerpgtlsggqrqrvaiaRALLTKPkLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1149-1314 |
5.70e-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: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1149 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP--V 1226
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 LLSGTIR---------FNLDPFDRhtDQQIWDALERTFLTK---------------------------AIILIDEATASI 1270
Cdd:cd03225 88 FFGPTVEeevafglenLGLPEEEI--EERVEEALELVGLEGlrdrspftlsggqkqrvaiagvlamdpDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 1271 DMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1314
Cdd:cd03225 166 DPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
527-693 |
8.85e-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: 92.53 E-value: 8.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV--------GVQGSLAYVPQQA----WIvsgNIRENILM 594
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQQDallpWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 G----GAYDKARYLQVLHCcslnrdLELLpfgdmteigerGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPL 661
Cdd:cd03293 97 GlelqGVPKAEARERAEEL------LELV-----------GLSgfenayphqLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....
gi 21729876 662 SAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQL 693
Cdd:cd03293 160 SALDALTREQLQEE-LLDIWRetGKTVLLVTHDI 192
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
518-719 |
1.03e-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: 92.64 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 518 EEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG----------------SLAYV 577
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI----NGLErptsGSVLVDGtdltllsgkelrkarrRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 578 PQQAWIVSG-NIRENIlmggAYDkaryLQVLHCCSLNRD---LELLPFGDMTEIGER-GLNLSGGQKQRISLARAVYSDR 652
Cdd:cd03258 88 FQHFNLLSSrTVFENV----ALP----LEIAGVPKAEIEervLELLELVGLEDKADAyPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 653 QIYLLDDPLSAVDAHVGKHIFeECIKKTLR--GKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:cd03258 160 KVLLCDEATSALDPETTQSIL-ALLRDINRelGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1156-1326 |
1.21e-20 |
|
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: 92.56 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDPVLLSG-T 1231
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1232 IRFNLD-PFDRHT-------DQQIWDALE---------------------RTFLTKAI------ILIDEATASIDMETDT 1276
Cdd:cd03261 94 VFENVAfPLREHTrlseeeiREIVLEKLEavglrgaedlypaelsggmkkRVALARALaldpelLLYDEPTAGLDPIASG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1277 LIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRK 1326
Cdd:cd03261 174 VIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
530-710 |
3.52e-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: 90.27 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-----------SLAYVPQQA----WIvsgNIRENI 592
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIagLERPD--SGEILIDGrdvtgvpperrNIGMVFQDYalfpHL---TVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 -----LMGGAYDKARylqvlhccslNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:cd03259 94 afglkLRGVPKAEIR----------ARVRELLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 667 HVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:cd03259 164 KLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
527-662 |
3.60e-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: 88.47 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRENI 592
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 593 LMGG---AYDKARYLQVLHccslnRDLELLPFGDM--TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:pfam00005 81 RLGLllkGLSKREKDARAE-----EALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
524-758 |
4.19e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLsAILEEMH-------LLEG----SVGVQG---SLAYVPQQAWIVSGNIR 589
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFdpqsgriLIDGtdirTVTRASlrrNIAVVFQDAGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMG--GAYDkARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:PRK13657 427 DNIRVGrpDATD-EEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 668 VgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQkmhkeaTSDMLQ 743
Cdd:PRK13657 506 T-----EAKVKAALdelmKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR------AQGMLQ 574
|
250
....*....|....*
gi 21729876 744 DTAKiAEKPKVESQA 758
Cdd:PRK13657 575 EDER-RKQPAAEGAN 588
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
527-710 |
6.17e-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: 88.61 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpQQAWIVSGNIRENIlmGGAYDKARYlqv 606
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRI--GYLPEEPSL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 607 lhccslnrdlellpFGDMTeiGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKK-TLRGKT 685
Cdd:cd03230 85 --------------YENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElKKEGKT 147
|
170 180
....*....|....*....|....*.
gi 21729876 686 VVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:cd03230 148 ILLSSHILEEAErLCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
527-710 |
8.39e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 89.72 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLL-------EGSVGVQG-----------------SLAYVPQQAW 582
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLL-------NILggldrptSGEVLIDGqdisslserelarlrrrHIGFVFQFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 583 IVSG-NIRENILMGGAYDKARYLQvlhccSLNRDLELLpfgDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1136 97 LLPElTALENVALPLLLAGVSRKE-----RRERARELL---ERVGLGDR-LDhrpsqLSGGQQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 657 LDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLEllrELNRE--LGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1156-1316 |
1.06e-19 |
|
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: 87.48 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQdpvlLSGTIRf 1234
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ----LSVGER- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1235 nldpfdrhtdQQIwdALERTFLTKAIILI-DEATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILV 1309
Cdd:cd03216 89 ----------QMV--EIARALARNARLLIlDEPTAALtPAEVERLFKviRRLRA--QGVAVIFISHRLDEVFEiADRVTV 154
|
....*..
gi 21729876 1310 MGNGKVV 1316
Cdd:cd03216 155 LRDGRVV 161
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
518-767 |
1.13e-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: 90.68 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 518 EEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHlLEGSVGVQG-------------SLAYVPQQAWIV 584
Cdd:cd03289 14 EGGNAV---LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 585 SGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:cd03289 90 SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 665 DAhvgkhIFEECIKKTLR----GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIqkmhkeATSD 740
Cdd:cd03289 170 DP-----ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI------SPSD 238
|
250 260 270
....*....|....*....|....*....|..
gi 21729876 741 MLQ-----DTAKIAEKPKVESQALATSLEESL 767
Cdd:cd03289 239 RLKlfprrNSSKSKRKPRPQIQALQEETEEEV 270
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
808-1115 |
1.46e-19 |
|
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: 90.74 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 808 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSsresngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQE------------------HGQVYLSVLGALAILQGITVFQYSMAVSIG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 967
Cdd:cd18559 66 GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 968 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLfLSSTRWMA 1047
Cdd:cd18559 145 PLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPS-IVYLRALA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1048 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18559 224 VRLWCVGPCIVLFASFFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
619-1312 |
1.50e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.48 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 619 LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKHIFEECIkKTLRG---KTVVLVTHQLQY 695
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTI-NNLKGnenRITIIIAHRLST 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 696 LEFCGQIILLENGK-----------------------------------------------ICENGTHSELMQ-KKGKYA 727
Cdd:PTZ00265 643 IRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKnKNGIYY 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 728 QLI--QKMHKEAT--------SDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQLTQEEEME---EGSLSW--RV 792
Cdd:PTZ00265 723 TMInnQKVSSKKSsnndndkdSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASEnnaGGKLPFlrNL 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 793 YHHYIQAAGGY-MVSCIIFFFV--VLIVFLTI---------FSFWWLSYWleqgsgtnssresnGTMADLGNI-ADNPQL 859
Cdd:PTZ00265 803 FKRKPKAPNNLrIVYREIFSYKkdVTIIALSIlvagglypvFALLYAKYV--------------STLFDFANLeANSNKY 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 860 SFYQLVYglnALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDT---IPiGRLLNCFAGDLEQLDQLL-- 934
Cdd:PTZ00265 869 SLYILVI---AIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLvn 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 935 --PIFSeQFLVLslmviavLLIVSVLSPYIL-LMGAIIMVICFIYYMMF-------------KKAIG------VFKRLEN 992
Cdd:PTZ00265 945 niVIFT-HFIVL-------FLVSMVMSFYFCpIVAAVLTGTYFIFMRVFairarltankdveKKEINqpgtvfAYNSDDE 1016
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 993 YSRSPLFShILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNylllflsstrwmALRLEIMTNLVTLAVALFVAFGISST 1072
Cdd:PTZ00265 1017 IFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNK------------GQKRKTLVNSMLWGFSQSAQLFINSF 1083
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1073 PY---SFKVMAVNIVLQ--LASSFQ-------ATARIGLETEAQfTAVERILQYMKMCVSEAPLHME---GTSCPQGWPQ 1137
Cdd:PTZ00265 1084 AYwfgSFLIRRGTILVDdfMKSLFTflftgsyAGKLMSLKGDSE-NAKLSFEKYYPLIIRKSNIDVRdngGIRIKNKNDI 1162
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1138 HGEIIFQDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL------------------------ 1191
Cdd:PTZ00265 1163 KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqd 1241
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1192 ------------------------------VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGT----IRF--- 1234
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSiyenIKFgke 1321
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1235 -----------------------------NLDPFDRHTD--QQIWDALERTFLTK-AIILIDEATASIDMETDTLIQRTI 1282
Cdd:PTZ00265 1322 datredvkrackfaaidefieslpnkydtNVGPYGKSLSggQKQRIAIARALLREpKILLLDEATSSLDSNSEKLIEKTI 1401
|
890 900 910
....*....|....*....|....*....|..
gi 21729876 1283 REAFQGC--TVLVIAHRVTTVLNCDHILVMGN 1312
Cdd:PTZ00265 1402 VDIKDKAdkTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
521-735 |
1.64e-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: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 521 NSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGN 587
Cdd:cd03288 31 NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:cd03288 111 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 668 VgKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELM-QKKGKYAQLIqKMHK 735
Cdd:cd03288 191 T-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV-RTDK 257
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1156-1321 |
1.12e-18 |
|
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: 88.57 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLR----SKLSVIPQD---- 1224
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRkirgREIQMIFQDpmts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1225 --PVLlsgTIRFNL-DPFDRHTD-------QQIWDALERTFLTKA--------------------I---------ILI-D 1264
Cdd:COG0444 99 lnPVM---TVGDQIaEPLRIHGGlskaearERAIELLERVGLPDPerrldryphelsggmrqrvmIaralalepkLLIaD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1265 EATASIDMetdtLIQRTI-------REAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE-------FDRP 1321
Cdd:COG0444 176 EPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelFENP 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1156-1316 |
1.29e-18 |
|
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: 86.05 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSKLSVIPQ------------ 1223
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQrrsidrdfpisv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 -DPVLLSGTIRFNLDPFDRHTDQQIWD-ALE---------------------RTFLTKA------IILIDEATASIDMET 1274
Cdd:cd03235 88 rDVVLMGLYGHKGLFRRLSKADKAKVDeALErvglseladrqigelsggqqqRVLLARAlvqdpdLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21729876 1275 DTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMgNGKVV 1316
Cdd:cd03235 168 QEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1141-1317 |
2.24e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 85.71 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSI---GLEDL 1214
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1215 RSKLSVIPQDPVLLSG-TIRFNLD-PF------DRHTDQQIWDALERTFLT-KA-------------------------- 1259
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEdKAdaypaqlsggqkqrvgiaralannpk 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1260 IILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1317
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
527-719 |
2.32e-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: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQGSLAYV---PQQAWIvsG------------NIR 589
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIagLE--TPDSGRIVLNGRDLFTnlpPRERRV--GfvfqhyalfphmTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMG---GAYDKARYLQVLHccslnrdlELLPFGDMTEIGER--GlNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:COG1118 94 ENIAFGlrvRPPSKAEIRARVE--------ELLELVQLEGLADRypS-QLSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 665 DAHVgkhifeeciKKTLR----------GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:COG1118 165 DAKV---------RKELRrwlrrlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
527-709 |
2.41e-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: 84.16 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG---------------SLAYVPQQAWIVSG-NI 588
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIagLEE--PDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENILMGgaydkarylqvlhccslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:cd03229 94 LENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21729876 669 GKHIFEECikKTLR---GKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:cd03229 136 RREVRALL--KSLQaqlGITVVLVTHDLDEAArLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
527-719 |
2.94e-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: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHLL------EGSVGVQGSLAYVP---------------QQAWIVS 585
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLR-LLNRLNDLipgapdEGEVLLDGKDIYDLdvdvlelrrrvgmvfQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 586 GNIRENILMGgaydkarylQVLHCCSLNRDL-----ELLPFGDMT-EIGER--GLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:cd03260 95 GSIYDNVAYG---------LRLHGIKLKEELderveEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 658 DDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSEL 719
Cdd:cd03260 166 DEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
525-720 |
4.44e-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: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRE 590
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NI-----LMGgaYDKARYLQvlhccslnRDLELLPFGDMTEIGERGL---NLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03295 95 NIalvpkLLK--WPKEKIRE--------RADELLALVGLDPAEFADRyphELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 663 AVDAHVGKHIFEECIK-KTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELM 720
Cdd:cd03295 165 ALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
527-721 |
4.99e-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: 84.86 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS----------------LAYVPQQ-AWIVSGNIR 589
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENI----LMGGAYDKARY----LQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPL 661
Cdd:cd03261 96 ENVafplREHTRLSEEEIreivLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 662 SAVDAhVGKHIFEECI---KKTLrGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:cd03261 165 AGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
527-737 |
9.33e-18 |
|
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: 89.62 E-value: 9.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRENIL 593
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 594 MGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhif 673
Cdd:TIGR00957 1382 PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET----- 1456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 674 EECIKKTLRGK----TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGkyaqLIQKMHKEA 737
Cdd:TIGR00957 1457 DNLIQSTIRTQfedcTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG----IFYSMAKDA 1520
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
527-723 |
1.46e-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: 83.15 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQG-------------SLAYVPQQAW--IVSGNI 588
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL---NGLLkptSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENIL-----MGGAYDKARyLQVLHCcslnrdLELLpfgDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:COG1122 94 EEDVAfgpenLGLPREEIR-ERVEEA------LELV---GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 663 AVDAHvGKHIFEECIKK-TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQKK 723
Cdd:COG1122 164 GLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
523-731 |
1.65e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.03 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 523 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:PLN03130 1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV----D 665
Cdd:PLN03130 1331 FNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdvrtD 1410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 666 AHVGKHIFEEcikktLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGK-YAQLIQ 731
Cdd:PLN03130 1411 ALIQKTIREE-----FKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSaFSKMVQ 1472
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
525-721 |
1.92e-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: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSL-------------------AYVPQQA---- 581
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALAL---MGLLPHGGRISGEVlldgrdllelsealrgrriGMVFQDPmtql 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 582 --WIVSGNIRE---NILMGGAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1123 97 npVTVGDQIAEaleNLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 657 LDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG1123 166 ADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
527-723 |
2.19e-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: 83.00 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS----------------LAYVPQQAWIVSG-NIR 589
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQFNLIERlSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMG------------GAYDKARYLQVLHCcsLNRdLELLPFgdmteIGERGLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:cd03256 97 ENVLSGrlgrrstwrslfGLFPKEEKQRALAA--LER-VGLLDK-----AYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 658 DDPLSAVD---AHVGKHIFEEcIKKTlRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQKK 723
Cdd:cd03256 169 DEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
525-693 |
2.41e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--SLAYVPQQ---AWIVSGNIRENILMG---- 595
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 -------GAYDKARYLQVLHCCSLnRDLELLPFGDmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:NF040873 86 rglwrrlTRDDRAAVDDALERVGL-ADLAGRQLGE----------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*
gi 21729876 669 GKHIFEECIKKTLRGKTVVLVTHQL 693
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDL 179
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1120-1329 |
2.65e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.08 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1120 SEAPLHMEGT-SCPQGwpqHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGR 1198
Cdd:PRK10789 295 AEAPVVKDGSePVPEG---RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1199 ILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDA------------------------- 1250
Cdd:PRK10789 372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVarlasvhddilrlpqgydtevgerg 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1251 ------------LERTFLTKAIILI-DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1317
Cdd:PRK10789 450 vmlsggqkqrisIARALLLNAEILIlDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
250
....*....|..
gi 21729876 1318 FDRPEVLRKKPG 1329
Cdd:PRK10789 530 RGNHDQLAQQSG 541
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
527-721 |
4.37e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 82.54 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhLLE----GSVGVQGS-------------LAYVPQQA-------W 582
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALA----GLErpwsGEVTFDGRpvtrrrrkafrrrVQMVFQDPyaslhprH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 583 IVSGNIRENI-LMGGAYDKARYLQVLHCCSLNRDLellpfgdmteigergLN-----LSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1124 97 TVDRILAEPLrIHGLPDREERIAELLEQVGLPPSF---------------LDryphqLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 657 LDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYLEF-CGQIILLENGKICENGTHSELMQ 721
Cdd:COG1124 162 LDEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
527-691 |
5.59e-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: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSV--------GVQGSLAYVPQQA----WIvsgNIRENI 592
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIagLEK--PTSGEVlvdgkpvtGPGPDRGVVFQEPallpWL---TVLDNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMG---------GAYDKARYLqvlhccslnrdLELLpfgdmteigerGL---------NLSGGQKQRISLARAVYSDRQI 654
Cdd:COG1116 102 ALGlelrgvpkaERRERAREL-----------LELV-----------GLagfedayphQLSGGMRQRVAIARALANDPEV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 21729876 655 YLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTH 691
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTH 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1158-1322 |
7.08e-17 |
|
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: 85.51 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPvllsgtirF 1234
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--------F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1235 N-LDPfdRHT---------------------DQQIWDALERTFLT----------------------KAIIL------ID 1264
Cdd:COG4172 373 GsLSP--RMTvgqiiaeglrvhgpglsaaerRARVAEALEEVGLDpaarhryphefsggqrqriaiaRALILepkllvLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1265 EATASIDMetdtLIQRTIREAFQ------GCTVLVIAH--RVTTVLnCDHILVMGNGKVVE-------FDRPE 1322
Cdd:COG4172 451 EPTSALDV----SVQAQILDLLRdlqrehGLAYLFISHdlAVVRAL-AHRVMVMKDGKVVEqgpteqvFDAPQ 518
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
530-710 |
1.10e-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: 79.99 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMHlleGSVGVQG----------SLAYVPQ--QAWIVSGNIRENILM 594
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLakiLAGLIKESS---GSILLNGkpikakerrkSIGYVMQdvDYQLFTDSVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 G---GAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH---- 667
Cdd:cd03226 96 GlkeLDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmer 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21729876 668 VGKhIFEECikkTLRGKTVVLVTHQLQYL-EFCGQIILLENGKI 710
Cdd:cd03226 165 VGE-LIREL---AAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
167-427 |
1.24e-16 |
|
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: 81.83 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 167 ALLGICFCIASVLGPILIiPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSS-SWIINqRTAIRFRAAVSSFAFEK 245
Cdd:cd18598 3 GLLKLLADVLGFAGPLLL-NKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHyNFQMN-KVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 246 LIQFKSVI--HITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYtAFIAILCYLLV-FPL 316
Cdd:cd18598 81 ALRVRSSSlsKFSTGEIVNLMSTDADRIvnfcpsFHDLWSLPLQIIVALYLL------YQQVGV-AFLAGLVFALVlIPI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 317 AVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKE------RKLLEK-CGLVQSLTSIt 389
Cdd:cd18598 154 NKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKElkalkgRKYLDAlCVYFWATTPV- 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 21729876 390 LFIIPTVATAVWvlihtsLKLKLTASMAFSMLASLNLL 427
Cdd:cd18598 233 LISILTFATYVL------MGNTLTAAKVFTSLALFNML 264
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
518-767 |
1.41e-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: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 518 EEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHlLEGSVGVQG-------------SLAYVPQQAWIV 584
Cdd:TIGR01271 1229 EAGRAV---LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 585 SGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 665 DAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHK-EATSDMLQ 743
Cdd:TIGR01271 1385 DP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRlKLFPLHRR 1463
|
250 260
....*....|....*....|....
gi 21729876 744 DTAKIAEKPKVesQALATSLEESL 767
Cdd:TIGR01271 1464 NSSKRKPQPKI--TALREEAEEEV 1485
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1141-1327 |
2.12e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.81 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDP------VLLSGTIRFNLD--PFDRHTDQQIWDAL------------ERTFLT----------------KAIILID 1264
Cdd:PRK13632 88 IFQNPdnqfigATVEDDIAFGLEnkKVPPKKMKDIIDDLakkvgmedyldkEPQNLSggqkqrvaiasvlalnPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 1265 EATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP-EVLRKK 1327
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNK 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
527-715 |
2.63e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLL----------SAILEEMHLLEGSVGVQGSLA-----------YVPQQAWIVS 585
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdKSAGSHIELLGRTVQREGRLArdirksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 586 G-NIRENILMGGAYDKARYLQVLHCCSLNRDLELLPfgDMTEIG------ERGLNLSGGQKQRISLARAVYSDRQIYLLD 658
Cdd:PRK09984 100 RlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQ--ALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 659 DPLSAVDAHVGKHIFEecikkTLR------GKTVVLVTHQLQY-LEFCGQIILLENGKICENGT 715
Cdd:PRK09984 178 EPIASLDPESARIVMD-----TLRdinqndGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
534-716 |
2.85e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 534 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslAYVPQQAWIVSGNI---------------RENILMGGAY 598
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARARIgvvpqfdnldleftvRENLLVFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 dkarylqvlhcCSLN-RDLE-----LLPFGDM-TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKH 671
Cdd:PRK13536 142 -----------FGMStREIEavipsLLEFARLeSKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARH 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 672 IFEECIKKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KICENGTH 716
Cdd:PRK13536 210 LIWERLRSLLaRGKTILLTTHFMEEAErLCDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1154-1315 |
3.04e-16 |
|
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: 78.24 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1154 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLL 1228
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRkregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1229 SGTIRFNLdpfdrhT--------DQQ--IwdaLERTFLTKA-IILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAH 1296
Cdd:cd03215 92 DLSVAENI------AlssllsggNQQkvV---LARWLARDPrVLILDEPTRGVDVGAKAEIYRLIRElADAGKAVLLISS 162
|
170 180
....*....|....*....|
gi 21729876 1297 RVTTVLN-CDHILVMGNGKV 1315
Cdd:cd03215 163 ELDELLGlCDRILVMYEGRI 182
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
163-431 |
3.87e-16 |
|
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: 80.38 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 163 LIFDALLGICFCIASVLGPIL---IIPKILEYSEEQLGNVVHGVGLCFALFLSECVksLSFSSSWIINqRTAIRFRAAVS 239
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVlgrILDVLLPDGDPETQALNVYSLALLLLGLAQFI--LSFLQSYLLN-HTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 240 SFAFEKLIQ-----FKSvihITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYL-LV 313
Cdd:pfam00664 78 RKLFKKILRqpmsfFDT---NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLpLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 314 FPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFII 393
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 21729876 394 PTVATAV--WVLIHTSLKLKLTASMAFSMLASLNLLRLSV 431
Cdd:pfam00664 235 GYLSYALalWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1141-1334 |
4.10e-16 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 79.27 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLS- 1219
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1220 VIPQDPVLLSGTIRFN---------------------------LDPF---DRHTDQQIWDALERTFLTKA------IILI 1263
Cdd:cd03295 80 VIQQIGLFPHMTVEENialvpkllkwpkekireradellalvgLDPAefaDRYPHELSGGQQQRVGVARAlaadppLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1264 DEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1334
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1157-1324 |
5.23e-16 |
|
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: 78.76 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLLS 1229
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1230 GTIRFNLDPFDRHT---DQQIWDALERTFLTKA----------------------------------IILIDEATASIDM 1272
Cdd:cd03260 95 GSIYDNVAYGLRLHgikLKEELDERVEEALRKAalwdevkdrlhalglsggqqqrlclaralanepeVLLLDEPTSALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1273 ETDTLIQRTIREAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVL 1324
Cdd:cd03260 175 ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
525-719 |
5.25e-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: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQG-----------SLAYVPQQ-AWIVSGNIRE 590
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIagLE--RPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGgaydkaryLQVLHCCSL-------NRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03296 94 NVAFG--------LRVKPRSERppeaeirAKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 663 AVDAHVGKHifeecIKKTLR------GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:cd03296 166 ALDAKVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1150-1322 |
7.57e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1150 YRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLRSKLSVIPQDPV-- 1226
Cdd:PRK13644 11 YPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPEtq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 ---------LLSGTIRFNLDPFD-----------------RHTDQQIWDALERTFLTKAIIL--------IDEATASIDM 1272
Cdd:PRK13644 90 fvgrtveedLAFGPENLCLPPIEirkrvdralaeiglekyRHRSPKTLSGGQGQCVALAGILtmepecliFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1273 ET-DTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 1322
Cdd:PRK13644 170 DSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
527-721 |
8.98e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 77.86 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQGS--------------LAYVPQQAWIVSG-NI 588
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MGLLpprSGSIRFDGRditglppheraragIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENILMG---GAYDKARYlqvlhccSLNRDLELLPfgdmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDP- 660
Cdd:cd03224 93 EENLLLGayaRRRAKRKA-------RLERVYELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPs 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 661 --LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:cd03224 161 egLAPK---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
527-714 |
9.52e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.96 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLayvpqqAWIVSGNI--------RENILMGGAy 598
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSLLGLGGgfnpeltgRENIYLNGR- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 dkarylqvLHCCSLNRDLELLPF-GDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvgkhiF 673
Cdd:cd03220 111 --------LLGLSRKEIDEKIDEiIEFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA-----F 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 674 -EECIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENG 714
Cdd:cd03220 178 qEKCQRRlrelLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1156-1317 |
9.86e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.12 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDPVLLS--- 1229
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLSsrt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1230 --GTIRFNL-----DPFDRhtDQQIWDALERTFLT-KA--------------------------IILIDEATASIDMETd 1275
Cdd:COG1135 99 vaENVALPLeiagvPKAEI--RKRVAELLELVGLSdKAdaypsqlsggqkqrvgiaralannpkVLLCDEATSALDPET- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1276 T-----LIQRtIREAFqGCTVLVIAH------RVttvlnCDHILVMGNGKVVE 1317
Cdd:COG1135 176 TrsildLLKD-INREL-GLTIVLITHemdvvrRI-----CDRVAVLENGRIVE 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
527-706 |
1.06e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGV----------QGSLAYVPQQA---WIVSgNIRENIL 593
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptrqalqKNLVAYVPQSEevdWSFP-VLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 594 MGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI 672
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 21729876 673 FEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLE 706
Cdd:PRK15056 182 IS--LLRELRdeGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
527-721 |
1.65e-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: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemHLLE---GSVGVQG----------------SLAYVPQQ------- 580
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLL---GLLRptsGSILFDGkdltklsrrslrelrrRVQMVFQDpysslnp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 581 ----AWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRD-LELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIY 655
Cdd:COG1123 358 rmtvGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 656 LLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG1123 427 ILDEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVvRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
527-721 |
2.44e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQ-----AWIVsgni 588
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHsslafPFTV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENILMG-------GAYDKARYLQVLHCCslnrdlellpfgDMTEIGERG-LNLSGGQKQRISLARA-------VYSDRQ 653
Cdd:COG4559 93 EEVVALGraphgssAAQDRQIVREALALV------------GLAHLAGRSyQTLSGGEQQRVQLARVlaqlwepVDGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 654 IYLLDDPLSAVD-AHvgKHIFEECIKK-TLRGKTVVLVTHQL----QYlefCGQIILLENGKICENGTHSELMQ 721
Cdd:COG4559 161 WLFLDEPTSALDlAH--QHAVLRLARQlARRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVLT 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
864-1227 |
2.91e-15 |
|
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: 80.61 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 864 LVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEqFLV 943
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 944 LSLMVIAVLLIVSVLSPYILLMGAIIMVIC-FIYYMMFKKAIGVFKRL-ENYSRspLFSHILNSLQG-----LSSihvyG 1016
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTLVLLGLGvAGYRLLVRRARRHLRRArEAEDR--LFKHFRALLEGfkelkLNR----R 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1017 KTEDFISQfkRLTDAQNNYLLLFLSSTRWMALrLEIMTN---LVTLAVALFVAFGISSTPYS----------FKVMAVNI 1083
Cdd:COG4615 205 RRRAFFDE--DLQPTAERYRDLRIRADTIFAL-ANNWGNllfFALIGLILFLLPALGWADPAvlsgfvlvllFLRGPLSQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1084 VLQLASSFqATARIgleteaqftAVERILQyMKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYR---DNTPTVLHG 1160
Cdd:COG4615 282 LVGALPTL-SRANV---------ALRKIEE-LELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPgedGDEGFTLGP 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL 1227
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHL 417
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1141-1314 |
4.57e-15 |
|
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: 75.20 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDN---TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsK 1217
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1218 LSVIPQDPVLLSGTIRFNL---DPFDR------------HTDQQIWD----------------------ALERTFLTKA- 1259
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDEeryekvikacalEPDLEILPdgdlteigekginlsggqkqriSLARAVYSDAd 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1260 IILIDEATASIDMET-DTLIQRTIREAFQGC-TVLVIAHRVTTVLNCDHILVMGNGK 1314
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1156-1325 |
4.57e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL-----LSG 1230
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpftVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1231 TIRFNLDPF--DRHTDQQIWD-ALERTFLT---------------------------------KAIILIDEATASIDM-- 1272
Cdd:PRK13548 96 VVAMGRAPHglSRAEDDALVAaALAQVDLAhlagrdypqlsggeqqrvqlarvlaqlwepdgpPRWLLLDEPTSALDLah 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1273 ETDTLiqRTIRE--AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRP-EVLR 1325
Cdd:PRK13548 176 QHHVL--RLARQlaHERGLAVIVVLHD----LNlaaryADRIVLLHQGRLVADGTPaEVLT 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
530-714 |
6.36e-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: 75.62 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQA-------WIVSG 586
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDPmsslnprMTIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 587 NIRE--NILMGGAYDKARYLQVLhccslnRDLELLPfgdmteIGERGLN-----LSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:cd03257 104 QIAEplRIHGKLSKKEARKEAVL------LLLVGVG------LPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 660 PLSAVDAHVGKHIFEEcIK--KTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENG 714
Cdd:cd03257 172 PTSALDVSVQAQILDL-LKklQEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
527-719 |
8.45e-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: 77.45 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG-----------SLAYVPQqawivSG------N 587
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFET--PDSGRILLDGrdvtglppekrNVGMVFQ-----DYalfphlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENI---LMGGAYDKARYLQvlhccslnRDLELLpfgDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:COG3842 94 VAENVafgLRMRGVPKAEIRA--------RVAELL---ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 661 LSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:COG3842 163 LSALDAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
530-721 |
1.08e-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: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMhllEGSVGVQG-SLAYVPQQAWIVS-----GN------IRENILM 594
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIagfLPPD---SGRILWNGqDLTALPPAERPVSmlfqeNNlfphltVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 G-------GAYDKARYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-- 665
Cdd:COG3840 95 GlrpglklTAEQRAQVEQALERVGLAGLLDRLP-------GQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 666 -----AHVGKHIFEEcikktlRGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG3840 164 lrqemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
530-719 |
1.49e-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: 74.46 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVG---------------VQGSLAYVPQqawivsgnirENILM 594
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKML---TGELRPTSGtayingysirtdrkaARQSLGYCPQ----------FDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 GG--AYDKARYLQVLHCCSLN----------RDLELLPFGDmTEIGerglNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03263 88 DEltVREHLRFYARLKGLPKSeikeevelllRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 663 AVDaHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEF-CGQIILLENGKICENGTHSEL 719
Cdd:cd03263 163 GLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1157-1325 |
2.53e-14 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 73.62 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDPVLLSG-TIRF 1234
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1235 NLD----PFDRHTDQQIWD----------------------------ALERTFLTKA-IILIDEATA----SIDMETDTL 1277
Cdd:cd03224 95 NLLlgayARRRAKRKARLErvyelfprlkerrkqlagtlsggeqqmlAIARALMSRPkLLLLDEPSEglapKIVEEIFEA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21729876 1278 IqRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLR 1325
Cdd:cd03224 175 I-RELRD--EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
527-710 |
2.80e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.88 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG-----------SLAYVPQQaWIV--SGNIREN 591
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLED--PTSGEILIGGrdvtdlppkdrNIAMVFQS-YALypHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 I-----LMGgaYDKARylqvlhccslnRD------LELLpfgDMTEIGER-GLNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:COG3839 96 IafplkLRK--VPKAE-----------IDrrvreaAELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21729876 660 PLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:COG3839 160 PLSNLDAKL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
527-710 |
3.16e-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: 73.06 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-----------SLAYVPQQ-AWIVSGNIRENI 592
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIagLEEPT--SGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMG-------------GAYDKARYLQVLHCcsLNRdlellpfgdmteigeRGLNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:cd03301 94 AFGlklrkvpkdeideRVREVAELLQIEHL--LDR---------------KPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21729876 660 PLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:cd03301 157 PLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
849-1068 |
3.18e-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: 74.89 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 849 DLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLE 928
Cdd:cd07346 28 DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 929 QLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQG 1008
Cdd:cd07346 108 AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1009 LSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd07346 188 IRVVKAFAAEEREIERFREANRD---LRDANLRAARLSALFSPLIGLLTALGTALVLLYG 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
527-710 |
4.54e-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: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLlEGSVGVQG----------SLAYVPQQAwIVSGN--IREN 591
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGV-SGEVLINGrpldkrsfrkIIGYVPQDD-ILHPTltVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMggaydkarylqVLHCcslnrdlellpfgdmteigeRGLnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKH 671
Cdd:cd03213 103 LMF-----------AAKL--------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 672 IFeecikKTLR-----GKTVVLVTHQLQYL--EFCGQIILLENGKI 710
Cdd:cd03213 150 VM-----SLLRrladtGRTIICSIHQPSSEifELFDKLLLLSQGRV 190
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
527-719 |
6.67e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEE---------------MHLLEGSVGvqgslaYVPQQ-AWIVSGNI 588
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIagLEHqtsghirfhgtdvsrLHARDRKVG------FVFQHyALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENILMG-----------GAYDKARYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK10851 92 FDNIAFGltvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 658 DDPLSAVDAHVGKHifeecIKKTLRGK------TVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK10851 161 DEPFGALDAQVRKE-----LRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
527-715 |
6.96e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLL---SAILE------EMH-----LLEGSVGVQGSLayvpqqawivSGniRENI 592
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLkliAGILEptsgrvEVNgrvsaLLELGAGFHPEL----------TG--RENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMGGAydkarylqvLHCCSLNRDLELLPF-GDMTEIGE------RglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:COG1134 110 YLNGR---------LLGLSRKEIDEKFDEiVEFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 666 AHvgkhiF-EECIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGT 715
Cdd:COG1134 179 AA-----FqKKCLARirelRESGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGD 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
530-710 |
8.00e-14 |
|
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: 71.93 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS---------LAYVPQQAwivsgnirenilmgGAY-- 598
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEER--------------GLYpk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 ----DKARYLQVLHCCS----LNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 669
Cdd:cd03269 85 mkviDQLVYLAQLKGLKkeeaRRRIDEWLERLELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21729876 670 KHIFEECIKKTLR-GKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:cd03269 164 VELLKDVIRELARaGKTVILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1144-1326 |
9.01e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.34 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1144 QDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVI 1221
Cdd:PRK13636 9 EELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1222 PQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERT---------------------------FLTKAIILIDE 1265
Cdd:PRK13636 88 FQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKRTgiehlkdkpthclsfgqkkrvaiagvlVMEPKVLVLDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1266 ATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTV-LNCDHILVMGNGKVV-------EFDRPEVLRK 1326
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVIlqgnpkeVFAEKEMLRK 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1156-1316 |
1.09e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.04 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVdicSIGLEDLRSKLSVIPQDPVLLSG-TI 1232
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1233 RFNLDpfdrhtdqqiWDAL-------ERTFLTKA--------IILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAH 1296
Cdd:cd03213 100 RETLM----------FAAKlrglsggERKRVSIAlelvsnpsLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIH 169
|
170 180
....*....|....*....|..
gi 21729876 1297 RVTTVL--NCDHILVMGNGKVV 1316
Cdd:cd03213 170 QPSSEIfeLFDKLLLLSQGRVI 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
526-722 |
1.10e-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: 71.98 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 526 ELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-----------LAYVPQQ-AWIVSGNIRENIL 593
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 594 MGgaydkaryLQVLHCCSLNRDLELLPFGDMTEIGE----RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03299 94 YG--------LKKRKVDKKEIERKVLEIAEMLGIDHllnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 670 KHIFEEcIKKTLR--GKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQK 722
Cdd:cd03299 166 EKLREE-LKKIRKefGVTVLHVTHDFEEAWALAdKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1141-1315 |
1.22e-13 |
|
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: 71.67 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 1217
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1218 LSVIPQDPVLLSgtirfNLDPFD-------------RHTDQQIWDALE---------------------RTFLTKAI--- 1260
Cdd:cd03292 80 IGVVFQDFRLLP-----DRNVYEnvafalevtgvppREIRKRVPAALElvglshkhralpaelsggeqqRVAIARAIvns 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1261 ---ILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKV 1315
Cdd:cd03292 155 ptiLIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
527-721 |
1.49e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRENI 592
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 lmggAYDKARYLQvlHCCSLNRDLELLPFGDM-----TEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:PRK11231 98 ----AYGRSPWLS--LWGRLSAEDNARVNQAMeqtriNHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 667 HvgkHIFEecIKKTLR-----GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK11231 172 N---HQVE--LMRLMRelntqGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1141-1317 |
2.14e-13 |
|
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: 70.96 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGledlrSKL 1218
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLL------------------SGTIR----------FNLDPFDRHTDQQIWD------ALERTFLTK-AIILI 1263
Cdd:cd03293 76 GYVFQQDALLpwltvldnvalglelqgvPKAEAreraeellelVGLSGFENAYPHQLSGgmrqrvALARALAVDpDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1264 DEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVT-TVLNCDHILVMGN--GKVVE 1317
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
527-721 |
2.68e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.28 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEM---HLLEGSVGVQGSLAYV---PQQAWIVSGNIR--------E 590
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEItsgDLIVDGLKVNDPKVDErliRQEAGMVFQQFYlfphltalE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMG-----GAYDKARYLQVLhccslnrdlELLpfgdmTEIG--ERGLN----LSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK09493 97 NVMFGplrvrGASKEEAEKQAR---------ELL-----AKVGlaERAHHypseLSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 660 PLSAVDAH-------VGKHIFEEcikktlrGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ 721
Cdd:PRK09493 163 PTSALDPElrhevlkVMQDLAEE-------GMTMVIVTHEIGFAEKVAsRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
527-692 |
5.15e-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: 68.33 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVG--VQGSLAYVPQQAWIVSGNIREnilmggaydkaryl 604
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGmpEGEDLLFLPQRPYLPLGTLRE-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 605 QVLHccslnrdlellPFGDMteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECikkTLRGK 684
Cdd:cd03223 83 QLIY-----------PWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KELGI 139
|
....*...
gi 21729876 685 TVVLVTHQ 692
Cdd:cd03223 140 TVISVGHR 147
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
525-707 |
5.68e-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: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLLEGSVGVQGS-----------LAYVPQQAWIVSG-NIR 589
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVLLNGRrltalpaeqrrIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMG------GAYDKARYLQVLhccslnRDLELLPFGD---MTeigerglnLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:COG4136 95 ENLAFAlpptigRAQRRARVEQAL------EEAGLAGFADrdpAT--------LSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21729876 661 LSAVDAH----VGKHIFEEcIKKtlRGKTVVLVTHQLQYLEFCGQIILLEN 707
Cdd:COG4136 161 FSKLDAAlraqFREFVFEQ-IRQ--RGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
530-719 |
6.42e-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: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLS------------AILEEMHLLEGSVGVQGSLAYVPQQAwIVSGNI--RENILM- 594
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKmlttllkptsgrATVAGHDVVREPREVRRRIGIVFQDL-SVDDELtgWENLYIh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 GGAY----DKARylqvlhccslNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03265 98 ARLYgvpgAERR----------ERIDELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 670 KHIFEEcIKKTLR--GKTVVLVTHqlqYLE----FCGQIILLENGKICENGTHSEL 719
Cdd:cd03265 168 AHVWEY-IEKLKEefGMTILLTTH---YMEeaeqLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
529-710 |
8.42e-13 |
|
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: 68.86 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 529 KINLVVSkGMMLGVCGNTGSGKSSLLSAI------------LEEMHLLEGSVGV-----QGSLAYVPQQAWIVSG-NIRE 590
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIaglekpdggtivLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGgaydkarylqvLHCCSLNRDL----ELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:cd03297 95 NLAFG-----------LKRKRNREDRisvdELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 666 AHVGKHIFEEC--IKKTLRGkTVVLVTHQLQYLEF-CGQIILLENGKI 710
Cdd:cd03297 164 RALRLQLLPELkqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
527-723 |
8.88e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAileeMHLLE----GSVGVQGS---LAYVPQQAWIVSgnIRENILM-GGAY 598
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLEmprsGTLNIAGNhfdFSKTPSDKAIRE--LRRNVGMvFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 DKARYLQVLH------CCSL--------NRDLELLPFGDMTEIGER-GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK11124 92 NLWPHLTVQQnlieapCRVLglskdqalARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 664 VDAHVGKHIFEecIKKTLR--GKTVVLVTHQlqyLEFCGQI----ILLENGKICENGTHSELMQKK 723
Cdd:PRK11124 172 LDPEITAQIVS--IIRELAetGITQVIVTHE---VEVARKTasrvVYMENGHIVEQGDASCFTQPQ 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
527-721 |
1.09e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIV-SGNIRENI 592
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMGGA-----YDKARYL--QVLHCCslnrdlellpfgDMTEIGERG-LNLSGGQKQRISLARA------VYSDRQIYLLD 658
Cdd:PRK13548 98 AMGRAphglsRAEDDALvaAALAQV------------DLAHLAGRDyPQLSGGEQQRVQLARVlaqlwePDGPPRWLLLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 659 DPLSAVD-AHvGKHIFEecIKKTL---RGKTVVLVTHQL----QYlefCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK13548 166 EPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVLT 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
527-712 |
1.14e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.93 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQAWIVSG-NIR 589
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENIL-------MGGAYDKARYLQVLhccslnrdlellpfgDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLD 658
Cdd:COG2884 98 ENVAlplrvtgKSRKEIRRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 659 DPLSAVDAHVGK---HIFEEcIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGKICE 712
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 ... |
530-714 |
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 21729876 530 INLVVSKGMmLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------------LAYVPQQaWIVSGNIRenilmggA 597
Cdd:cd03264 19 VSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQE-FGVYPNFT-------V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 598 YDKARYLQVLHCCS-------LNRDLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 669
Cdd:cd03264 90 REFLDYIAWLKGIPskevkarVDEVLELV---NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 670 KHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENG 714
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1153-1323 |
1.27e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1153 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGlEDLRSKLSVIPQD----PV 1226
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPEDrkgeGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 LLSGTIRFN-----LDPF-----------DRHTDQQIwDALE------------------------RTFLTKA-IILIDE 1265
Cdd:COG1129 342 VLDLSIRENitlasLDRLsrgglldrrreRALAEEYI-KRLRiktpspeqpvgnlsggnqqkvvlaKWLATDPkVLILDE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1266 ATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVL-NCDHILVMGNGKVV-EFDRPEV 1323
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
525-694 |
1.41e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.34 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVP---------QQAWIVSGNIRENILMG 595
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 ---GAYDKARYLQVLHccslnrdlELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKH 671
Cdd:PRK11248 95 lqlAGVEKMQRLEIAH--------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....
gi 21729876 672 IFEECIKKTLR-GKTVVLVTHQLQ 694
Cdd:PRK11248 167 MQTLLLKLWQEtGKQVLLITHDIE 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
532-714 |
1.49e-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: 68.29 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 532 LVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAWIVSGNIRENILMGgaydkarYLQVLHcc 610
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFA-------HLTVEQ-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 611 slNRDLELLPFGDMTE---------IGERGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHV 668
Cdd:cd03298 90 --NVGLGLSPGLKLTAedrqaievaLARVGLAglekrlpgeLSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 669 GKHIFEECIKktlRGKTVVLVTHQLQYLEFCGQ-IILLENGKICENG 714
Cdd:cd03298 168 LDLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
527-710 |
1.73e-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: 67.94 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQGSLAYVPQQAWIvsgNIRENILM-GGAYDKARY 603
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNIN---ELRQKVGMvFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 604 LQVLHCCSLN-RDLELLPFGDMTEIGER-----GL---------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:cd03262 91 LTVLENITLApIKVKGMSKAEAEERALEllekvGLadkadaypaQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21729876 669 GKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKI 710
Cdd:cd03262 171 VGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
525-715 |
1.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMhllEGSVGVQG-------SLAYVPQQAWIVSGNiRENILM 594
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQ---KGKVLVSGidtgdfsKLQGIRKLVGIVFQN-PETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 GGAYDKARYLQVLHCCSlnRDLELLPFGDMTeIGERGL---------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK13644 92 GRTVEEDLAFGPENLCL--PPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21729876 666 AHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1141-1317 |
2.31e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.83 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS-- 1216
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1217 -KLSVIPQDPVLLSG-TIRFN------LDPFDR-HTDQQIWDALERTFLT-KA--------------------------I 1260
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNvalpleLAGTPKaEIKARVTELLELVGLSdKAdrypaqlsggqkqrvaiaralasnpkV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 1261 ILIDEATASIDMET-----DTL--IQRTIreafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1317
Cdd:PRK11153 162 LLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
527-720 |
2.35e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------------SLAYVPQQAWIVSG-NIREN 591
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMGGAY-DKARYLQvlhccSLNRDLELLPFGDMTEIgERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:PRK11614 101 LAMGGFFaERDQFQE-----RIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21729876 671 HIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 720
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1150-1316 |
3.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1150 YRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKLSVIPQD 1224
Cdd:PRK13637 12 YMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1225 P--VLLSGTI---------RFNLD--------------------------PFDRHTDQQIWDALERTFLTKAIILI-DEA 1266
Cdd:PRK13637 92 PeyQLFEETIekdiafgpiNLGLSeeeienrvkramnivgldyedykdksPFELSGGQKRRVAIAGVVAMEPKILIlDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1267 TASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1316
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1152-1315 |
3.10e-12 |
|
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: 67.51 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPV 1226
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 LLSG-TIRFNLD-------PFDRHTDQQIWDALERTFLTK---------------------------AIILIDEATASID 1271
Cdd:cd03255 93 LLPDlTALENVElplllagVPKKERRERAEELLERVGLGDrlnhypselsggqqqrvaiaralandpKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 1272 METDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1315
Cdd:cd03255 173 SETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1156-1328 |
3.38e-12 |
|
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: 67.85 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGVDICSIGlEDLRSKLSV-----IPQ--- 1223
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIgrtfqIPRlfp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 -----DPVLLSGTIR----FNLDPFDRH---TDQQIWDALERTFLTK---------------------------AIILID 1264
Cdd:cd03219 89 eltvlENVMVAAQARtgsgLLLARARREereARERAEELLERVGLADladrpagelsygqqrrleiaralatdpKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1265 EATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1328
Cdd:cd03219 169 EPAAGLnPEETEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
530-719 |
3.46e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.86 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVP-----------QQAWIVSGNIRENILMGGA 597
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 598 YDKARYLQVLhccslNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC 676
Cdd:PRK11607 118 QDKLPKAEIA-----SRVNEMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21729876 677 IKKTLR-GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK11607 193 VDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1156-1319 |
3.86e-12 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 67.16 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLL------- 1228
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFphltvae 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1229 ------------SGTIR---------FNLDPF-DRHTD-----QQIWDALERTFLTKA-IILIDEATASIDMETDTLIQR 1280
Cdd:cd03259 92 niafglklrgvpKAEIRarvrellelVGLEGLlNRYPHelsggQQQRVALARALAREPsLLLLDEPLSALDAKLREELRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21729876 1281 TIREAF--QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 1319
Cdd:cd03259 172 ELKELQreLGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1156-1322 |
4.38e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIR- 1233
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1234 ---FNLDPFDRH------TDQQIWD-ALERTFLTK---------------------------AIILIDEATASIDMETDT 1276
Cdd:PRK11231 96 lvaYGRSPWLSLwgrlsaEDNARVNqAMEQTRINHladrrltdlsggqrqraflamvlaqdtPVVLLDEPTTYLDINHQV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1277 LIQRTIRE-AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE 1322
Cdd:PRK11231 176 ELMRLMRElNTQGKTVVTVLHD----LNqasryCDHLVVLANGHVMAQGTPE 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1156-1334 |
4.59e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.49 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPvllsgTIRFN 1235
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1236 LD----------P----FDRHTD---QQIWDALERT---------------------FLTKA------IILIDEATASID 1271
Cdd:PRK09536 92 FDvrqvvemgrtPhrsrFDTWTEtdrAAVERAMERTgvaqfadrpvtslsggerqrvLLARAlaqatpVLLLDEPTASLD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1272 M----ETDTLIQRTIREafqGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE-VLrkKPGSLFAA 1334
Cdd:PRK09536 172 InhqvRTLELVRRLVDD---GKTAVAAIHD----LDlaaryCDELVLLADGRVRAAGPPAdVL--TADTLRAA 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1156-1326 |
5.05e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.05 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIgLEDLRSKLSVIPQDPVL---LS- 1229
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLvpnLSv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1230 -------------GTIR----------------FNLDPfdrHT--------DQQIwdaLE--RTFLTKAIILI-DEATAS 1269
Cdd:COG1129 97 aeniflgreprrgGLIDwramrrrarellarlgLDIDP---DTpvgdlsvaQQQL---VEiaRALSRDARVLIlDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1270 I-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EFDRPEVLRK 1326
Cdd:COG1129 171 LtEREVERLFRiiRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVgtgpvaELTEDELVRL 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
527-715 |
5.71e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.57 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG----------------SLAYVPQQA---Wi 583
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGvdltalserelraarrKIGMIFQHFnllS- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 584 vSGNIRENI-----LMGgaYDKARYLQvlhccslnRDLELLpfgDMTEIGERGL----NLSGGQKQRISLARAVYSDRQI 654
Cdd:COG1135 96 -SRTVAENValpleIAG--VPKAEIRK--------RVAELL---ELVGLSDKADaypsQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 655 YLLDDPLSAVDAHVGKHIFE---EcIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGT 715
Cdd:COG1135 162 LLCDEATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVrRICDRVAVLENGRIVEQGP 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
525-712 |
5.81e-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: 67.52 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQA------- 581
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 582 ----WIVSGNIRENILMGGAYDKARYLQVLHCCSL-NRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYL 656
Cdd:TIGR02769 105 mtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLP-----------RQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 657 LDDPLSAVDAHVGKHIFEECIKKTLRGKTV-VLVTHQLQYLE-FCGQIILLENGKICE 712
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQsFCQRVAVMDKGQIVE 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1156-1323 |
6.15e-12 |
|
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: 67.07 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKL---SV---------IPQ 1223
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARARLrarHVgfvfqsfqlLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 ----DPVLLSGTIRFNLDPFDR---------------HTDQQIWD------ALERTFLTK-AIILIDEATASIDMETDTL 1277
Cdd:COG4181 105 ltalENVMLPLELAGRRDARARarallervglghrldHYPAQLSGgeqqrvALARAFATEpAILFADEPTGNLDAATGEQ 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 1278 IQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEV 1323
Cdd:COG4181 185 IIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
494-722 |
7.11e-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: 67.28 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 494 ALELERNGHASEGMTrprdalgpEEEGNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLE---GSVGV 570
Cdd:cd03294 17 AFKLLAKGKSKEEIL--------KKTGQTVG--VNDVSLDVREGEIFVIMGLSGSGKSTLLRCI---NRLIEptsGKVLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 571 QG------------------------SLAYVPQQawivsgNIRENILMGgaydkaryLQVLHCCSLNRD------LELLP 620
Cdd:cd03294 84 DGqdiaamsrkelrelrrkkismvfqSFALLPHR------TVLENVAFG--------LEVQGVPRAEREeraaeaLELVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 621 FGDMTE--IGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYL 696
Cdd:cd03294 150 LEGWEHkyPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlQAELQKTIVFITHDLdEAL 225
|
250 260
....*....|....*....|....*.
gi 21729876 697 EFCGQIILLENGKICENGTHSELMQK 722
Cdd:cd03294 226 RLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
617-719 |
7.38e-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: 66.49 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 617 ELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC--IKKTLrGKTVVLVTH-Q 692
Cdd:cd03300 113 EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrLQKEL-GITFVFVTHdQ 191
|
90 100
....*....|....*....|....*..
gi 21729876 693 LQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:cd03300 192 EEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
530-710 |
8.32e-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: 66.53 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLLEGSVGVQG----------SLAYVPQQAWIVSG-NIRE----- 590
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDILLPGlTVREtltyt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGGAYDKARYLQVLHCCSLNRDLELLPFGdmteiGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:cd03234 106 AILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21729876 671 HIFEECIKKTLRGKTVVLVTHQ--LQYLEFCGQIILLENGKI 710
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1147-1326 |
1.00e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 65.63 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1147 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVDICSIGLEDlRSKLSVI--P 1222
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1223 QDPVLLSGTirfNLDPFDRHTDQ----------QIwdaLERTFLTKAIILIDEATASIDMETDTLIQRTIRE-AFQGCTV 1291
Cdd:cd03217 84 QYPPEIPGV---KNADFLRYVNEgfsggekkrnEI---LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 21729876 1292 LVIAH--RVTTVLNCDHILVMGNGKVVEFDRPEVLRK 1326
Cdd:cd03217 158 LIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1147-1320 |
1.23e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1147 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPV 1226
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 LLSGTIRFNLD-PF----DRHTDQQIWDALER-----TFLTKAI-----------------------ILIDEATASIDME 1273
Cdd:PRK10247 92 LFGDTVYDNLIfPWqirnQQPDPAIFLDDLERfalpdTILTKNIaelsggekqrislirnlqfmpkvLLLDEITSALDES 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 1274 TDT----LIQRTIREafQGCTVLVIAHRVTTVLNCDHILV----MGNGKVVEFDR 1320
Cdd:PRK10247 172 NKHnvneIIHRYVRE--QNIAVLWVTHDKDEINHADKVITlqphAGEMQEARYEL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1141-1315 |
1.29e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 65.63 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKL 1218
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDpvllsgtirFNLDP----FDRHTDQQIW-------DALERT--FLTK----------------------AI--- 1260
Cdd:cd03262 79 GMVFQQ---------FNLFPhltvLENITLAPIKvkgmskaEAEERAleLLEKvgladkadaypaqlsggqqqrvAIara 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1261 -------ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1315
Cdd:cd03262 150 lamnpkvMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1151-1314 |
1.53e-11 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 65.19 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1151 RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG 1230
Cdd:COG4133 12 RGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1231 -TIRFNLDpF------DRHTDQQIWDALE--------------------------RTFLTKA-IILIDEATASIDMETDT 1276
Cdd:COG4133 90 lTVRENLR-FwaalygLRADREAIDEALEavglagladlpvrqlsagqkrrvalaRLLLSPApLWLLDEPFTALDAAGVA 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 21729876 1277 LIQRTIRE-AFQGCTVLVIAHRvTTVLNCDHILVMGNGK 1314
Cdd:COG4133 169 LLAELIAAhLARGGAVLLTTHQ-PLELAAARVLDLGDFK 206
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
527-721 |
1.54e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSG-NIRENI 592
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQLPAAEGmTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMG--------GAYDKARYLQVLHCCSLnrdLELLPFGdmteigERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK10575 107 AIGrypwhgalGRFGAADREKVEEAISL---VGLKPLA------HRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 664 VD-AHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK10575 178 LDiAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1156-1337 |
1.62e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.51 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLR-SKLSVIPQDP----VLLSG 1230
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrgLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1231 TIRFNLDpFDRHTDQQI-------WDALERtfLTKAiiLIDE---ATASIDMETDTL----IQRTI--RE---------A 1285
Cdd:COG3845 352 SVAENLI-LGRYRRPPFsrggfldRKAIRA--FAEE--LIEEfdvRTPGPDTPARSLsggnQQKVIlaRElsrdpklliA 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1286 FQ-----------------------GCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPEVLRKKPGslfaALMA 1337
Cdd:COG3845 427 AQptrgldvgaiefihqrllelrdaGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREEIG----LLMA 499
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1141-1228 |
1.68e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.46 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 1217
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90
....*....|.
gi 21729876 1218 LSVIPQDPVLL 1228
Cdd:COG2884 81 IGVVFQDFRLL 91
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
527-710 |
1.73e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLS--AILEEM---HLLEGSvgvqGSLAyvpqqawivsgNIRENI-LMggaYDK 600
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRllAGLETPsagELLAGT----APLA-----------EAREDTrLM---FQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 601 ARYL---QVLHccslNRDLELLpfGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK11247 90 ARLLpwkKVID----NVGLGLK--GQWRDAALQALAavgladranewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21729876 664 VDAhVGKHIFEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKI 710
Cdd:PRK11247 164 LDA-LTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
527-708 |
1.86e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEemhlL----EGSVGV--QGSLAYVPQQAWIVSGNIRENIL---MGGA 597
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLypaTAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 598 YDKARYLQVLHCCSLNRdleLLPfgDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcI 677
Cdd:COG4178 455 FSDAELREALEAVGLGH---LAE--RLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-L 528
|
170 180 190
....*....|....*....|....*....|.
gi 21729876 678 KKTLRGKTVVLVTHQLQYLEFCGQIILLENG 708
Cdd:COG4178 529 REELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
808-1064 |
1.88e-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: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 808 IIFFFVVLIVFLTIFSFWWLsywleqGSGTN--SSRESNGTMADLGNIAdnPQLSFYQLVYGLNALLLICVGVcssgIFT 885
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLL------GKAIDliIEGLGGGGGVDFSGLL--RILLLLLGLYLLSALFSYLQNR----LMA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 886 KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ-LLPIFSeQFLVLSLMVIAVLLIVSVLSPYILL 964
Cdd:cd18547 71 RVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQaLSQSLT-QLISSILTIVGTLIMMLYISPLLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 965 MGAIIMVICFIYYMMF-KKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA--QNNYLLLFLS 1041
Cdd:cd18547 150 IVLVTVPLSLLVTKFIaKRSQKYFRKQQK-ALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEElyKASFKAQFYS 228
|
250 260
....*....|....*....|...
gi 21729876 1042 STRWMALRLeiMTNLVTLAVALF 1064
Cdd:cd18547 229 GLLMPIMNF--INNLGYVLVAVV 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
527-714 |
1.99e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWI-VSGNIRENI 592
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMGgaydkarylqvlhccslnRDLELLPFGDMTEIGERGL------------------NLSGGQKQRISLARAVYSDRQI 654
Cdd:PRK09536 99 EMG------------------RTPHRSRFDTWTETDRAAVeramertgvaqfadrpvtSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 655 YLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENG 714
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
527-719 |
2.04e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGV--------------QGSLAYVPQQAWIVSGNI 588
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeaGTIRVgditidtarslsqqKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 R--------ENILMGGAYDKarylQVLHCCSLNRDLELLpfgdmTEIGERG------LNLSGGQKQRISLARAVYSDRQI 654
Cdd:PRK11264 95 NlfphrtvlENIIEGPVIVK----GEPKEEATARARELL-----AKVGLAGketsypRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 655 YLLDDPLSAVDAH-VGKhifeecIKKTLRG-----KTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:PRK11264 166 ILFDEPTSALDPElVGE------VLNTIRQlaqekRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
526-720 |
2.31e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 526 ELHK----------INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQGS-------------------- 573
Cdd:PRK10619 10 DLHKrygehevlkgVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPS--EGSIVVNGQtinlvrdkdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 574 ------LAYVPQQAWIVSG-NIRENILMGGaydkaryLQVLHCCSLNRDLELLPFGDMTEIGERG-----LNLSGGQKQR 641
Cdd:PRK10619 88 rllrtrLTMVFQHFNLWSHmTVLENVMEAP-------IQVLGLSKQEARERAVKYLAKVGIDERAqgkypVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 642 ISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELM 720
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFArHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
527-822 |
2.83e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSL----------------AYVPQQ-AWIVSGNIR 589
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFRSPKGVKGSGSVllngmpidakemraisAYVQQDdLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENIL------MGGAYDK----ARYLQVLhccslnRDLELLPFGDmTEIGERGL--NLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:TIGR00955 118 EHLMfqahlrMPRRVTKkekrERVDEVL------QALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 658 DDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFC--GQIILLENGKICENGTHSELMQKKGKYAQLIQKMHK 735
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 736 EAtsDMLQDTAKIAEKPKVESQA-------------LATSLEESLNGNAVPEHQLTQEEEMEEGSlswrvyhhyiqaagG 802
Cdd:TIGR00955 271 PA--DFYVQVLAVIPGSENESREriekicdsfavsdIGRDMLVNTNLWSGKAGGLVKDSENMEGI--------------G 334
|
330 340
....*....|....*....|.
gi 21729876 803 YMVSCIIFFFVVLI-VFLTIF 822
Cdd:TIGR00955 335 YNASWWTQFYALLKrSWLSVL 355
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1144-1322 |
2.92e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.81 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1144 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 1223
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 DP--VLLSGTIR----FNLD----PFDRHTdQQIWDALERT----FLTKA-----------------------IILIDEA 1266
Cdd:PRK13635 89 NPdnQFVGATVQddvaFGLEnigvPREEMV-ERVDQALRQVgmedFLNREphrlsggqkqrvaiagvlalqpdIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1267 TASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 1322
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
527-721 |
2.99e-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: 65.00 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL----------------------EEMHLLEGSVGV--QGSlayvpqqAW 582
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIgllrpdsgeilvdgqditglseKELYELRRRIGMlfQGG-------AL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 583 IVSGNIRENI----LMGGAYDKA----RYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQI 654
Cdd:COG1127 94 FDSLTVFENVafplREHTDLSEAeireLVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 655 YLLDDPLSAVDAhVGKHIFEECIKKtLR---GKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG1127 163 LLYDEPTAGLDP-ITSAVIDELIRE-LRdelGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
527-719 |
3.72e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.07 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSG-NIRENILMG---------- 595
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVGMVfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 GAYDKARYLQVLHCCSLNRDLE------LLPFGDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKkiveecLRKVGLWKEVYDR-LNspasqLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 665 DAhVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:PRK14246 185 DI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
525-723 |
3.82e-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: 65.14 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEmhlLEGSVGVQGSLAYVPQQAWivsgNIRENILMggaydka 601
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLLP---TSGKVTVDGLDTLDEENLW----EIRKKVGM------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 602 rYLQvlhccslNRD---------------LELL--PFGDMTEIGERGL--------------NLSGGQKQRISLARAVYS 650
Cdd:TIGR04520 82 -VFQ-------NPDnqfvgatveddvafgLENLgvPREEMRKRVDEALklvgmedfrdrephLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 651 DRQIYLLDDPLSAVDAhVGKhifEEcIKKTLR------GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKK 723
Cdd:TIGR04520 154 RPDIIILDEATSMLDP-KGR---KE-VLETIRklnkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
577-731 |
3.84e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 577 VPQQAWIVSGNIRENILMGGayDKARYLQVLHCC---SLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQ 653
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 654 IYLLDDPLSAVDAHVgkhifEECIKKTL------RGKTVVLVTHQLQYLEFCGQIILLEN----GKICE-NGTHSELMQ- 721
Cdd:PTZ00265 1379 ILLLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSv 1453
|
170
....*....|
gi 21729876 722 KKGKYAQLIQ 731
Cdd:PTZ00265 1454 QDGVYKKYVK 1463
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1157-1318 |
4.38e-11 |
|
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: 63.75 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIrGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG-TIRFN 1235
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1236 LDPF-------DRHTDQQIWDALE---------------------RTFLTKA------IILIDEATASIDMETDTLIQRT 1281
Cdd:cd03264 93 LDYIawlkgipSKEVKARVDEVLElvnlgdrakkkigslsggmrrRVGIAQAlvgdpsILIVDEPTAGLDPEERIRFRNL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 21729876 1282 IREAFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEF 1318
Cdd:cd03264 173 LSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
525-710 |
4.85e-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: 63.97 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG---------SLAYVPQQAWIV--------SGN 587
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGVVfqdfrllpDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENIL--MGGAYDKARYLQ-----VLHCCSLNRDLELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:cd03292 95 VYENVAfaLEVTGVPPREIRkrvpaALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21729876 661 LSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1141-1316 |
4.93e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNT----PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLR 1215
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1216 SKLSVIPQDP------VLLSGTIRF---NLDPFDRHTDQQIWDALERTFLTK-----------------AI--------- 1260
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEyrrhaphllsggqkqrvAIagilamrpe 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1261 -ILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVV 1316
Cdd:PRK13633 165 cIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
541-720 |
5.34e-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: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 541 GVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQG-----------------SLAYVPQQAwiv-sgNIRENILMG----- 595
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIagLE--RPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEArlfphlSVRGNLLYGrkrap 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 GAYDKARYLQVLhccslnrdlELLpfgdmtEIG---ERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKH 671
Cdd:COG4148 107 RAERRISFDEVV---------ELL------GIGhllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR-KA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 672 ifeECIK--KTLRGKT---VVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELM 720
Cdd:COG4148 171 ---EILPylERLRDELdipILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
529-723 |
5.65e-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: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 529 KINLVVSKGMMLGVCGNTGSGKSSLLSAI------------LEEMHLLEGSVGVQGS-----LAYVPQQAWIVSG-NIRE 590
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIagltrpdegeivLNGRTLFDSRKGIFLPpekrrIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGGAYDKARYLQVlhccSLNRDLELLPFGDMTEIGERglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:TIGR02142 95 NLRYGMKRARPSERRI----SFERVIELLGIGHLLGRLPG--RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 671 HI--FEECIKKTLRgKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKK 723
Cdd:TIGR02142 169 EIlpYLERLHAEFG-IPILYVSHSLQEVLrLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
527-718 |
7.01e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.59 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG---------SLAYVPQQ-AWI--------- 583
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGqdltalsekELRKARRQiGMIfqhfnllss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 584 --VSGNI----------RENIlmggaydKARYLqvlhccslnrdlELLpfgDMTEIGERGL----NLSGGQKQRISLARA 647
Cdd:PRK11153 97 rtVFDNValplelagtpKAEI-------KARVT------------ELL---ELVGLSDKADrypaQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 648 VYSDRQIYLLDDPLSAVDAHVGKHIFE--ECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSE 718
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSE 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
527-694 |
7.44e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.29 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAiLEEMHLLEGSVGVQGSLAY---------------------VPQQAwivs 585
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLIPGARVEGEILLdgediydpdvdvvelrrrvgmVFQKP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 586 gN-----IRENILMG----GAYDKArylqvlhccslnrdlellpfgDMTEIGER------------------GLNLSGGQ 638
Cdd:COG1117 102 -NpfpksIYDNVAYGlrlhGIKSKS---------------------ELDEIVEEslrkaalwdevkdrlkksALGLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 639 KQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKtLRGK-TVVLVTHQLQ 694
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EELILE-LKKDyTIVIVTHNMQ 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
634-710 |
7.51e-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: 62.06 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQLQ-YLEFCGQIILLENGKI 710
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaqGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
633-715 |
7.65e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.74 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 633 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGK 709
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNE-LKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGR 222
|
....*.
gi 21729876 710 ICENGT 715
Cdd:PRK09452 223 IEQDGT 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
537-692 |
7.93e-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: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 537 GMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSlaYVPQQAwivsGNIRENIL-------MGGAYDKARYLQVLHc 609
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT--PLAEQR----DEPHENILylghlpgLKPELSALENLHFWA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 610 cSLNRDLELLPFGDMTEIGERGLN------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-R 682
Cdd:TIGR01189 99 -AIHGGAQRTIEDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLaR 176
|
170
....*....|
gi 21729876 683 GKTVVLVTHQ 692
Cdd:TIGR01189 177 GGIVLLTTHQ 186
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
527-710 |
1.13e-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: 63.22 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLS--AILEemHLLEGSVGVQG-----------------SLAYVpQQAW--IVS 585
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGllAGLD--RPTSGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 586 GNIRENILMggaydkarylqvlhccslnrDLELLPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSD 651
Cdd:COG4181 105 LTALENVML--------------------PLELAGRRDARARARALLErvglghrldhypaqLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 652 RQIYLLDDPLSAVDAHVGKHI----FEecIKKTlRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
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 ... |
527-709 |
1.15e-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: 60.93 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV--GVQGSLAYVPQqawivsgnirenilmggaydkaryl 604
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtwGSTVKIGYFEQ------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 605 qvlhccslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKtLRGk 684
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-YPG- 118
|
170 180
....*....|....*....|....*.
gi 21729876 685 TVVLVTHQLQYL-EFCGQIILLENGK 709
Cdd:cd03221 119 TVILVSHDRYFLdQVATKIIELEDGK 144
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
527-719 |
1.43e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.09 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG---------------SLAYVPQQAwivsgN-- 587
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGedltdskkdinklrrKVGMVFQQF-----Nlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 ----IRENILMGGaydkaryLQVLHccsLNRD------LELLpfgdmteigER-GL---------NLSGGQKQRISLARA 647
Cdd:COG1126 90 phltVLENVTLAP-------IKVKK---MSKAeaeeraMELL---------ERvGLadkadaypaQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 648 VYSDRQIYLLDDPLSAVDAhvgkhifeECIK------KTL--RGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSE 718
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDP--------ELVGevldvmRDLakEGMTMVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEE 222
|
.
gi 21729876 719 L 719
Cdd:COG1126 223 F 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
527-720 |
1.57e-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: 62.69 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQGS--------------LAYVPQQAWIVSG-NI 588
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAI---SGLLpprSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENILMGgAY---DKARYLQVLHccslnRDLELLPfgdmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDP- 660
Cdd:COG0410 96 EENLLLG-AYarrDRAEVRADLE-----RVYELFP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPs 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 661 --LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELM 720
Cdd:COG0410 165 lgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELL 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
534-716 |
2.65e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 534 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLayVPQQAWIVSG---------------NIRENILMGGay 598
Cdd:PRK13537 30 VQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP--VPSRARHARQrvgvvpqfdnldpdfTVRENLLVFG-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 dkaRYLQVLHCCSLNRDLELLPFGDMTEIGE-RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECI 677
Cdd:PRK13537 106 ---RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21729876 678 KKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KICENGTH 716
Cdd:PRK13537 182 RSLLaRGKTILLTTHFMEEAErLCDRLCVIEEGrKIAEGAPH 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1158-1323 |
2.75e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLgM-ALFRLVEPMAGRILIDG--VDICS--------IG--------------LE 1212
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSprdaialgIGmvhqhfmlvpnltvAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1213 DL-----RSKLSVIPQDPVL-----LSGTIRFNLDPfdrhtDQQIWD-------ALE--RTFLTKAIILI-DEATASI-D 1271
Cdd:COG3845 100 NIvlglePTKGGRLDRKAARarireLSERYGLDVDP-----DAKVEDlsvgeqqRVEilKALYRGARILIlDEPTAVLtP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1272 METDTLIqRTIRE-AFQGCTVLVIAHR---VTTVlnCDHILVMGNGKVV-EFDRPEV 1323
Cdd:COG3845 175 QEADELF-EILRRlAAEGKSIIFITHKlreVMAI--ADRVTVLRRGKVVgTVDTAET 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
527-694 |
3.05e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIlEEMHLLEGSVGVQGSLAY---------------------VPQQAWIVS 585
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 586 GNIRENILMG----GAYDKARYLQVLHccslnRDLELLPFGDmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK14239 100 MSIYENVVYGlrlkGIKDKQVLDEAVE-----KSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 21729876 658 DDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 694
Cdd:PRK14239 173 DEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1141-1316 |
3.19e-10 |
|
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: 61.61 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdLRSKL 1218
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1219 SVIPQDPVLLSG-TIRFNLDPFDR---------------------------------HTDQQIWDALERTFL-TKAIILI 1263
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGlyglkgdeltarleeladrlgmeelldrrvggfSTGMRQKVAIARALVhDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1264 DEATASID-METDTLIQ--RTIREAfqGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1316
Cdd:cd03266 161 DEPTTGLDvMATRALREfiRQLRAL--GKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
522-710 |
3.22e-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: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 522 SLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVP----QQAWI 583
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 584 VSGNIRENILMGgaydkarylqvlhccSLnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:cd03215 91 LDLSVAENIALS---------------SL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21729876 664 VDahVG--KHIFEECIKKTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKI 710
Cdd:cd03215 135 VD--VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
530-692 |
4.61e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------SLAYV-PQQAWIVSGNIRENILMGGAY 598
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 DKARYLQVLHC-CSLN-RDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEEC 676
Cdd:PRK13539 101 LGGEELDIAAAlEAVGlAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAEL 169
|
170
....*....|....*..
gi 21729876 677 IKKTL-RGKTVVLVTHQ 692
Cdd:PRK13539 170 IRAHLaQGGIVIAATHI 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
528-692 |
4.82e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 528 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-----NIRE 590
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTEltaleNLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGGAYDKARYLQVLHCCSLnRDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH--- 667
Cdd:PRK13538 98 YQRLHGPGDDEALWEALAQVGL-AGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgva 166
|
170 180
....*....|....*....|....*
gi 21729876 668 VGKHIFEECIKktlRGKTVVLVTHQ 692
Cdd:PRK13538 167 RLEALLAQHAE---QGGMVILTTHQ 188
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
527-732 |
4.99e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.97 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLL-------EGSVGVQG---------SLA--------YVPQQAW 582
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTL-------MNILgcldkptSGTYRVAGqdvatldadALAqlrrehfgFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 583 IVS-----GNIRENILMGGAYDKARylqvlhccsLNRDLELLP-FGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYL 656
Cdd:PRK10535 97 LLShltaaQNVEVPAVYAGLERKQR---------LLRAQELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 657 LDDPLSAVDAHVGKHIFeeCIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRdrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNT 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
527-720 |
5.88e-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: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEG-SVGVQG-------------SLAYV-PQQAWIVSGNIR-E 590
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggedvwelrkRIGLVsPALQLRFPRDETvL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGGAYD--------------KARYLqvlhccslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIY 655
Cdd:COG1119 99 DVVLSGFFDsiglyreptdeqreRAREL-----------LELL---GLAHLADRPFGtLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 656 LLDDPLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELM 720
Cdd:COG1119 165 ILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
519-692 |
6.47e-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: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 519 EGNSLGPELhkiNLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHLLEG---SVGVQGSLAYVPQQAWIVSGNIRENIL-- 593
Cdd:TIGR00954 463 NGDVLIESL---SFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIyp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 594 -------MGGAYDK--ARYLQVLHCCS-LNRDLELLPFGDMTEIgerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:TIGR00954 539 dssedmkRRGLSDKdlEQILDNVQLTHiLEREGGWSAVQDWMDV------LSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 21729876 664 VDAHVGKHIFEECIKKtlrGKTVVLVTHQ 692
Cdd:TIGR00954 613 VSVDVEGYMYRLCREF---GITLFSVSHR 638
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
512-692 |
6.80e-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: 60.20 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 512 DALGPEEEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpQQAWIVSGNIREN 591
Cdd:cd03231 4 DELTCERDGRAL---FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMGGAYD--KARY-----LQVLHC-CSLNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03231 75 LLYLGHAPgiKTTLsvlenLRFWHAdHSDEQVEEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|
gi 21729876 663 AVDAHVGKHIFEECIKKTLRGKTVVLVTHQ 692
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
527-722 |
6.90e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVqGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQV 606
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 607 lhccSLNRDLELLP--FGDMTEIGER---------GLN----------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK13643 101 ----TVLKDVAFGPqnFGIPKEKAEKiaaeklemvGLAdefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 666 --AHVGKHIFEECIKKTlrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13643 177 pkARIEMMQLFESIHQS--GQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1156-1310 |
7.10e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFR------------LVEPMAGRILidgvdicsigledlrsklsVIPQ 1223
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTL----LRaiaglwpygsgrIARPAGARVL-------------------FLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 DPVLLSGTIRFNL---DPFDRHTDQQIWDALE--------------------------------RTFLTK-AIILIDEAT 1267
Cdd:COG4178 434 RPYLPLGTLREALlypATAEAFSDAELREALEavglghlaerldeeadwdqvlslgeqqrlafaRLLLHKpDWLFLDEAT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21729876 1268 ASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVM 1310
Cdd:COG4178 514 SALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1145-1333 |
7.96e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1145 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 1222
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1223 QDP------VLLSGTIRF---NLDPFDRHTDQQIWDAL---------------------ERTFLTKAII------LIDEA 1266
Cdd:PRK13638 84 QDPeqqifyTDIDSDIAFslrNLGVPEAEITRRVDEALtlvdaqhfrhqpiqclshgqkKRVAIAGALVlqarylLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1267 TASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDrpevlrkKPGSLFA 1333
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG-------APGEVFA 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
527-753 |
8.53e-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: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLLEGS----------------------VGVQ-----------GS 573
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVL-------MHVLRGMdqyeptsgriiyhvalcekcgyVERPskvgepcpvcgGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 574 LAYVPQQAWIVSGNIRENILMGGA---------YDKARYLQ-VLHCC---------SLNRDLELLpfgDMTEIGER---- 630
Cdd:TIGR03269 89 LEPEEVDFWNLSDKLRRRIRKRIAimlqrtfalYGDDTVLDnVLEALeeigyegkeAVGRAVDLI---EMVQLSHRithi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQLQYLE-FCGQIILLE 706
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEdLSDKAIWLE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 21729876 707 NGKICENGTHSELMQkkgKYAQLIQKMHKEATSDMLQDTAKIAEKPK 753
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
525-691 |
8.69e-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: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQ----AWIvsgNIRENI 592
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvtgpgaDRGVVFQKdallPWL---NVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMG----GAyDKARYLQvlhccslnRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:COG4525 98 AFGlrlrGV-PKAERRA--------RAEELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180
....*....|....*....|....*..
gi 21729876 668 VGKHIFE---ECIKKTlrGKTVVLVTH 691
Cdd:COG4525 169 TREQMQElllDVWQRT--GKGVFLITH 193
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1141-1331 |
9.29e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDP--VLLSGTIRF--------NLDPFD---RHTDQQIWDA--LERT---------------------FLTKAIILID 1264
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYdvafglenHAVPYDemhRRVSEALKQVdmLERAdyepnalsggqkqrvaiagvlALNPSVIILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1265 EATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSL 1331
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
520-694 |
9.50e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.95 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 520 GNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAI-----LEEMHLLEGSVGVQGSLAYVPQqawIVSGNIRENILM 594
Cdd:PRK14243 21 GSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPD---VDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 ----GGAYDKARYLQVLHCCSLNRDLellpfGDMTEIGER------------------GLNLSGGQKQRISLARAVYSDR 652
Cdd:PRK14243 96 vfqkPNPFPKSIYDNIAYGARINGYK-----GDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21729876 653 QIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 694
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQ 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
530-714 |
1.01e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 60.07 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAW----IVSGN--------IRENIlmgg 596
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlgFVSDStglydrltARENL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 597 aydkaRYLQVLHccSLNRDL------ELLPFGDMTEIGE-RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03266 100 -----EYFAGLY--GLKGDEltarleELADRLGMEELLDrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 670 KHIFEecIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENG 714
Cdd:cd03266 173 RALRE--FIRQLRalGKCILFSTHIMQEVErLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1157-1334 |
1.17e-09 |
|
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: 60.04 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLLSG-TIRFN 1235
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1236 LDPFDRH-------TDQQIWD--------------------------ALERTFLTK-AIILIDEATASIDMET-DTLIQ- 1279
Cdd:cd03299 92 IAYGLKKrkvdkkeIERKVLEiaemlgidhllnrkpetlsggeqqrvAIARALVVNpKILLLDEPFSALDVRTkEKLREe 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1280 -RTIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1334
Cdd:cd03299 172 lKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
527-712 |
1.23e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsAILE--------EMHLL---------EGSVGVQG-SLAYVPQQAWIV-SGN 587
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLL-AILAglddgssgEVSLVgqplhqmdeEARAKLRAkHVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENI----LMGGAYD---KARYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:PRK10584 105 ALENVelpaLLRGESSrqsRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21729876 661 LSAVDAHVGKHIFEECIKKTLR-GKTVVLVTHQLQYLEFCGQIILLENGKICE 712
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
527-710 |
1.45e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--SLAYVPQQAWIVSGN-IRENILMGgaydKARY 603
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDLtVLDTVLDG----DAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 604 LQVLHccSLNRDLELLPFGD-----MTEIGER------------------GL------------NLSGGQKQRISLARAV 648
Cdd:COG0488 90 RALEA--ELEELEAKLAEPDedlerLAELQEEfealggweaearaeeilsGLgfpeedldrpvsELSGGWRRRVALARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 649 YSDRQIYLLDDP-----LSAVDAhvgkhiFEECIKKtlRGKTVVLVTHQLQYL-EFCGQIILLENGKI 710
Cdd:COG0488 168 LSEPDLLLLDEPtnhldLESIEW------LEEFLKN--YPGTVLVVSHDRYFLdRVATRILELDRGKL 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
633-719 |
1.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 633 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKIC 711
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKII 244
|
....*....
gi 21729876 712 ENG-THSEL 719
Cdd:PRK13651 245 KDGdTYDIL 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
527-708 |
1.90e-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: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVP-QQAWIVSGN--------IRENIlmgga 597
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRMVVFQNysllpwltVRENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 598 ydkarYLQVlhccslNRDLELLPFGDMTEIGERGLNL--------------SGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:TIGR01184 76 -----ALAV------DRVLPDLSKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 664 VDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENG 708
Cdd:TIGR01184 145 LDALTRGNLQEELMQiWEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1156-1322 |
2.19e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvDICSIgLE---DLRSKLSVIpqDPVLLSGTI 1232
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL-LElgaGFHPELTGR--ENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1233 R-FNLDPFDRHTDQ-----QIWDALER------------------TFLTKAIILIDEATASIDmetdtliqrtirEAFQ- 1287
Cdd:COG1134 116 LgLSRKEIDEKFDEivefaELGDFIDQpvktyssgmrarlafavaTAVDPDILLVDEVLAVGD------------AAFQk 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 1288 ------------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1322
Cdd:COG1134 184 kclarirelresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPE 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
525-857 |
2.39e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIREN 591
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILM-----GGAYDKARylqvlhccsLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:TIGR01257 1024 ILFyaqlkGRSWEEAQ---------LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 667 HVGKHIFEECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ--KKGKYAQLIQKMHK-EATSDML 742
Cdd:TIGR01257 1095 YSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGdRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVRKMKNiQSQRGGC 1173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 743 QDTAKIAEK---PKVESQALATSLEESLNGNAvpehqltqEEEMEegslswRVYHHYIQAAggyMVSCIiffFVVLIVFL 819
Cdd:TIGR01257 1174 EGTCSCTSKgfsTRCPARVDEITPEQVLDGDV--------NELMD------LVYHHVPEAK---LVECI---GQELIFLL 1233
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 21729876 820 TIFSFwwlsywlEQGSGTNSSRESNGTMADLG----NIADNP 857
Cdd:TIGR01257 1234 PNKNF-------KQRAYASLFRELEETLADLGlssfGISDTP 1268
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1162-1330 |
2.79e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.82 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1162 NLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS----KLSVIPQDPVLLSGTIRFNLD 1237
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1238 PFD--------RHTDQQIWDAL---------------------ERTFLTKA------IILIDEATASIDMETDTLIQRTI 1282
Cdd:PRK10070 128 AFGmelaginaEERREKALDALrqvglenyahsypdelsggmrQRVGLARAlainpdILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1283 --REAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGS 1330
Cdd:PRK10070 208 vkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
527-723 |
3.65e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileeMHL------LEGSVGVQGSLAYVPQQAWI---------------VS 585
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLL------LHLngiylpQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 586 GNIRENILMGGAYDKARYLQVLhccslNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVE-----RRVEEALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 665 DAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQKK 723
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1156-1314 |
4.49e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 56.30 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLvepMAGRILIDGVDICSIGledlRSKLSVIPQdpvlLSG--TIR 1233
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKST----LLKL---IAGELEPDEGIVTWGS----TVKIGYFEQ----LSGgeKMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1234 FnldpfdrhtdqqiwdALERTFLTKA-IILIDEATASIDMETDTLIQRTIREaFQGcTVLVIAH------RVttvlnCDH 1306
Cdd:cd03221 79 L---------------ALAKLLLENPnLLLLDEPTNHLDLESIEALEEALKE-YPG-TVILVSHdryfldQV-----ATK 136
|
....*...
gi 21729876 1307 ILVMGNGK 1314
Cdd:cd03221 137 IIELEDGK 144
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1145-1326 |
5.78e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1145 DYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 1222
Cdd:PRK13639 6 DLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1223 QDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERT----FLTKA-----------------------IILIDEA 1266
Cdd:PRK13639 85 QNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVgmegFENKPphhlsggqkkrvaiagilamkpeIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1267 TASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE-------FDRPEVLRK 1326
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNkEGITIIISTHDVDLVpVYADKVYVMSDGKIIKegtpkevFSDIETIRK 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1156-1319 |
6.29e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRL----VEPMAGRILIdGVDIcSIG-----LEDLRSKLSVI----- 1221
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVLdelrd 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1222 --PQDPVLLSGTI--RFNLDPfDRHtDQQIWD---------ALERTFLTKAIILI-DEATASIDMETDTLIQRTIREaFQ 1287
Cdd:COG0488 403 gaPGGTEQEVRGYlgRFLFSG-DDA-FKPVGVlsggekarlALAKLLLSPPNVLLlDEPTNHLDIETLEALEEALDD-FP 479
|
170 180 190
....*....|....*....|....*....|....*...
gi 21729876 1288 GcTVLVIAH------RVttvlnCDHILVMGNGKVVEFD 1319
Cdd:COG0488 480 G-TVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
897-1068 |
7.46e-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: 58.55 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 897 NKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLlpiFSEQFLVL---SLMVIAVLLIVSVLSPYILLMGAIIMVIC 973
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNEL---FTSGLVTLigdLLLLIGILIAMFLLNWRLALISLLVLPLL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 974 FIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIM 1053
Cdd:cd18544 155 LLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQE---YRKANLKSIKLFALFRPLV 231
|
170
....*....|....*
gi 21729876 1054 TNLVTLAVALFVAFG 1068
Cdd:cd18544 232 ELLSSLALALVLWYG 246
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1158-1328 |
8.47e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.04 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPVLLSG-TI 1232
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1233 RFN---------LDPFDRHtdQQIWDALE---------------------RTFLTKA------IILIDEATASIdmetDT 1276
Cdd:cd03294 120 LENvafglevqgVPRAERE--ERAAEALElvglegwehkypdelsggmqqRVGLARAlavdpdILLMDEAFSAL----DP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1277 LIQRTIREAF------QGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKP 1328
Cdd:cd03294 194 LIRREMQDELlrlqaeLQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
527-719 |
8.92e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.16 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL----------------------EEMHLLEGSVGV--QGSLAYV-PQQA 581
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVglespsqgnvswrgeplaklnrAQRKAFRRDIQMvfQDSISAVnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 582 --WIVSGNIRENILMGGAYDKARYLQVLHCCSLnrDLELLpfgdmteiGERGLNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK10419 108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDL--DDSVL--------DKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 660 PLSAVDAHVGKHIFEecIKKTLR---GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSEL 719
Cdd:PRK10419 178 AVSNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVErFCQRVMVMDNGQIVETQPVGDK 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
527-729 |
1.04e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSaileemHL------LEGSVGV----------QGSLAYVPQQAWIV------ 584
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQ------HLngllqpTSGTVTIgervitagkkNKKLKPLRKKVGIVfqfpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 585 ---SGNIRENILMG---------GAYDKARYLqvLHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSD 651
Cdd:PRK13634 97 qlfEETVEKDICFGpmnfgvseeDAKQKAREM--IELVGLPEElLARSPF-----------ELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 652 RQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQL----QYLEfcgQIILLENGKICENGTHSELMQKKG 724
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMmemFYKLHKE--KGLTTVLVTHSMedaaRYAD---QIVVMHKGTVFLQGTPREIFADPD 238
|
....*
gi 21729876 725 KYAQL 729
Cdd:PRK13634 239 ELEAI 243
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1161-1317 |
1.08e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICsIGLEDLRS-KLSVIPQDPV-----------LL 1228
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqrisqIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1229 SGTIRFN--LDPFDRhtDQQIWDAL----------------------ERTFLTKAIIL------IDEATASIDMETDTLI 1278
Cdd:PRK15112 111 DFPLRLNtdLEPEQR--EKQIIETLrqvgllpdhasyyphmlapgqkQRLGLARALILrpkviiADEALASLDMSMRSQL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21729876 1279 QRTIRE--AFQGCT-VLVIAHRVTTVLNCDHILVMGNGKVVE 1317
Cdd:PRK15112 189 INLMLElqEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1156-1340 |
1.47e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGV----------DIC------------SI 1209
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEdvthrsiqqrDICmvfqsyalfphmSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1210 GlEDLRSKLSVIPQDPVLLSGTIR-----FNLDPF-DRHTDQ-----QIWDALERTFLTK-AIILIDEATASIDMETDTL 1277
Cdd:PRK11432 96 G-ENVGYGLKMLGVPKEERKQRVKealelVDLAGFeDRYVDQisggqQQRVALARALILKpKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1278 IQRTIREAFQ--GCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGSLF-AALMATAT 1340
Cdd:PRK11432 175 MREKIRELQQqfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQPASRFmASFMGDAN 241
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
527-729 |
1.50e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------SLAYVPQQAWIV---------SGN 587
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkYIRPVRKRIGMVfqfpesqlfEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENILMGGA-------YDKARYLQVLHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK13646 103 VEREIIFGPKnfkmnldEVKNYAHRLLMDLGFSRDvMSQSPF-----------QMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 660 PLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQL----QYLEfcgQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:PRK13646 172 PTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnevaRYAD---EVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
868-1068 |
1.50e-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: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 868 LNALLLICVGVCSS----GIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLP 935
Cdd:cd18552 35 LEALLLVPLAIIGLfllrGLASylqtylmaYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 936 IFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVF-KRLENYSR------SPLFSHILNSLQG 1008
Cdd:cd18552 115 SALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL-------PIRRIgKRLRKISRrsqesmGDLTSVLQETLSG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1009 LSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18552 188 IRVVKAFGAEDYEIKRFRKANE---RLRRLSMKIARARALSSPLMELLGAIAIALVLWYG 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
525-722 |
1.52e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMHLLEGSVGVQGsLAYVPQQAWivsgNIRE----------N 591
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVW----DIREkvgivfqnpdN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMGGAY--DKARYLQvlhccslNRDLellPFGDMTEIGERGL--------------NLSGGQKQRISLARAVYSDRQIY 655
Cdd:PRK13640 96 QFVGATVgdDVAFGLE-------NRAV---PRPEMIKIVRDVLadvgmldyidsepaNLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 656 LLDDPLSAVDAHvGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13640 166 ILDESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
517-720 |
1.64e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.51 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 517 EEEGNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 596
Cdd:PRK10070 36 EKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 597 AYDKARYLQVLHCCSLNRDLELLPFGDMTE-----IGERGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAGINAEERREkaldaLRQVGLEnyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 663 AVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 720
Cdd:PRK10070 194 ALDPLIRTEMQDELVKlQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
527-751 |
2.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.33 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLS-----AILEEMHLLEGSVGVQGSLAYVPQ---------------QAWIVSG 586
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQltnglIISETGQTIVGDYAIPANLKKIKEvkrlrkeiglvfqfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 587 NIRENILMG----GAYDKARYLQV---LHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLD 658
Cdd:PRK13645 107 TIEKDIAFGpvnlGENKQEAYKKVpelLKLVQLPEDyVKRSPF-----------ELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 659 DPLSAVDAHVGK---HIFEECIKKtlRGKTVVLVTHQL-QYLEFCGQIILLENGKICENG------THSELMQK----KG 724
Cdd:PRK13645 176 EPTGGLDPKGEEdfiNLFERLNKE--YKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGspfeifSNQELLTKieidPP 253
|
250 260
....*....|....*....|....*..
gi 21729876 725 KYAQLIQKMhKEATSDMLQDTAKIAEK 751
Cdd:PRK13645 254 KLYQLMYKL-KNKGIDLLNKNIRTIEE 279
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
616-719 |
2.17e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 616 LELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLR-GKTVVLVTHQL- 693
Cdd:PRK13631 170 LERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMe 237
|
90 100
....*....|....*....|....*.
gi 21729876 694 QYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK13631 238 HVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
509-736 |
2.35e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.75 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 509 RPRDALGPEEEGNSLGPeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIvSGNI 588
Cdd:PRK13546 23 RMKDALIPKHKNKTFFA-LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 R--ENI-----LMGGAYDKARYLQVlhccslnrdlELLPFGDMTE-IGERGLNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:PRK13546 101 TgiENIefkmlCMGFKRKEIKAMTP----------KIIEFSELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 661 LSavdahVGKHIF-EECIKKTL----RGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMH 734
Cdd:PRK13546 171 LS-----VGDQTFaQKCLDKIYefkeQNKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKS 245
|
..
gi 21729876 735 KE 736
Cdd:PRK13546 246 KA 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
527-693 |
2.97e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAiLEEMHLLEGSVGVQGSLAYVPQQAWIVSGNI------------RENILM 594
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsmvhpKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 GGAYDKARYlqVLHCCSLNRDLEL-------LPFGDM-----TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:PRK14258 102 MSVYDNVAY--GVKIVGWRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190
....*....|....*....|....*....|..
gi 21729876 663 AVDAHVGKHIFEECIKKTLRGK-TVVLVTHQL 693
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1146-1322 |
3.42e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 55.63 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1146 YHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLeDLRSKLSVI--PQ 1223
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGylPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 DPVLLSG-TIRFNLD------PFDRHTDQQIWDAL----------------------ERTFLTKA------IILIDEATA 1268
Cdd:cd03218 83 EASIFRKlTVEENILavleirGLSKKEREEKLEELleefhithlrkskasslsggerRRVEIARAlatnpkFLLLDEPFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 1269 SIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1322
Cdd:cd03218 163 GVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPE 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1149-1324 |
3.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1149 KYRDNT--PTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 1225
Cdd:PRK13650 13 KYKEDQekYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1226 -----VLLSGTIRFNLD----PFDRhTDQQIWDALE----RTFLTK-----------------------AIILIDEATAS 1269
Cdd:PRK13650 92 nqfvgATVEDDVAFGLEnkgiPHEE-MKERVNEALElvgmQDFKEReparlsggqkqrvaiagavamrpKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1270 IDMETD-TLIQ--RTIREAFQgCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVL 1324
Cdd:PRK13650 171 LDPEGRlELIKtiKGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
531-721 |
3.76e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.74 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 531 NLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--LAYVPQQAwIVSG-----------NIRENILMG-- 595
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRR-PVSMlfqennlfshlTVAQNIGLGln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 -----GAYDKARYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:PRK10771 98 pglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 671 HIF----EECIKKTLrgkTVVLVTHQlqyLEFCGQI----ILLENGKICENGTHSELMQ 721
Cdd:PRK10771 167 EMLtlvsQVCQERQL---TLLMVSHS---LEDAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
530-722 |
3.82e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAI-----LEEMHLLEGSVGVQGSLAYVPQQAWIvsgNIRENILMGGAY-DKARY 603
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPI---EVRREVGMVFQYpNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 604 LQVLHCCSLNRDLELL--PFGDMTEIGERGL------------------NLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALkkaalwdevkdrlndypsNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 664 VDAhVGKHIFEECIKKTLRGKTVVLVTHQ-------LQYLEFCGQIILLENG---KICENGTHsELMQK 722
Cdd:PRK14267 180 IDP-VGTAKIEELLFELKKEYTIVLVTHSpaqaarvSDYVAFLYLGKLIEVGptrKVFENPEH-ELTEK 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
525-714 |
4.49e-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: 55.42 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILeemHLLEGSVGVQGslaYVPqqaWIVSGNIRENI--LMGGAYD 599
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLL---QPTSGEVRVAG---LVP---WKRRKKFLRRIgvVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 600 KARYLQVLHCCSLNRDLELLP----------FGDMTEIGE------RglNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPparfkkrldeLSELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21729876 664 VDAhVGKHIFEECIKK--TLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENG 714
Cdd:cd03267 184 LDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEaLARRVLVIDKGRLLYDG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1156-1319 |
4.53e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 55.23 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE-DLRSKLSVIpqDPVLLSGTIRf 1234
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRLL- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1235 nldpfdRHTDQQIWDALER-------------------------------TFLTKAIILIDEATASIDMETDTLIQRTIR 1283
Cdd:cd03220 113 ------GLSRKEIDEKIDEiiefselgdfidlpvktyssgmkarlafaiaTALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 21729876 1284 EAFQGCTVLVIA-HRVTTVLN-CDHILVMGNGKVVEFD 1319
Cdd:cd03220 187 ELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1156-1317 |
4.61e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDP------- 1225
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPnsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1226 --VL-------------LSGTIR----------FNLDPFDRH---------TDQQIwdALERTFLTK-AIILIDEATASI 1270
Cdd:PRK15134 379 lnVLqiieeglrvhqptLSAAQReqqviavmeeVGLDPETRHrypaefsggQRQRI--AIARALILKpSLIILDEPTSSL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 1271 DMETDTLI-------QRTIREAFqgctvLVIAHRVTTVLN-CDHILVMGNGKVVE 1317
Cdd:PRK15134 457 DKTVQAQIlallkslQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1140-1331 |
5.48e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1140 EIIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIdGVDICSIG-----L 1211
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1212 EDLRSKLSVIPQDP--VLLSGT----IRFNLDPFDRHTDqqiwDALERT------------FLTK-------------AI 1260
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETvekdICFGPMNFGVSEE----DAKQKAremielvglpeeLLARspfelsggqmrrvAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1261 ----------ILIDEATASID-------MEtdtLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1322
Cdd:PRK13634 157 agvlamepevLVLDEPTAGLDpkgrkemME---MFYKLHKE--KGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*....
gi 21729876 1323 VLRKKPGSL 1331
Cdd:PRK13634 232 EIFADPDEL 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
530-692 |
6.06e-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: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQgslayVPQQAWIVSGNIRENILMGGAYDKAryLQVLHC 609
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDA--VELLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 610 CSLNrD--LELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD---AHVGKHIFEECIKKtlRGK 684
Cdd:COG2401 122 VGLS-DavLWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR--AGI 188
|
....*...
gi 21729876 685 TVVLVTHQ 692
Cdd:COG2401 189 TLVVATHH 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
525-729 |
9.37e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMhllEGSVGVQGSLaYVPQQAWivsgNIRENILMG------ 595
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAE---SGQIIIDGDL-LTEENVW----DIRHKIGMVfqnpdn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 ---GAY---DKARYLQ---VLHCCSLNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK13650 93 qfvGATvedDVAFGLEnkgIPHEEMKERVNEALELVGMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 666 AHvGKhifEECIK--KTLR---GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:PRK13650 173 PE-GR---LELIKtiKGIRddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
530-719 |
9.40e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.81 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEM---HLLEG------------SVG-VQGSLAYVPQQawivsgNIREN 591
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIagLEDItsgDLFIGekrmndvppaerGVGmVFQSYALYPHL------SVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMG----GAyDKARYLQvlhccSLNRDLELLPFGDMTEigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA- 666
Cdd:PRK11000 96 MSFGlklaGA-KKEEINQ-----RVNQVAEVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAa 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 667 -HVGKHIFEECIKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK11000 168 lRVQMRIEISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
518-694 |
1.03e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.44 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 518 EEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLLEG-SVGVQGSLAYVPQQAWIVSGNIR------- 589
Cdd:PRK11629 16 QEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLL-------HLLGGlDTPTSGDVIFNGQPMSKLSSAAKaelrnqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 -----------------ENILMGGAYDKARYLQVLhccslNRDLELL-PFGDMTEIGERGLNLSGGQKQRISLARAVYSD 651
Cdd:PRK11629 89 lgfiyqfhhllpdftalENVAMPLLIGKKKPAEIN-----SRALEMLaAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21729876 652 RQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVL-VTHQLQ 694
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLQ 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1132-1224 |
1.06e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1132 PQGWPQHGEIIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 1211
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90
....*....|...
gi 21729876 1212 EDLRSKLSVIPQD 1224
Cdd:PRK10522 393 EDYRKLFSAVFTD 405
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
527-705 |
1.38e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENIL 593
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 594 M-----GGAYDKARYLqvlhccslnRDLEllPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:PRK10247 103 FpwqirNQQPDPAIFL---------DDLE--RFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21729876 668 vGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQIILL 705
Cdd:PRK10247 172 -NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
635-714 |
1.47e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLRGKtvvlvtHQLQYL----------EFCGQIIL 704
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQK------HQLAYLfishdlhvvrALCHQVIV 498
|
90
....*....|
gi 21729876 705 LENGKICENG 714
Cdd:PRK15134 499 LRQGEVVEQG 508
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1158-1333 |
1.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.33 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP------VLLSGT 1231
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnqfvgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1232 IRFNLD----PFD---RHTDQQIWDALERTFLTK-----------------------AIILIDEATASIDMETDTLIQRT 1281
Cdd:PRK13642 103 VAFGMEnqgiPREemiKRVDEALLAVNMLDFKTReparlsggqkqrvavagiialrpEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1282 IREAFQG--CTVLVIAHRVTTVLNCDHILVMGNGKVVEfdrpevlRKKPGSLFA 1333
Cdd:PRK13642 183 IHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIK-------EAAPSELFA 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1133-1326 |
1.57e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1133 QGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 1212
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1213 DLRSKLSVIPQD-PVLLSGTIR-------------------------------FNLDPF-DRHTD-------QQIWDALE 1252
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVRelvaigrypwhgalgrfgaadrekveeaislVGLKPLaHRLVDslsggerQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1253 RTFLTKAiILIDEATASIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EFDRP 1321
Cdd:PRK10575 162 VAQDSRC-LLLDEPTSALDIahqvDVLALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIaqgtpaELMRG 238
|
....*
gi 21729876 1322 EVLRK 1326
Cdd:PRK10575 239 ETLEQ 243
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1168-1322 |
1.63e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1168 HEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdiCSIGLEDLRSKLSVIPQDPVLLSGTirfnldpfDRHTDQQI 1247
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID---GEDILEEVLDQLLLIIVGGKKASGS--------GELRLRLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1248 WDALERtfLTKAIILIDEATASIDMETDTLIQRTIR-------EAFQGCTVLVIAHRVTTVLncDHILVMGNGKVVEFDR 1320
Cdd:smart00382 71 LALARK--LKPDVLILDEITSLLDAEQEALLLLLEElrlllllKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLL 146
|
..
gi 21729876 1321 PE 1322
Cdd:smart00382 147 IL 148
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
527-724 |
1.67e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 53.30 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhllegsvgvqGSLAYVpqqawIVSGNIR---ENILMGGAYDKARy 603
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-------------GHPKYE-----VTEGEILfkgEDITDLPPEERAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 604 lqvlhcCSLnrdleLLPFGDMTEIGE-------RGLN--LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE 674
Cdd:cd03217 77 ------LGI-----FLAFQYPPEIPGvknadflRYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 675 EcIKKTLR-GKTVVLVTHQLQYLEFcgqII-----LLENGKICENGThSELMQ---KKG 724
Cdd:cd03217 146 V-INKLREeGKSVLIITHYQRLLDY---IKpdrvhVLYDGRIVKSGD-KELALeieKKG 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1149-1320 |
1.67e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1149 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE--PMAGRILIDGVDI---CSIgLEDL--------- 1214
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFgreASL-IDAIgrkgdfkda 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1215 -----RSKLSvipqDPVLLsgtirfnLDPFDRHTDQQiwdaLERTFLTKAI------ILIDEATASIDMETDTLIQRTIR 1283
Cdd:COG2401 116 vellnAVGLS----DAVLW-------LRRFKELSTGQ----KFRFRLALLLaerpklLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21729876 1284 EAFQ--GCTVLVIAHR--VTTVLNCDHILVMGNGKVVEFDR 1320
Cdd:COG2401 181 KLARraGITLVVATHHydVIDDLQPDLLIFVGYGGVPEEKR 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1156-1330 |
1.81e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.56 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG-------VDICSIGLED--LRSKLSVIPQ--- 1223
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkVDERLIRQEAgmVFQQFYLFPHlta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 ------DPVLLSGTI-------------------RFNLDPFDRHTDQQIWDALERTFLTK-AIILIDEATASIDMETDTL 1277
Cdd:PRK09493 95 lenvmfGPLRVRGASkeeaekqarellakvglaeRAHHYPSELSGGQQQRVAIARALAVKpKLMLFDEPTSALDPELRHE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1278 IQRTIRE-AFQGCTVLVIAH------RVTTVLncdhiLVMGNGKVVEFDRPEVLRKKPGS 1330
Cdd:PRK09493 175 VLKVMQDlAEEGMTMVIVTHeigfaeKVASRL-----IFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
527-723 |
1.91e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.45 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------------SLAYVPQQAWIVSGN 587
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENILMG----GAYD---KARYLQVLHCCSLNRDL-ELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK13641 103 VLKDVEFGpknfGFSEdeaKEKALKWLKKVGLSEDLiSKSPF-----------ELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 660 PLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQKK 723
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1152-1225 |
2.19e-07 |
|
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: 55.08 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA----GRILIDGVDICSIGLEDLR----SKLSVIPQ 1223
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERELRrirgNRIAMIFQ 99
|
..
gi 21729876 1224 DP 1225
Cdd:COG4172 100 EP 101
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1141-1324 |
2.34e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:PRK13647 5 IEVEDLHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1221 IPQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALE----RTFLTKA-----------------------IILID 1264
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKavrmWDFRDKPpyhlsygqkkrvaiagvlamdpdVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 1265 EATASIDMETdtliQRTIREAF-----QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1324
Cdd:PRK13647 164 EPMAYLDPRG----QETLMEILdrlhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1157-1317 |
2.77e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIGLEDLRSKLSVIPQDP------ 1225
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1226 ---------VLLSGTIRFNLDPFDR----HTDQQIWDAL----------------ERTFLTKA------IILIDEATASI 1270
Cdd:PRK14247 98 sifenvalgLKLNRLVKSKKELQERvrwaLEKAQLWDEVkdrldapagklsggqqQRLCIARAlafqpeVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1271 DMETDTLIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVVE 1317
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVE 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1156-1299 |
3.57e-07 |
|
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: 51.39 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlRSKLSVIPQDPVLLSGTIRfn 1235
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQRPYLPLGTLR-- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1236 ldpfdrhtdQQI---WD-----------ALERTFLTK-AIILIDEATASIDMETDTLIQRTIREAfqGCTVLVIAHRVT 1299
Cdd:cd03223 82 ---------EQLiypWDdvlsggeqqrlAFARLLLHKpKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPS 149
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
634-720 |
3.58e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 53.30 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIinlMLE-LQEKL-GISYIYVSQHLGIVKhISDKVLVMHQGE 227
|
90
....*....|.
gi 21729876 710 ICENGTHSELM 720
Cdd:COG4167 228 VVEYGKTAEVF 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1156-1337 |
4.17e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicSIGLEDLRSKLSVIPQDPVL-------- 1227
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLlpwkkvid 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1228 -----LSGTIRFN----LDPF---DRHTDqqiWDAL------ERTFLTKAII------LIDEATASID----METDTLIQ 1279
Cdd:PRK11247 101 nvglgLKGQWRDAalqaLAAVglaDRANE---WPAAlsggqkQRVALARALIhrpgllLLDEPLGALDaltrIEMQDLIE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1280 RTIREafQGCTVLVIAHRVT-TVLNCDHILVMGNGKV-----VEFDRPevlRKKPGSLFAALMA 1337
Cdd:PRK11247 178 SLWQQ--HGFTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP---RRRGSARLAELEA 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1156-1321 |
4.54e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.77 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDP---VLLS 1229
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1230 GTIR----------FNLDPFDR-HTDQQIWDA-------------------LERTFLTKA------IILIDEATASIDME 1273
Cdd:PRK10419 106 KTVReiireplrhlLSLDKAERlARASEMLRAvdlddsvldkrppqlsggqLQRVCLARAlavepkLLILDEAVSNLDLV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1274 TDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEfDRP 1321
Cdd:PRK10419 186 LQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE-TQP 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1155-1322 |
4.64e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1155 PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGL----------EDlRSKLSVIP 1222
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDairagimlcpED-RKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1223 ----QDPVLLSG-----TIRFNLDPF--DRHTDQQIWDALERT--------FLT-----KAI-----------ILIDEAT 1267
Cdd:PRK11288 345 vhsvADNINISArrhhlRAGCLINNRweAENADRFIRSLNIKTpsreqlimNLSggnqqKAIlgrwlsedmkvILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1268 ASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPE 1322
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELAREQ 482
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
256-445 |
4.90e-07 |
|
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: 52.99 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 256 TSGEAISFFTGDVNYLFEGVCY------GPLVLITCASLVICSISSYFIIGytafiaILCYLLVFPLAVFMTRMAVKAQH 329
Cdd:cd18559 93 PSGELVNLFSKDLDRVDSMAPQvikmwmGPLQNVIGLYLLILLAGPMAAVG------IPLGLLYVPVNRVYAASSRQLKR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 330 HTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKC----GLVQSLTSITLFIIPTVATAVWVLIH 405
Cdd:cd18559 167 LESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIvylrALAVRLWCVGPCIVLFASFFAYVSRH 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21729876 406 TSlkLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSK 445
Cdd:cd18559 247 SL--AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
530-721 |
5.28e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAIL--------------EEMHLLEGSVGVQGSLAYVPQQAWI-----VSGN--- 587
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVgivprdagniiiddEDISLLPLHARARRGIGYLPQEASIfrrlsVYDNlma 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 ---IRENILMGGAYDKARYL-QVLHCCSLNRDLellpfgdmteigerGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK10895 102 vlqIRDDLSAEQREDRANELmEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 664 VDAhvgkhIFEECIKKTL-----RGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK10895 168 VDP-----ISVIDIKRIIehlrdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1156-1317 |
6.23e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI------------------------CSIGL 1211
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkglirqlrqhvgfvfQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1212 EDLRSKLSVIPQDPVLLSGTIRFNL-----------------DPFDRHTD--QQIWDALERTF-LTKAIILIDEATASID 1271
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEAtararellakvglagkeTSYPRRLSggQQQRVAIARALaMRPEVILFDEPTSALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 1272 METDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1317
Cdd:PRK11264 177 PELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
524-721 |
6.77e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.39 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMH----------LLEGSVGVQGSL-----AYV---PQQAW--- 582
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqtagrvLLDGKPVAPCALrgrkiATImqnPRSAFnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 583 -IVSGNIRENIL-MGGAYDKARYLQVLHCCSLN---RDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK10418 96 hTMHTHARETCLaLGKPADDATLTAALEAVGLEnaaRVLKLYPF-----------EMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 658 DDPLSAVDAHVGKHIFE--ECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ 721
Cdd:PRK10418 165 DEPTTDLDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLAdDVAVMSHGRIVEQGDVETLFN 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1161-1312 |
7.20e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI-DGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL--- 1236
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1237 ----------------DPFDRHTDQQI----------------------------------------------------- 1247
Cdd:PTZ00265 484 lyslkdlealsnyyneDGNDSQENKNKrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdvskkvlihdfvs 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1248 -----WDAL-------------ERTFLTKAII------LIDEATASIDMETDTLIQRTIR--EAFQGCTVLVIAHRVTTV 1301
Cdd:PTZ00265 564 alpdkYETLvgsnasklsggqkQRISIARAIIrnpkilILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
250
....*....|.
gi 21729876 1302 LNCDHILVMGN 1312
Cdd:PTZ00265 644 RYANTIFVLSN 654
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
527-736 |
7.27e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.39 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMhllEGSVGVQG--------SLAYVPQQAWIVSGN-------- 587
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPT---SGEVLIKGepikydkkSLLEVRKTVGIVFQNpddqlfap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 -IRENILMGgaydkarylqvlhccSLNRDLellpfgDMTEIGER--------GL---------NLSGGQKQRISLARAVY 649
Cdd:PRK13639 95 tVEEDVAFG---------------PLNLGL------SKEEVEKRvkealkavGMegfenkpphHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 650 SDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKG---- 724
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDIEtirk 233
|
250
....*....|....*...
gi 21729876 725 ------KYAQLIQKMHKE 736
Cdd:PRK13639 234 anlrlpRVAHLIEILNKE 251
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
525-721 |
8.50e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.32 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGsLAYVPQQAWivsgNIRENILM---------G 595
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVW----DVRRQVGMvfqnpdnqfV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 GAY---DKARYL---QVLHCCSLNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhV 668
Cdd:PRK13635 96 GATvqdDVAFGLeniGVPREEMVERVDQALRQVGMEDFLNREpHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP-R 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 669 GKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK13635 175 GRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
527-703 |
8.74e-07 |
|
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: 50.40 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEmhllEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYdkarylqv 606
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 607 lhcCSLNRDLEllpfgdmteigerglNLSGGQKQRISLARAVYSD--RQIYLLDDPLSAVDaHVGKHIFEECIKKTL-RG 683
Cdd:cd03238 79 ---LTLGQKLS---------------TLSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLG 139
|
170 180
....*....|....*....|
gi 21729876 684 KTVVLVTHQLQYLEFCGQII 703
Cdd:cd03238 140 NTVILIEHNLDVLSSADWII 159
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1156-1334 |
1.07e-06 |
|
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: 51.47 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI-------------------------- 1209
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphkrpvntvfqnyalfphltvfeni 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1210 --GLEDLRSKLSVIPQ------DPVLLSGTIrfNLDPFDRHTDQQIWDALERTFLTK-AIILIDEATASIDMETDTLIQR 1280
Cdd:cd03300 94 afGLRLKKLPKAEIKErvaealDLVQLEGYA--NRKPSQLSGGQQQRVAIARALVNEpKVLLLDEPLGALDLKLRKDMQL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1281 TIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1334
Cdd:cd03300 172 ELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1141-1327 |
1.08e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 1213
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1214 LRSKLSVIPQDP-----------VLLSGTIRFNLD---PFDRHTDQQIWDALERTFLTKA-------------------- 1259
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtverEIIFGPKNFKMNldeVKNYAHRLLMDLGFSRDVMSQSpfqmsggqmrkiaivsilam 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1260 ---IILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKK 1327
Cdd:PRK13646 163 npdIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1141-1316 |
1.14e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRdNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsigLEDLRSKL-S 1219
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1220 VIPQD-------PVLLSGTI---RFNLDPFDRHT---DQQIWDAL----------------------ERTFLTKAI---- 1260
Cdd:PRK15056 82 YVPQSeevdwsfPVLVEDVVmmgRYGHMGWLRRAkkrDRQIVTAAlarvdmvefrhrqigelsggqkKRVFLARAIaqqg 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1261 --ILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHIlVMGNGKVV 1316
Cdd:PRK15056 162 qvILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
869-1027 |
1.30e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 51.68 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 869 NALLLICVGVCSSGIF------------TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPI 936
Cdd:cd18570 39 NLLNIISIGLILLYLFqsllsyirsyllLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 937 FSEQFLVLSLMVIAVLLIVSVLSPY----ILLMGAIIMVICFIYYMMFKKAIGvfKRLENYSRspLFSHILNSLQGLSSI 1012
Cdd:cd18570 118 TTISLFLDLLMVIISGIILFFYNWKlfliTLLIIPLYILIILLFNKPFKKKNR--EVMESNAE--LNSYLIESLKGIETI 193
|
170
....*....|....*
gi 21729876 1013 HVYGKTEDFISQFKR 1027
Cdd:cd18570 194 KSLNAEEQFLKKIEK 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1156-1206 |
1.33e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 52.00 E-value: 1.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GmalfrLVEPMAGRILIDGVDI 1206
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV 67
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
634-719 |
1.33e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 712
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*..
gi 21729876 713 NGTHSEL 719
Cdd:PRK14271 243 EGPTEQL 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1141-1328 |
1.63e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.34 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK 1217
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1218 LSVIPQDP------VLLSGTIRFNLDpfDRHTDQQ-----IWDALERTFLTK---------------------------A 1259
Cdd:PRK13640 86 VGIVFQNPdnqfvgATVGDDVAFGLE--NRAVPRPemikiVRDVLADVGMLDyidsepanlsggqkqrvaiagilavepK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1260 IILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKP 1328
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1154-1330 |
1.84e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1154 TPTVL-HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP----MAGRILIDGVdicSIGLEDLRSKL-SVIPQDPvl 1227
Cdd:PRK10418 14 AAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRKiATIMQNP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1228 lsgtiR--FN-LDPFDRH------------TDQQIWDALE------------------------RTFLTKAI------IL 1262
Cdd:PRK10418 89 -----RsaFNpLHTMHTHaretclalgkpaDDATLTAALEavglenaarvlklypfemsggmlqRMMIALALlceapfII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1263 IDEATASID----METDTLIQRTIREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGS 1330
Cdd:PRK10418 164 ADEPTTDLDvvaqARILDLLESIVQK--RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
850-1070 |
1.87e-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: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 850 LGNIADNPQLSFYQLVYGLNALLLICVGVCSS-------GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 922
Cdd:cd18557 19 IGRLIDTIIKGGDLDVLNELALILLAIYLLQSvftfvryYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 923 FAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLF--- 999
Cdd:cd18557 99 LSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALAkag 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1000 SHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS 1070
Cdd:cd18557 176 QVAEESLSNIRTVRSFSAEEKEIRRYS---EALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGY 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
527-709 |
2.47e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILE------EMHLLEGSVGVQG-------SLAYVPQQAWIVSG-NIR 589
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPhgtwdgEIYWSGSPLKASNirdteraGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMGG---------AYDkaryLQVLHCCSLNRDLELLPFGDMTEIGERGlnlsGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:TIGR02633 97 ENIFLGNeitlpggrmAYN----AMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21729876 661 LSAVDAHVGKHIFEecIKKTLRGKTV--VLVTHQLQYLE-FCGQIILLENGK 709
Cdd:TIGR02633 169 SSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKaVCDTICVIRDGQ 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
527-743 |
2.49e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaiLEEMHLLE---GSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLL---LTFMRMVEvcgGEIRVNGreigayglrelrrQFSMIPQDPVLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NIlmgGAYDKARYLQVLhccslnRDLELLPF---------GDMTEIGERGLNLSGGQKQRISLARAVYS-DRQIYLLDDP 660
Cdd:PTZ00243 1403 NV---DPFLEASSAEVW------AALELVGLrervaseseGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEA 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 661 LSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSEL-MQKKGKYAQLIQKMHKEATS 739
Cdd:PTZ00243 1474 TANIDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEALGRSEAK 1552
|
....
gi 21729876 740 DMLQ 743
Cdd:PTZ00243 1553 RFLQ 1556
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
589-747 |
2.77e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 589 RENILMGGaydkaRYLQVLHCCSLNRDLELLPFGDMTEI-GERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:NF000106 104 RENLYMIG-----R*LDLSRKDARARADELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 668 VGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSDMLQDTA 746
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIA 258
|
.
gi 21729876 747 K 747
Cdd:NF000106 259 Q 259
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
528-698 |
3.45e-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: 48.51 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 528 HKINLVV-----SKGMMLGVCGNTGSGKSSLLSAILeemhLLEGSVGVQGSLAYVPQQAWIVsgnirenilmggAYDKAR 602
Cdd:cd03227 7 FPSYFVPndvtfGEGSLTIITGPNGSGKSTILDAIG----LALGGAQSATRRRSGVKAGCIV------------AAVSAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 603 YLQVLHCcslnrdlellpfgdmteigerglnLSGGQKQRISLARAV----YSDRQIYLLDDPLSAVDAHVGKHIFEECIK 678
Cdd:cd03227 71 LIFTRLQ------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170 180
....*....|....*....|
gi 21729876 679 KTLRGKTVVLVTHQLQYLEF 698
Cdd:cd03227 127 HLVKGAQVIVITHLPELAEL 146
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
527-721 |
3.60e-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: 49.85 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------------SLAYVPQQAWIVSG-NIREN 591
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILM---GGAYDKARYLQVLHccSLNRDLELLPFGDmteigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:cd03218 96 ILAvleIRGLSKKEREEKLE--ELLEEFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 669 GKHIFEecIKKTLRGKTV-VLVT-HQL-QYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:cd03218 169 VQDIQK--IIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
530-722 |
4.25e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLS--AILEEMHllEGSVGVQG------------------SLAYVPQQAwiVSGNIR 589
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRlvAGLEKPT--EGQIFIDGedvthrsiqqrdicmvfqSYALFPHMS--LGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMGGAYDKARYLQVlhccslNRDLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK11432 101 YGLKMLGVPKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 669 GKHIFEEC--IKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK11432 172 RRSMREKIreLQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1163-1316 |
4.55e-06 |
|
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: 49.03 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1163 LTIRGHEVVGIVGRTGSGKSSL--GMALFRLvePMAGRILIDGVDICSigLEDLRSKLSVIPQDPVLLSG-TIRFNLD-- 1237
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLlnLIAGFET--PQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHlTVEQNVGlg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1238 --PFDRHT--DQQIWD---------------------------ALERTFL-TKAIILIDEATASID----METDTLIQRT 1281
Cdd:cd03298 95 lsPGLKLTaeDRQAIEvalarvglaglekrlpgelsggerqrvALARVLVrDKPVLLLDEPFAALDpalrAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 21729876 1282 IREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVV 1316
Cdd:cd03298 175 HAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
517-722 |
4.67e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 517 EEEGNSLgPELHKINLVVSKGMMLGVCGNTGSGKSSllsaILEEMHLL----EGSVGVQGSLAYVPQQAWivsgNIRENI 592
Cdd:PRK13633 17 NEESTEK-LALDDVNLEVKKGEFLVILGRNGSGKST----IAKHMNALlipsEGKVYVDGLDTSDEENLW----DIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 593 LMggaydkarylqVLHccslNRDLELLP--------FG------DMTEIGERGLN-----------------LSGGQKQR 641
Cdd:PRK13633 88 GM-----------VFQ----NPDNQIVAtiveedvaFGpenlgiPPEEIRERVDEslkkvgmyeyrrhaphlLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 642 ISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDP-SGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 21729876 720 MQK 722
Cdd:PRK13633 232 FKE 234
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
163-427 |
4.82e-06 |
|
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: 49.86 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 163 LIFDALLGICFCIASVLGP----ILIIPKILEYSEEQLGNVVhgVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAV 238
Cdd:cd07346 1 LLLALLLLLLATALGLALPlltkLLIDDVIPAGDLSLLLWIA--LLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 239 ssfaFEKLIQ-----FKSvihITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYL-L 312
Cdd:cd07346 79 ----FRHLQRlslsfFDR---NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLpL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 313 VFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:cd07346 152 YVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 21729876 393 IPTVATAV--WVLIHTSLKLKLTASMAFSMLASLNLL 427
Cdd:cd07346 232 LTALGTALvlLYGGYLVLQGSLTIGELVAFLAYLGML 268
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
525-699 |
5.47e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-----LAYVPQQAWIV---SG-----NIREN 591
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdLCTYQKQLCFVghrSGinpylTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILmggaYD---KARYLQVLHCCSLNRDLELLPFgdmteigERGLnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK13540 95 CL----YDihfSPGAVGITELCRLFSLEHLIDY-------PCGL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 21729876 669 GKHIFEECIKKTLRGKTVVLVTHQ------LQYLEFC 699
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQdlplnkADYEEYH 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1153-1317 |
5.50e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.66 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1153 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE------PMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 1225
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1226 ----VLLSGTIRFNLDPFDRHTDQQIWDALERTF-----------------------------------LTKAIILIDEA 1266
Cdd:PRK14246 101 pfphLSIYDNIAYPLKSHGIKEKREIKKIVEECLrkvglwkevydrlnspasqlsggqqqrltiaralaLKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1267 TASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1317
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
517-712 |
5.88e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 517 EEEGNSLGPelhkINLVVSKGMMLGVCGNTGSGKSSLlsaileEMhLLEGsvgvqgslAYVPQQAWI------VSGNIRE 590
Cdd:PRK10522 333 QDNGFSVGP----INLTIKRGELLFLIGGNGSGKSTL------AM-LLTG--------LYQPQSGEIlldgkpVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NI----------------LMGG---AYDKARYLQVLHCCSLNRDLELlpfgdmtEIGE-RGLNLSGGQKQRISLARAVYS 650
Cdd:PRK10522 394 DYrklfsavftdfhlfdqLLGPegkPANPALVEKWLERLKMAHKLEL-------EDGRiSNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 651 DRQIYLLDDPLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICE 712
Cdd:PRK10522 467 ERDILLLDEWAADQDPHF-RREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
527-710 |
6.21e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.31 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQ---AWI-------VSG-----NIRE 590
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvfqdpMMGtapsmTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMggAY---------------DKARYLQVLhcCSLNRDLEllpfgDM--TEIGerglNLSGGQKQRISLARAVYSDRQ 653
Cdd:COG1101 102 NLAL--AYrrgkrrglrrgltkkRRELFRELL--ATLGLGLE-----NRldTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 654 IYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENGKI 710
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
517-710 |
6.35e-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: 50.57 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 517 EEEGNSLGPelhkINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLLEGsvgvqgsLaYVPQqawivSGNIR------- 589
Cdd:COG4615 342 GDEGFTLGP----IDLTIRRGELVFIVGGNGSGKSTL-------AKLLTG-------L-YRPE-----SGEILldgqpvt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 -ENI-------------------LMGGAY----DKARYLqvlhccslnrdLELLPFGDMTEIgERG----LNLSGGQKQR 641
Cdd:COG4615 398 aDNReayrqlfsavfsdfhlfdrLLGLDGeadpARAREL-----------LERLELDHKVSV-EDGrfstTDLSQGQRKR 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 642 ISLARAVYSDRQIYLLD------DPlsavdahVGKHIF-EECI---KKtlRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:COG4615 466 LALLVALLEDRPILVFDewaadqDP-------EFRRVFyTELLpelKA--RGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1143-1316 |
7.01e-06 |
|
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: 48.43 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1143 FQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG-----VDICSIGL--ED-- 1213
Cdd:cd03269 3 VENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiAARNRIGYlpEErg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1214 LRSKLSVIPQdpVLLSGTIRfNLDPfdRHTDQQIWDALERTFLTK---------------------------AIILIDEA 1266
Cdd:cd03269 81 LYPKMKVIDQ--LVYLAQLK-GLKK--EEARRRIDEWLERLELSEyankrveelskgnqqkvqfiaavihdpELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1267 TASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1316
Cdd:cd03269 156 FSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1141-1322 |
9.25e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTPTVLHG---INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC----SIGLED 1213
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1214 LRSKLSVIPQDP--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFLTKA------------------------- 1259
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTvlkdVEFgpkNFGFSEDEAKEKALKWLKKVGLSEDliskspfelsggqmrrvaiagvmay 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1260 ---IILIDEATASIDMETdtliQRTIREAFQ-----GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1322
Cdd:PRK13641 163 epeILCLDEPAAGLDPEG----RKEMMQLFKdyqkaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPK 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1153-1288 |
9.43e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1153 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GMALFRLVEpmaGRILIDGVDICSIGLEDlRSKLSVIP--QDP 1225
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLskviaGHPAYKILE---GDILFKGESILDLEPEE-RAHLGIFLafQYP 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1226 VLLSGT-----IRFNLDPFDRHTDQQIWDALErtFLTkaiiLIDEATASIDMETdTLIQRTIREAFQG 1288
Cdd:CHL00131 94 IEIPGVsnadfLRLAYNSKRKFQGLPELDPLE--FLE----IINEKLKLVGMDP-SFLSRNVNEGFSG 154
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
544-710 |
1.03e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 544 GNTGSGKSSLLSAI------------LEEMHLLEGSVGV-----QGSLAYVPQQA-----WIVSGNIRENIlmgGAYDKA 601
Cdd:PRK11144 31 GRSGAGKTSLINAIsgltrpqkgrivLNGRVLFDAEKGIclppeKRRIGYVFQDArlfphYKVRGNLRYGM---AKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 602 RYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI--FEECIKK 679
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLERLAR 176
|
170 180 190
....*....|....*....|....*....|...
gi 21729876 680 TLrgKTVVL-VTHQLQ-YLEFCGQIILLENGKI 710
Cdd:PRK11144 177 EI--NIPILyVSHSLDeILRLADRVVVLEQGKV 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
530-720 |
1.04e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQ----AWIVSGNIREN 591
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITESrrdnGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILM---------GGAY------------DKARYLQVLHCCSLNRDlellpfgdmteIGErglnLSGGQKQRISLARAVYS 650
Cdd:PRK09700 362 MAIsrslkdggyKGAMglfhevdeqrtaENQRELLALKCHSVNQN-----------ITE----LSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 651 DRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKI------CENGTHSELM 720
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLtqiltnRDDMSEEEIM 503
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1153-1313 |
1.08e-05 |
|
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: 48.10 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1153 NTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK----LSVIPQDPVLL 1228
Cdd:cd03290 13 GLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1229 SGTIRFNL---DPFDRHTDQQIWDAL-----------------------------ERTFLTKA------IILIDEATASI 1270
Cdd:cd03290 92 NATVEENItfgSPFNKQRYKAVTDACslqpdidllpfgdqteigerginlsggqrQRICVARAlyqntnIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 1271 DME-TDTLIQRTIREAFQG--CTVLVIAHRVTTVLNCDHILVMGNG 1313
Cdd:cd03290 172 DIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1136-1322 |
1.09e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1136 PQHGEIIFQ-----DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-----RLVepmAGRILIDG-- 1203
Cdd:NF040905 251 PKIGEVVFEvknwtVYHPLHPERK--VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDGke 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1204 VDICSI------GL----EDlRSKLSVIpqdpvlLSGTIRFN-----LDPF------DRHTDQQIWDALERTFLTKA--- 1259
Cdd:NF040905 326 VDVSTVsdaidaGLayvtED-RKGYGLN------LIDDIKRNitlanLGKVsrrgviDENEEIKVAEEYRKKMNIKTpsv 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1260 --------------------------IILIDEATASIDM----ETDTLIQRTireAFQGCTVLVIAHRVTTVLN-CDHIL 1308
Cdd:NF040905 399 fqkvgnlsggnqqkvvlskwlftdpdVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVISSELPELLGmCDRIY 475
|
250
....*....|....*
gi 21729876 1309 VMGNGKVV-EFDRPE 1322
Cdd:NF040905 476 VMNEGRITgELPREE 490
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
850-1068 |
1.11e-05 |
|
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: 48.95 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 850 LGNIAD---NPQLSFYQLVYglNALLLICVGVCSsGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGR 918
Cdd:cd18541 22 IGRAIDaltAGTLTASQLLR--YALLILLLALLI-GIFRflwrylifGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 919 LLNCFAGDLEQLDQLL-P--IFSEQFLVLSLMVIAVLLIVSV-LSPYILLMgAIIMVICFIYY--MMFKKaigvFKRL-E 991
Cdd:cd18541 99 LMARATNDLNAVRMALgPgiLYLVDALFLGVLVLVMMFTISPkLTLIALLP-LPLLALLVYRLgkKIHKR----FRKVqE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 992 NYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18541 174 AFSD--LSDRVQESFSGIRVIKAFVQEEAEIERFDKLNE---EYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYG 245
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
525-733 |
1.20e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.45 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMH---LLEGSVGVQGSLAYVPQQAWIVSGNiRENILMGGAY 598
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQSgeiKIDGITISKENLKEIRKKIGIIFQN-PDNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 --DKARYLQvlhccslNRdleLLPFGDMTEIGE--------------RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:PRK13632 102 edDIAFGLE-------NK---KVPPKKMKDIIDdlakkvgmedyldkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 663 AVDAHvGKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKgkyaQLIQKM 733
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 ... |
530-720 |
1.50e-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: 47.82 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQAWIVSG-NIRENILM 594
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 GGAYDKARYLQVLHCCSLNRDL-----ELLpfgDMTEIGER-----GlNLSGGQKQRISLARAVYSDRQIYLLDDP---L 661
Cdd:cd03219 99 AAQARTGSGLLLARARREEREAreraeELL---ERVGLADLadrpaG-ELSYGQQRRLEIARALATDPKLLLLDEPaagL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 662 SAVDAHVGKHIFEEcIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELM 720
Cdd:cd03219 175 NPEETEELAELIRE-LRE--RGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
530-719 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 530 INLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGS-----------------------LAYVPQQA----- 581
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAI---LGLLPPPGITSGEilfdgedllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 582 ------WIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELL---PFgdmteigerglNLSGGQKQRISLARAVYSDR 652
Cdd:COG0444 101 pvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 653 QIYLLDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQIlnlLKD-LQRE-LGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1141-1324 |
1.75e-05 |
|
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: 47.77 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG---RIL---IDGVDIC----SIG 1210
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWelrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1211 L------EDLRSKLSVIpqDpVLLSGtiRFN-LDPFDRHTDQQ------------IWDALERTFLT-------------- 1257
Cdd:COG1119 82 LvspalqLRFPRDETVL--D-VVLSG--FFDsIGLYREPTDEQrerarellellgLAHLADRPFGTlsqgeqrrvliara 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21729876 1258 -----KAIILiDEATASIDMETDTLIQRTIRE-AFQGCTVLV-IAHRVTTVLNC-DHILVMGNGKVVEF-DRPEVL 1324
Cdd:COG1119 157 lvkdpELLIL-DEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAgPKEEVL 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1160-1225 |
2.07e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 2.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1160 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL---RSKLSVIPQDP 1225
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP 107
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1169-1243 |
2.34e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 2.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1169 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIG-LEDLRSKLSVIPQDPVLlsgtirfNLDPfdRHT 1243
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPYA-------SLDP--RQT 419
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
634-721 |
2.69e-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: 48.53 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTL---RGKTVVLVTHQLQ---YLefCGQIILLEN 707
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLqreHGLAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 21729876 708 GKICENGTHSELMQ 721
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
524-722 |
2.82e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.43 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHL-LEGSVGVQGS----------LAYVPQQAWIV-----SGN 587
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQ-LLNGLHVpTQGSVRVDDTlitstsknkdIKQIRKKVGLVfqfpeSQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 IRENILMGGAYD-----------KARYLQVLHCCSLNRDL-ELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIY 655
Cdd:PRK13649 99 FEETVLKDVAFGpqnfgvsqeeaEALAREKLALVGISESLfEKNPF-----------ELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 656 LLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
527-722 |
3.49e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.05 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------LAYVPQQAWIVSGNiRENILMGG--AY 598
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnFEKLRKHIGIVFQN-PDNQFVGSivKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 599 DKARYLQvlhccslNrdlELLPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK13648 104 DVAFGLE-------N---HAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 665 DAHVGKHIFeECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13648 174 DPDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
527-715 |
3.59e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.03 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSL--AYVPQQAWI-------VS-------GNIRE 590
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYLdttlpltVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 591 NILMGGAYDKARYLqvlhccsLNRDLEllpfgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD--AHV 668
Cdd:PRK09544 100 DILPALKRVQAGHL-------IDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 669 GKHIFEECIKKTLrGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:PRK09544 158 ALYDLIDQLRREL-DCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGT 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1154-1233 |
3.68e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.14 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1154 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGvdicsigleDLRskLSVIPQDPVLLS 1229
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPK---------GLR--IGYLPQEPPLDD 74
|
....*
gi 21729876 1230 G-TIR 1233
Cdd:COG0488 75 DlTVL 79
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
527-719 |
3.94e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.11 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS---------------LAYVPQQAWIVSGNIREN 591
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMG-------GAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 665 DAHVGKHI--FEECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:PRK13652 169 DPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1156-1316 |
3.95e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI--------CSIGLEDLRSKLSVIPQDPV- 1226
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 -------------------------------LLSGTIRFNLDPFDRH---TDQQIWDALERTFLTKAIILIDEATASI-D 1271
Cdd:PRK09700 99 enlyigrhltkkvcgvniidwremrvraammLLRVGLKVDLDEKVANlsiSHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21729876 1272 METDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1316
Cdd:PRK09700 179 KEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1156-1257 |
4.14e-05 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 45.95 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 1235
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100
....*....|....*....|...
gi 21729876 1236 LDPFDR-HTDQQIWDALERTFLT 1257
Cdd:cd03231 94 LRFWHAdHSDEQVEEALARVGLN 116
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
634-719 |
4.93e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTH-QLQYLEFCGQIILLENGKICE 712
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 21729876 713 NGTHSEL 719
Cdd:PRK14247 226 WGPTREV 232
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
870-1091 |
6.00e-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: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 870 ALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVI 949
Cdd:cd18548 49 ALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 950 AVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLN-----SLQGLSSIHVYGKtEDFi 1022
Cdd:cd18548 129 GAIIMAFRINPKLaLILLVAIPILALVVFLIMKKAIPLFKKVqKKLDR-------LNrvvreNLTGIRVIRAFNR-EDY- 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1023 sQFKRLTDAQNNYLLLFLSSTRWMALRLEIMT---NLVTLAVALFVAFGISSTPYSF-KVMA-VNIVLQLASSF 1091
Cdd:cd18548 200 -EEERFDKANDDLTDTSLKAGRLMALLNPLMMlimNLAIVAILWFGGHLINAGSLQVgDLVAfINYLMQILMSL 272
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
527-718 |
6.13e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.58 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQAWIV---------SGNIR 589
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKVGLVfqypeyqlfEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 590 ENILMG----GAYDKARYLQVlhccslNRDLEL--LPFGDMTEigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK13637 103 KDIAFGpinlGLSEEEIENRV------KRAMNIvgLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 664 VDAHVGKHIFEECikKTLRGK---TVVLVTHQLQYL-EFCGQIILLENGKICENGTHSE 718
Cdd:PRK13637 175 LDPKGRDEILNKI--KELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
900-1068 |
6.33e-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: 46.79 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 900 FNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVIcfIYYMM 979
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPL--IIAGT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 980 FKkaigvF-KRLE-NYSR-----SPLFSHILNSLQGLSSIHVYGkTEDFisQFKRLTDAQNNYLllflsSTRWMALRLEI 1052
Cdd:cd18565 172 YW-----FqRRIEpRYRAvreavGDLNARLENNLSGIAVIKAFT-AEDF--ERERVADASEEYR-----DANWRAIRLRA 238
|
170 180
....*....|....*....|..
gi 21729876 1053 M----TNLVTLA--VALFVAFG 1068
Cdd:cd18565 239 AffpvIRLVAGAgfVATFVVGG 260
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
634-722 |
6.84e-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: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
90
....*....|..
gi 21729876 711 CENGTHSELMQK 722
Cdd:PRK11650 214 EQIGTPVEVYEK 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1156-1206 |
7.33e-05 |
|
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: 45.32 E-value: 7.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI 1206
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV 64
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
503-690 |
8.53e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 503 ASEGMTRPRDALgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAW 582
Cdd:PRK13543 13 AAHALAFSRNEE----------PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 583 IVS-----GNIRENIlmgGAYDKARYLQVLHCCSLNRdlelLPFGDMTEIGERGL------NLSGGQKQRISLARAVYSD 651
Cdd:PRK13543 83 FMAylghlPGLKADL---STLENLHFLCGLHGRRAKQ----MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 21729876 652 RQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGKTVVLVT 690
Cdd:PRK13543 156 APLWLLDEPYANLDLE-GITLVNRMISAHLRGGGAALVT 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
528-734 |
8.63e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 528 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAwIVSGNIRENILM 594
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNA-TTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 595 GgaydKARYLQVLHCCSLNRDLELLPFGDMTEIGERGL------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahV 668
Cdd:PRK10253 103 A----RGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLadqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--I 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 669 GKHI-FEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQkkgkyAQLIQKMH 734
Cdd:PRK10253 177 SHQIdLLELLSELNRekGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT-----AELIERIY 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1156-1317 |
8.92e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---------IGLED-LRSKLSVIP--- 1222
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeachyLGHRNaMKPALTVAEnle 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1223 -------QDPVLLSGTI-RFNLDP-FDRH-----TDQQIWDALERTFLTKAII-LIDEATASIDMETDTLIQRTIRE-AF 1286
Cdd:PRK13539 96 fwaaflgGEELDIAAALeAVGLAPlAHLPfgylsAGQKRRVALARLLVSNRPIwILDEPTAALDAAAVALFAELIRAhLA 175
|
170 180 190
....*....|....*....|....*....|.
gi 21729876 1287 QGCTVLVIAHRVTTVLNCdHILVMGNGKVVE 1317
Cdd:PRK13539 176 QGGIVIAATHIPLGLPGA-RELDLGPFAAED 205
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
870-1069 |
9.22e-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: 45.89 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 870 ALLLICVGVcSSGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQF 941
Cdd:cd18542 42 ALLILGVAL-LRGVFRylqgylaeKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 942 LVLSLMVIAVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLNS-LQ-GLSSIHV--- 1014
Cdd:cd18542 121 VRAVLLFIGALIIMFSINWKLtLISLAIIPFIALFSYVFFKKVRPAFEEIrEQEGE-------LNTvLQeNLTGVRVvka 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1015 YGKtEDF-ISQFkrltDAQN-NYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 1069
Cdd:cd18542 194 FAR-EDYeIEKF----DKENeEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGG 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
527-723 |
1.06e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.61 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIvsgNIRENIlmGGAYDKARylQV 606
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLM---KLRESV--GMVFQDPD--NQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 607 LHCCSLNRDLEL------LPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:PRK13636 95 LFSASVYQDVSFgavnlkLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 667 hVGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKK 723
Cdd:PRK13636 175 -MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
517-687 |
1.17e-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: 44.56 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 517 EEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 596
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL---ANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 597 AYDkarylqvLHCCSLNRDlELLPF------GDMTeigeRGlnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:cd03233 90 EED-------VHFPTLTVR-ETLDFalrckgNEFV----RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180
....*....|....*....|
gi 21729876 671 HIFeECIK---KTLRGKTVV 687
Cdd:cd03233 156 EIL-KCIRtmaDVLKTTTFV 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
632-718 |
1.26e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 632 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-------AHVGKHIFEEcikktlRGKTVVLVTHQLQYLEFCGQIIL 704
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKTALVVEHDLAVLDYLSDRIH 143
|
90
....*....|....
gi 21729876 705 LENGKICENGTHSE 718
Cdd:cd03222 144 VFEGEPGVYGIASQ 157
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1157-1236 |
1.27e-04 |
|
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: 45.62 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsKLSVIPQDPVLLSGTIRFNL 1236
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
205-427 |
1.36e-04 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 45.49 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 205 LCFALFLSECVKSL-SFSSSWIIN---QRTAIRFRAAVssfaFEKLIQ-----FKSvihITSGEAISFFTGDVNYLFEGV 275
Cdd:cd18552 41 VPLAIIGLFLLRGLaSYLQTYLMAyvgQRVVRDLRNDL----FDKLLRlplsfFDR---NSSGDLISRITNDVNQVQNAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 276 CYGPLVLITCASLVICSISSYFIIGYT-AFIAilcyLLVFPLAVFMT--------RMAVKAQHHTSEVSdqriRVTSEVL 346
Cdd:cd18552 114 TSALTVLVRDPLTVIGLLGVLFYLDWKlTLIA----LVVLPLAALPIrrigkrlrKISRRSQESMGDLT----SVLQETL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 347 TCIKLIKMYTWEKP----FAKIIEDLRRKERKLLekcgLVQSLTS--ITLFIIPTVATAVWVLIHTSLKLKLTASMAFSM 420
Cdd:cd18552 186 SGIRVVKAFGAEDYeikrFRKANERLRRLSMKIA----RARALSSplMELLGAIAIALVLWYGGYQVISGELTPGEFISF 261
|
....*..
gi 21729876 421 LASLNLL 427
Cdd:cd18552 262 ITALLLL 268
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1152-1318 |
1.61e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.49 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSI---GLEDLRS-KLSVIPQD 1224
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekELNKLRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1225 PVLlsgtirfNLDPFDRHTDQ---------------------QIWDAL---------------------ERTFLTKAI-- 1260
Cdd:PRK09473 106 PMT-------SLNPYMRVGEQlmevlmlhkgmskaeafeesvRMLDAVkmpearkrmkmyphefsggmrQRVMIAMALlc 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1261 ---ILI-DEATASIDMETD----TLIQRTIREaFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1318
Cdd:PRK09473 179 rpkLLIaDEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1170-1319 |
1.62e-04 |
|
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: 46.08 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1170 VVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILI-DGVDICSI-----GLEDLRSKLSVIP--QDPVLLSGTI----- 1232
Cdd:TIGR03719 350 IVGVIGPNGAGKST----LFRMItgqeQPDSGTIEIgETVKLAYVdqsrdALDPNKTVWEEISggLDIIKLGKREipsra 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1233 ---RFNLdpfdRHTDQQ----IWDALERTFLTKA--------IILIDEATASIDMETdtliQRTIREA---FQGCTVlVI 1294
Cdd:TIGR03719 426 yvgRFNF----KGSDQQkkvgQLSGGERNRVHLAktlksggnVLLLDEPTNDLDVET----LRALEEAllnFAGCAV-VI 496
|
170 180 190
....*....|....*....|....*....|..
gi 21729876 1295 AH------RVTTvlncdHILVM-GNGKVVEFD 1319
Cdd:TIGR03719 497 SHdrwfldRIAT-----HILAFeGDSHVEWFE 523
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1158-1315 |
1.86e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.00 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLgmalfrlVEPMAGRILIDGVDICSIGL------------EDLR---------- 1215
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTL-------LRHLSGLITGDKSAGSHIELlgrtvqregrlaRDIRksrantgyif 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1216 ------SKLSVIP-----------------------QDPVLLSGTIRFNLDPFDRHT------DQQIWDALERTFLTKA- 1259
Cdd:PRK09984 93 qqfnlvNRLSVLEnvligalgstpfwrtcfswftreQKQRALQALTRVGMVHFAHQRvstlsgGQQQRVAIARALMQQAk 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1260 IILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKV 1315
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1161-1315 |
1.95e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQD----------PV--- 1226
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqssglyldaPLawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 ---LLSGTIRFNLDP------FDR----------HTDQQIwdaleRT---------FLTK------AIILIDEATASIDM 1272
Cdd:PRK15439 362 vcaLTHNRRGFWIKParenavLERyrralnikfnHAEQAA-----RTlsggnqqkvLIAKcleaspQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21729876 1273 ETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1315
Cdd:PRK15439 437 SARNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1157-1341 |
1.98e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.87 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPVLLS--- 1229
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLShlt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1230 ------------GT-------------IRFNL-DPFDRHTDQQIWDALERTFLTKA------IILIDEATASIDM---ET 1274
Cdd:PRK10535 103 aaqnvevpavyaGLerkqrllraqellQRLGLeDRVEYQPSQLSGGQQQRVSIARAlmnggqVILADEPTGALDShsgEE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1275 DTLIQRTIREafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEfDRPEVLRKKPGSLFAALMATATS 1341
Cdd:PRK10535 183 VMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPAQEKVNVAGGTEPVVNTASG 246
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
527-692 |
2.26e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMH--LLEGSVGVQGSlaYVPQQAWIVSGNIRENILMggaYDKARYL 604
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNR--KPTKQILKRTGFVTQDDIL---YPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 605 QVLHCCSLNRDLELLPFGDMTE-----IGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILvaesvISELGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*..
gi 21729876 666 AHVGKHIFEECIKKTLRGKTVVLVTHQ 692
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1158-1316 |
2.27e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI-CSIGLEDLRSKLSVIPQD-PVLLSGTIRFN 1235
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1236 L--------DPFDRHTD-----QQIWDALE-----------------------RTFLTKA-IILIDEATASI-DMETDTL 1277
Cdd:PRK10982 94 MwlgryptkGMFVDQDKmyrdtKAIFDELDididprakvatlsvsqmqmieiaKAFSYNAkIVIMDEPTSSLtEKEVNHL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21729876 1278 --IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1316
Cdd:PRK10982 174 ftIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
533-698 |
3.61e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 533 VVSKGMMLGVCGNTGSGKS---SLLS-----------------AILE-----EMH-----LLEGSVGVQGSLAYVPQQAW 582
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTtavKILSgelipnlgdyeeepswdEVLKrfrgtELQnyfkkLYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 583 IVSGNIREnILMG----GAYDkarylqvlhccslnrdlELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK13409 175 VFKGKVRE-LLKKvderGKLD-----------------EVVERLGLENILDRDIsELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 658 DDPLSAVDahvgkhIFE-----ECIKKTLRGKTVVLVTHQLQYLEF 698
Cdd:PRK13409 237 DEPTSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDLAVLDY 276
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
889-1069 |
3.87e-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: 43.94 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 889 RKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSeQFL-------VLSLMVIAVLLIVSVLSpy 961
Cdd:cd18584 66 ARVKAELRRRLLARLLALGPALLRRQSSGELATLL---TEGVDALDGYFA-RYLpqlvlaaIVPLLILVAVFPLDWVS-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 962 illmgAIIMVICF---IYYMMFkkaIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAq 1032
Cdd:cd18584 140 -----ALILLVTApliPLFMIL---IGKAaqaasrRQWAALSR--LSGHFLDRLRGLPTLKLFGRARAQAARIARASED- 208
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21729876 1033 nnylllFLSSTrwMA-LRLEIMTNLV-----TLAVALfVAFGI 1069
Cdd:cd18584 209 ------YRRRT--MKvLRVAFLSSAVleffaTLSIAL-VAVYI 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
527-733 |
3.92e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.62 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILE----EMhLLEGSV------------GVqgslAYVPQQAWIVSG- 586
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLmkiLSGVYQpdsgEI-LLDGEPvrfrsprdaqaaGI----AIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 587 NIRENILMG------GAYDK----ARYLQVLHCCSLNRDLEllpfgdmTEIGErglnLSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1129 95 SVAENIFLGreprrgGLIDWramrRRARELLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 657 LDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELmqkkgKYAQLIQKM 733
Cdd:COG1129 164 LDEPTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL-----TEDELVRLM 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1156-1322 |
4.20e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.73 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL-EDLRSKLSVIPQDPVLLSG---- 1230
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlsvy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1231 -------TIRFNLDPFDR--------------HTDQQIWDAL-----ERTFLTKAI------ILIDEATASIDMETDTLI 1278
Cdd:PRK10895 97 dnlmavlQIRDDLSAEQRedranelmeefhieHLRDSMGQSLsggerRRVEIARALaanpkfILLDEPFAGVDPISVIDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 1279 QRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1322
Cdd:PRK10895 177 KRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPT 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
635-668 |
5.12e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 5.12e-04
10 20 30
....*....|....*....|....*....|....
gi 21729876 635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
525-667 |
5.45e-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: 43.19 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhlleGSVGVQ-GSLAYVPQQAWI--VSGNIREnIL------MG 595
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIY-------GNYLPDsGSILVRHDGGWVdlAQASPRE-ILalrrrtIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 596 ------------GAYD----KARYLQVLHCCSLNRDLELLpfgDMTEIGERGLNL-----SGGQKQRISLARAVYSDRQI 654
Cdd:COG4778 97 yvsqflrviprvSALDvvaePLLERGVDREEARARARELL---ARLNLPERLWDLppatfSGGEQQRVNIARGFIADPPL 173
|
170
....*....|...
gi 21729876 655 YLLDDPLSAVDAH 667
Cdd:COG4778 174 LLLDEPTASLDAA 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1158-1314 |
5.82e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK--------LSVIPQDPV 1226
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHGtyeGEIIFEGEELQASNIRDTERAgiaiihqeLALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 L--------------------------LSGTIRFNLDPFDRHTD-----QQ---IWDALERtfltKAIILI-DEATASI- 1270
Cdd:PRK13549 100 LeniflgneitpggimdydamylraqkLLAQLKLDINPATPVGNlglgqQQlveIAKALNK----QARLLIlDEPTASLt 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21729876 1271 DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1314
Cdd:PRK13549 176 ESETAVLldIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
860-1070 |
6.78e-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: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 860 SFYQLVYGLNALLL--ICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAgDLEQLDQ----- 932
Cdd:cd18566 40 TLQVLVIGVVIAILleSLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREfltgq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 933 -LLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGAIIMVICFIYYMMfKKAIGvfKRLENYSRSplFSHILNSLQGLSS 1011
Cdd:cd18566 119 aLLALLDLPFVLIFLGLIWYLGGKLVLVP-LVLLGLFVLVAILLGPIL-RRALK--ERSRADERR--QNFLIETLTGIHT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1012 IHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRwMALRLEIMTNLVT-LAVALFVAFGIS 1070
Cdd:cd18566 193 IKAMAMEPQMLRRYERL---QANAAYAGFKVAK-INAVAQTLGQLFSqVSMVAVVAFGAL 248
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
917-1093 |
8.03e-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: 42.85 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 917 GRLLNCFAGDLEQLDQL-LPIFSEqFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-----VICFIYYMMfKKAIGVFKRl 990
Cdd:cd18585 92 GDLLNRIVADIDTLDNLyLRVLSP-PVVALLVILATILFLAFFSPALALILLAGLllagvVIPLLFYRL-GKKIGQQLV- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 991 enYSRSPLFSHILNSLQGLSSIHVYGKTEdfiSQFKRLTDAQNNYL--------LLFLSSTrWMALRLEIMTNLVTLAVA 1062
Cdd:cd18585 169 --QLRAELRTELVDGLQGMAELLIFGALE---RQRQQLEQLSDALIkeqrrlarLSGLSQA-LMILLSGLTVWLVLWLGA 242
|
170 180 190
....*....|....*....|....*....|....*.
gi 21729876 1063 LFVAFGISSTPY----SFKVMAV-NIVLQLASSFQA 1093
Cdd:cd18585 243 PLVQNGALDGALlamlVFAVLASfEAVAPLPLAFQY 278
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
634-754 |
8.35e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIkkTLRGK---TVVLVTHQLQYL-EFCGQIILLENGK 709
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL--ELQQKenmALVLITHDLALVaEAAHKIIVMYAGQ 231
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 21729876 710 ICENGTHSELMQK-KGKYAQLIQKmhkeATSDMLQDTAKIAEKPKV 754
Cdd:PRK11022 232 VVETGKAHDIFRApRHPYTQALLR----ALPEFAQDKARLASLPGV 273
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1141-1208 |
9.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.81 E-value: 9.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1141 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS 1208
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS 73
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1159-1253 |
1.03e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1159 HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSVIPQDP---VLLSGT--IR 1233
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPgikTELTALenLR 96
|
90 100
....*....|....*....|
gi 21729876 1234 FNLDPFDRHTDQQIWDALER 1253
Cdd:PRK13538 97 FYQRLHGPGDDEALWEALAQ 116
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
883-1069 |
1.06e-03 |
|
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: 42.50 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 883 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNcFAGDLEQLDQLLpifSEQFLVL---SLMVIAVLLIVSVLS 959
Cdd:cd18555 65 IIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLF-RANSNVYIRQIL---SNQVISLiidLLLLVIYLIYMLYYS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 960 PYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLtdaQNNYLLLF 1039
Cdd:cd18555 141 PLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENL---FKKQLKAF 217
|
170 180 190
....*....|....*....|....*....|
gi 21729876 1040 LSSTRWMALRLEIMTNLVTLAVALFVAFGI 1069
Cdd:cd18555 218 KKKERLSNILNSISSSIQFIAPLLILWIGA 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
634-720 |
1.13e-03 |
|
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: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKI 710
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKI 506
|
90
....*....|
gi 21729876 711 CENGTHSELM 720
Cdd:TIGR03269 507 VKIGDPEEIV 516
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
855-1069 |
1.20e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 42.45 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 855 DNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLL 934
Cdd:cd18545 35 DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 935 -----PIFSEQFLVlsLMVIAVLLIVSV-LSpyiLLMGAIIMVICFIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQG 1008
Cdd:cd18545 115 sngliNLIPDLLTL--VGIVIIMFSLNVrLA---LVTLAVLPLLVLVVFLLRRRARKAWQRVRK-KISNLNAYLHESISG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1009 LSSIHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 1069
Cdd:cd18545 189 IRVIQSFAREDENEEIFDEL---NRENRKANMRAVRLNALFWPLVELISALGTALVYWYGG 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1141-1225 |
1.30e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 42.41 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1141 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 1213
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90
....*....|..
gi 21729876 1214 LRSKLSVIPQDP 1225
Cdd:PRK13643 82 VRKKVGVVFQFP 93
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
634-723 |
1.32e-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: 42.89 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 712
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKG 483
|
90
....*....|.
gi 21729876 713 NGTHSELMQKK 723
Cdd:TIGR02633 484 DFVNHALTQEQ 494
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
893-1068 |
1.34e-03 |
|
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: 42.27 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 893 TALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVI 972
Cdd:cd18561 69 QHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 973 CFIYYMMFKKAIGvfKRLENY--SRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnylllFLSSTRWM---- 1046
Cdd:cd18561 149 IPLSPALWDRLAK--DTGRRHwaAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAED-------LRQATMKVlavs 219
|
170 180
....*....|....*....|..
gi 21729876 1047 ALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18561 220 LLSSGIMGLATALGTALALGVG 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1149-1206 |
1.62e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 42.24 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21729876 1149 KYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGVDI 1206
Cdd:PRK09452 22 KSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDI 78
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
527-709 |
1.63e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQAWIV-SGNIREN 591
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELNLVlQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 592 ILMGgaydkaRY----LQVLHCcSLNRDLELLpFGDM---TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK10982 94 MWLG------RYptkgMFVDQD-KMYRDTKAI-FDELdidIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21729876 665 DAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGK 709
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1156-1228 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK-LSVIPQDPVLL 1228
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLV 90
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
601-703 |
1.76e-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: 41.83 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 601 ARYLQVLHccslnrDLELlpfgDMTEIGERGLNLSGGQKQRISLARAVY---SDRQIYLLDDPLSAVDAHVGKHIFEECI 677
Cdd:cd03271 147 ARKLQTLC------DVGL----GYIKLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQ 216
|
90 100
....*....|....*....|....*.
gi 21729876 678 KKTLRGKTVVLVTHQLQYLEFCGQII 703
Cdd:cd03271 217 RLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1161-1225 |
1.88e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-P---MAGRILIDGVDICSIGLEDLR----SKLSVIPQDP 1225
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDP 98
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1157-1200 |
2.01e-03 |
|
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: 42.48 E-value: 2.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 21729876 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLV---EPMAGRIL 1200
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRII 60
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
610-778 |
2.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 610 CSLNrdLELLPFGdmteigeRGL-NLSGGQKQRISLARAVYSDRQ---IYLLDDPLSAVDAHVGKHIFEECIKKTLRGKT 685
Cdd:PRK00635 794 CSLG--LDYLPLG-------RPLsSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHT 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 686 VVLVTHQLQYLEFCGQIILL------ENGKICENGTHSELMQKKGKYAQLIQKMHKEAtsdmlQDTAKIAEKPKVESQAL 759
Cdd:PRK00635 865 VVIIEHNMHVVKVADYVLELgpeggnLGGYLLASCSPEELIHLHTPTAKALRPYLSSP-----QELPYLPDPSPKPPVPA 939
|
170 180
....*....|....*....|....*
gi 21729876 760 ATSLEESLNGN------AVPEHQLT 778
Cdd:PRK00635 940 DITIKNAYQHNlkhidlSLPRNALT 964
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
853-976 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 853 IADNPQLSFYQLVYGLnALLLICVGVCS---SGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQ 929
Cdd:cd18572 27 VADGSREAFYRAVLLL-LLLSVLSGLFSglrGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQK 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 21729876 930 LDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VICFIY 976
Cdd:cd18572 106 VSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVpVIALIT 153
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
635-744 |
2.27e-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: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICEN 713
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEaLCTRLAIMVKGAFQCL 2151
|
90 100 110
....*....|....*....|....*....|.
gi 21729876 714 GTHSELMQKKGKYAQLIQKMhKEATSDMLQD 744
Cdd:TIGR01257 2152 GTIQHLKSKFGDGYIVTMKI-KSPKDDLLPD 2181
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
632-693 |
2.32e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 2.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21729876 632 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlrGKTVVLVTHQL 693
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNRV---GVTVLMATHDI 197
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1158-1225 |
2.45e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.87 E-value: 2.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDP 1225
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNP 101
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1140-1199 |
2.66e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.61 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21729876 1140 EIIFQDYHMKYRDNTPT---VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRI 1199
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1144-1288 |
2.88e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1144 QDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF--RLVEPMAGRILIDGVDICSIGLEDlRSKLSVI 1221
Cdd:PRK09580 5 KDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIF 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21729876 1222 P--QDPVLLSGT-----IRFNLDPFDRHTDQqiwDALERTFLTKaiiLIDEATASIDMETDtLIQRTIREAFQG 1288
Cdd:PRK09580 82 MafQYPVEIPGVsnqffLQTALNAVRSYRGQ---EPLDRFDFQD---LMEEKIALLKMPED-LLTRSVNVGFSG 148
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1158-1317 |
2.93e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.06 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI---DGVDICSIGLED------LRSKLSVIPQDPV-- 1226
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrrlLRTEWGFVHQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1227 --------------LLS------GTIR---------FNLDPfDRHTDQ------------QIwdalERTFLTKA-IILID 1264
Cdd:PRK11701 102 lrmqvsaggnigerLMAvgarhyGDIRatagdwlerVEIDA-ARIDDLpttfsggmqqrlQI----ARNLVTHPrLVFMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 1265 EATASIDMETDT----LIQRTIREafQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE 1317
Cdd:PRK11701 177 EPTGGLDVSVQArlldLLRGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
850-1068 |
3.00e-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: 41.32 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 850 LGNIADNPQLSFYQLVYGLNALLLICV----GVCSSG---IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 922
Cdd:cd18576 19 AGQLIDAALGGGDTASLNQIALLLLGLfllqAVFSFFriyLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 923 FAGDLEQLDQ----LLPIFSEQFLVLslmVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVFKRLENYSR--- 995
Cdd:cd18576 99 LSNDVTQIQDtlttTLAEFLRQILTL---IGGVVLLFFISWKLTLLMLATVPVVVLV-------AVLFGRRIRKLSKkvq 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 996 ---SPLFSHILNSLQGLSSIHVYGKtEDF-ISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18576 169 delAEANTIVEETLQGIRVVKAFTR-EDYeIERYRKALER---VVKLALKRARIRALFSSFIIFLLFGAIVAVLWYG 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1158-1314 |
3.18e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED--------LRSKLSVIPQ------ 1223
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLIPQltiaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1224 -----DPVLLSGTI--------------RFNLdPFDRHT--------DQQ---IWDALerTFLTKAIILiDEAT-ASIDM 1272
Cdd:PRK10762 100 iflgrEFVNRFGRIdwkkmyaeadkllaRLNL-RFSSDKlvgelsigEQQmveIAKVL--SFESKVIIM-DEPTdALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21729876 1273 ETDTLIqRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1314
Cdd:PRK10762 176 ETESLF-RVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1170-1190 |
4.30e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.90 E-value: 4.30e-03
10 20
....*....|....*....|.
gi 21729876 1170 VVGIVGRTGSGKSSLGMALFR 1190
Cdd:COG3596 41 VIALVGKTGAGKSSLINALFG 61
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
634-665 |
4.52e-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: 4.52e-03
10 20 30
....*....|....*....|....*....|..
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1156-1224 |
4.58e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 40.35 E-value: 4.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQD 1224
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1156-1328 |
4.87e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPM-----AGRILIDGVDICSI-GLEDLRSKLSVIPQDP---- 1225
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrySGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPnpfp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 1226 -----VLLSGTIRFNLDPFD--------RHTDQQIWDA---------------------LERTF-LTKAIILIDEATASI 1270
Cdd:PRK14271 115 msimdNVLAGVRAHKLVPRKefrgvaqaRLTEVGLWDAvkdrlsdspfrlsggqqqllcLARTLaVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21729876 1271 DMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1328
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
527-665 |
5.06e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQqawivsG---N-- 587
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------GlgkNly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 588 ----IRENI-----LMG-GAYDKARYLQvlhccSLNRDLELLPFGDmteigeR--GlNLSGGQKQRISLARAVYSDRQIY 655
Cdd:NF033858 91 ptlsVFENLdffgrLFGqDAAERRRRID-----ELLRATGLAPFAD------RpaG-KLSGGMKQKLGLCCALIHDPDLL 158
|
170
....*....|
gi 21729876 656 LLDDPLSAVD 665
Cdd:NF033858 159 ILDEPTTGVD 168
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
635-710 |
5.70e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 5.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21729876 635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTlrgKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNtVVTDILHLHGQKL 419
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
629-722 |
6.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 629 ERGLN-LSGGQKQRISLARAVYSDRQ--IYLLDDP---LSAVDAHvgKHIfeECIKKtLR--GKTVVLVTHQLQYLEFCG 700
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIgiTYILDEPsigLHPQDTH--KLI--NVIKK-LRdqGNTVLLVEHDEQMISLAD 545
|
90 100
....*....|....*....|....*...
gi 21729876 701 QIILLE------NGKICENGTHSELMQK 722
Cdd:PRK00635 546 RIIDIGpgagifGGEVLFNGSPREFLAK 573
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
895-1068 |
6.34e-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: 40.10 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 895 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICF 974
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 975 IYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMT 1054
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVN 237
|
170
....*....|....
gi 21729876 1055 NLVTLAVALFVAFG 1068
Cdd:cd18554 238 TITDLAPLLVIGFA 251
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
895-1031 |
6.57e-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: 40.19 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 895 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VIC 973
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVpLVV 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 21729876 974 FIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA 1031
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWR-RWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1161-1209 |
6.98e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 40.59 E-value: 6.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 21729876 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI 1209
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV 86
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
634-720 |
8.95e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.77 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21729876 634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINlmlELQEK--QGISYIYVTQHLGMMKhISDQVLVMHQGE 227
|
90
....*....|.
gi 21729876 710 ICENGTHSELM 720
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
523-561 |
9.37e-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: 9.37e-03
10 20 30
....*....|....*....|....*....|....*....
gi 21729876 523 LGPELHKINLVvSKGMMLgVCGNTGSGKSSLLSAILEEM 561
Cdd:COG2805 113 LPPVLKELAEL-PRGLVL-VTGPTGSGKSTTLAAMIDYI 149
|
|
| |
