|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
45-1168 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 877.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 45 PVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQC 124
Cdd:PLN03130 425 PFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 125 VQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFHLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEA 204
Cdd:PLN03130 505 VQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 205 SVAVDRFKSLFLMEEVHMIKNKPASPHI-KIEMKNATLAWDSShssiqnspkltpkmkkdkratrgkkeksrqlqhtehq 283
Cdd:PLN03130 585 NVSLKRLEELLLAEERVLLPNPPLEPGLpAISIKNGYFSWDSK------------------------------------- 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 284 avlaeqkghllldsDERPspeeeegkqihtgslrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQM-TLLEGS 362
Cdd:PLN03130 628 --------------AERP-------------------TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDAS 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 363 IAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARA 442
Cdd:PLN03130 675 VVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARA 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 443 LYSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdya 522
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG--- 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 523 TIFNNLL-----LGET--PPVEINSKKEATGSQKSQDKGPKPGSVKKEKAVKSEEGQLVQVEEKGQGSVPWSVYWVYIQA 595
Cdd:PLN03130 831 PLFQKLMenagkMEEYveENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNA 910
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 596 AGGplaFLVIMVLFMLNVGSTAF---STWWLSYWIKQGSGNStvyqgnrsfvsdsmkDNPFmqYYASIYALSMAVMLILK 672
Cdd:PLN03130 911 LGG---AWVVMILFLCYVLTEVFrvsSSTWLSEWTDQGTPKT---------------HGPL--FYNLIYALLSFGQVLVT 970
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 673 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNV---ILVFFCVGM 749
Cdd:PLN03130 971 LLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIfqlLSTFVLIGI 1050
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 750 IAGVFPWflvAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYnKRQEFLHRYQELLDDNQA 829
Cdd:PLN03130 1051 VSTISLW---AIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAY-KAYDRMAEINGRSMDNNI 1126
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 830 PFFLFT-CAMRWLAVRLDLISIALITTTGLMIVLMHGQI--PSAYA---GLAISYAVQLTGLFQFTVRLASETEARFTSV 903
Cdd:PLN03130 1127 RFTLVNmSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAenQAAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAV 1206
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 904 ERINHYIKtLSLEAPARIKNKAPPHDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL 983
Cdd:PLN03130 1207 ERVGTYID-LPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNAL 1285
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 984 FRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLE 1063
Cdd:PLN03130 1286 FRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLD 1365
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1064 SEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVL 1143
Cdd:PLN03130 1366 AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVL 1445
|
1130 1140
....*....|....*....|....*
gi 1720387222 1144 AQGQVVEFDTPSVLLSNDSSRFYAM 1168
Cdd:PLN03130 1446 DAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-1168 |
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: 869.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 16 SLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAAT 95
Cdd:TIGR00957 413 TVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 96 DDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFH--LT 173
Cdd:TIGR00957 493 DNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLD 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 174 AAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEV--HMIKNKPASP--HIKIEMKNATLAWDSshss 249
Cdd:TIGR00957 573 AEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELepDSIERRTIKPgeGNSITVHNATFTWAR---- 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 250 iqnspkltpkmkkdkratrgkkeksrqlqhtehqavlaeqkghllldsDERPspeeeegkqihtgslrlqrTLYNIDLEI 329
Cdd:TIGR00957 649 ------------------------------------------------DLPP-------------------TLNGITFSI 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 330 EEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRP 409
Cdd:TIGR00957 662 PEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLP 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 410 DLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKR--LKSKTVLFVTHQ 487
Cdd:TIGR00957 742 DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvLKNKTRILVTHG 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 488 LQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGET--------PPVEINSKKEA--------------- 544
Cdd:TIGR00957 822 ISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQqghledswTALVSGEGKEAkliengmlvtdvvgk 901
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 545 -------TGSQKSQDKGPKPGSVKK-EKA-VKSEEGQLVQVEEKGQGSVPWSVYWVYIQAAGGPLAFLVIMvLFMLNVGS 615
Cdd:TIGR00957 902 qlqrqlsASSSDSGDQSRHHGSSAElQKAeAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIF-LFVCNHVS 980
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 616 TAFSTWWLSYWIKQGSGNSTvyQGNRSFVSDSMKDNPFMQYYAsIYALSMAVMLilkairgvvfvkGTLRASSRLHDELF 695
Cdd:TIGR00957 981 ALASNYWLSLWTDDPMVNGT--QNNTSLRLSVYGALGILQGFA-VFGYSMAVSI------------GGIQASRVLHQDLL 1045
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 696 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLLILFSLLHIVS 775
Cdd:TIGR00957 1046 HNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFY 1125
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 776 RVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITT 855
Cdd:TIGR00957 1126 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1205
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 856 TGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTlSLEAPARIKNKAPPHDWPQEGE 935
Cdd:TIGR00957 1206 AALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGR 1284
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAI 1015
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILI 1095
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1096 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNdSSRFYAM 1168
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ-RGIFYSM 1516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-1168 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 805.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 18 GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDD 97
Cdd:PLN03232 398 GKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 98 RVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKA---GYFQSITVGVAPIVVviaSVVTFSVHMTLGFHLTA 174
Cdd:PLN03232 478 RVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAqllSAFNSFILNSIPVVV---TLVSFGVFVLLGGDLTP 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 175 AQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPHI-KIEMKNATLAWDSshssiqns 253
Cdd:PLN03232 555 ARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGApAISIKNGYFSWDS-------- 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 254 pkltpkmkkdkratrgKKEKSrqlqhtehqavlaeqkghllldsderpspeeeegkqihtgslrlqrTLYNIDLEIEEGK 333
Cdd:PLN03232 627 ----------------KTSKP----------------------------------------------TLSDINLEIPVGS 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 334 LVGICGSVGSGKTSLVSAILGQMTLLE-GSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLA 412
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLD 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 413 ILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLV 492
Cdd:PLN03232 725 LLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLP 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 493 DCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLlgetppvEINSKKEATGSQKSQD-----KGPKP---------G 558
Cdd:PLN03232 805 LMDRIILVSEGMIKEEGTFAELSK-SG---SLFKKLM-------ENAGKMDATQEVNTNDenilkLGPTVtidvsernlG 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 559 SVKKEKAVKSeegQLVQVEEKGQGSVPWSVYWVYIQAAGGplaFLVIMVLFMLNVGSTAF---STWWLSYWIKQGSGNSt 635
Cdd:PLN03232 874 STKQGKRGRS---VLVKQEERETGIISWNVLMRYNKAVGG---LWVVMILLVCYLTTEVLrvsSSTWLSIWTDQSTPKS- 946
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 636 vYQGNrsfvsdsmkdnpfmqYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRIL 715
Cdd:PLN03232 947 -YSPG---------------FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVI 1010
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 716 NRFSKDMDEVDVRLPFQAEMFIQ---NVILVFFCVGMIAGVFPWflvAVGPLLILFSLLHIVSRVLIRELKRLDNITQSP 792
Cdd:PLN03232 1011 NRFSKDIGDIDRNVANLMNMFMNqlwQLLSTFALIGTVSTISLW---AIMPLLILFYAAYLYYQSTSREVRRLDSVTRSP 1087
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 793 FLSHITSSIQGLATIHAYnKRQEFLHRYQELLDDNQAPFFLFTCAM-RWLAVRLDLISIALITTTGLMIVLMHGQIP--- 868
Cdd:PLN03232 1088 IYAQFGEALNGLSSIRAY-KAYDRMAKINGKSMDNNIRFTLANTSSnRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqa 1166
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 869 --SAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKAPPHDWPQEGEVTFENAEMRYR 946
Cdd:PLN03232 1167 gfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID-LPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYR 1245
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 947 ENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGT 1026
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGT 1325
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1027 VRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTE 1106
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1107 TDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1168
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRM 1467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-1177 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 659.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 14 EKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 93
Cdd:PTZ00243 340 DMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 94 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSIT--VGVAPIVVVIASVvtFSVHMTLGFH 171
Cdd:PTZ00243 420 AADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATsfVNNATPTLMIAVV--FTVYYLLGHE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 172 LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFkSLFL------------MEE-VHMIKNKPASPHIKIEMKN 238
Cdd:PTZ00243 498 LTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRI-STFLecdnatcstvqdMEEyWREQREHSTACQLAAVLEN 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 239 AtlawdSSHSSIQNSPKLTPKMKKD--KRATR-----GKKEKSRQLQHTEH---------QAVLAEQKGHLLLDSDERPS 302
Cdd:PTZ00243 577 V-----DVTAFVPVKLPRAPKVKTSllSRALRmlcceQCRPTKRHPSPSVVvedtdygspSSASRHIVEGGTGGGHEATP 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 303 PEEEEGKQIHTGS-----LRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAW 377
Cdd:PTZ00243 652 TSERSAKTPKMKTddffeLEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAW 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:PTZ00243 732 IMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 458 ALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlngdyATIFNNLLLGET---P 534
Cdd:PTZ00243 812 ALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-----TSLYATLAAELKenkD 886
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 535 PVEINSKKEATGSQKSQDKG--PKPGSVKKEKAVKSEE--------GQLVQVEEKGQGSVPWSVYWVYIQAAGGPLAFLV 604
Cdd:PTZ00243 887 SKEGDADAEVAEVDAAPGGAvdHEPPVAKQEGNAEGGDgaaldaaaGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGF 966
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 605 IMVLFMLNVGSTAFSTWWLSYWIKQGSGNS-----TVYQGnrsFVSDSMKDNPFmQYYASIYALSmavmlilkairgvvf 679
Cdd:PTZ00243 967 VLATFAVTELVTVSSGVWLSMWSTRSFKLSaatylYVYLG---IVLLGTFSVPL-RFFLSYEAMR--------------- 1027
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 680 vkgtlRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPfqaeMFIQNVILVFF--CVGMIAGVF--P 755
Cdd:PTZ00243 1028 -----RGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLP----MSYLYLLQCLFsiCSSILVTSAsqP 1098
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 756 WFLVAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKR----QEFLHRyqelLDDNQAPF 831
Cdd:PTZ00243 1099 FVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAhlvmQEALRR----LDVVYSCS 1174
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 832 FLFTCAMRWLAVRLDLIS------IALITTTGLMIVLMHGQIpsAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVER 905
Cdd:PTZ00243 1175 YLENVANRWLGVRVEFLSnivvtvIALIGVIGTMLRATSQEI--GLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVER 1252
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 906 INHYIKTLSLEA-----------------------PARIKNKAPPHDWP---QEGEVTFENAEMRYRENLPLVLKKVSFT 959
Cdd:PTZ00243 1253 LLYYTDEVPHEDmpeldeevdalerrtgmaadvtgTVVIEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFR 1332
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 960 IKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFNQYTE 1039
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS 1412
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1040 DQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL-DEATAAMDTETDLLIQETIREA 1118
Cdd:PTZ00243 1413 AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSA 1492
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1119 FADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENKVA 1177
Cdd:PTZ00243 1493 FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGRSEA 1551
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
598-910 |
1.41e-178 |
|
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: 526.36 E-value: 1.41e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 598 GPLAFLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVYQGNRSFVSDSMKDNPFMQYYASIYALSMAVMLILKAIRGV 677
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 678 VFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWF 757
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 758 LVAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCA 837
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 838 MRWLAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 910
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-1173 |
2.06e-155 |
|
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: 502.90 E-value: 2.06e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 16 SLGELINICSNDGQRMFEAAAVGSLLAGGPVVAIL--GMIYNviILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 93
Cdd:TIGR01271 177 STGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILlmGLIWE--LLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 94 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAG---YFQSITVGVAPIVVVIASVVTFSVHMTLGF 170
Cdd:TIGR01271 255 KISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAylrYFYSSAFFFSGFFVVFLSVVPYALIKGIIL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 171 HltaaQAFTvvTVFNSMTFALKVT---PFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPhiKIEMKNATLAWDSSH 247
Cdd:TIGR01271 335 R----RIFT--TISYCIVLRMTVTrqfPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTT--EVEMVNVTASWDEGI 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 248 SSIqnspkltpkmkkdkratrgkKEKSRQlqhtehqavlaeqkghlllDSDERPSPEEEEGKQIHTGSLRLQRTLYNIDL 327
Cdd:TIGR01271 407 GEL--------------------FEKIKQ-------------------NNKARKQPNGDDGLFFSNFSLYVTPVLKNISF 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 328 EIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCL 407
Cdd:TIGR01271 448 KLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQL 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 408 RPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQ 487
Cdd:TIGR01271 528 EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSK 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 488 LQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF-------------NNLLLGET--------------------- 533
Cdd:TIGR01271 608 LEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerRNSILTETlrrvsidgdstvfsgpetikq 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 534 ----PPVEINSKKEA-----------------TGSQKSQ-----DKGPKPGSVKKEKAVKSEEG---------------- 571
Cdd:TIGR01271 688 sfkqPPPEFAEKRKQsiilnpiasarkfsfvqMGPQKAQattieDAVREPSERKFSLVPEDEQGeeslprgnqyhhglqh 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 572 ---------QLVQVEEKGQG----------------------------------------------------------SV 584
Cdd:TIGR01271 768 qaqrrqsvlQLMTHSNRGENrreqlqtsfrkkssitqqnelaseldiysrrlskdsvyeiseeineedlkecfadereNV 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 585 P----WSVYWVYIqAAGGPLAFLVI--MVLFMLNVGSTAFSTWWLSywikqGSGNSTVYQGNRSfVSDSMKDNPF----- 653
Cdd:TIGR01271 848 FetttWNTYLRYI-TTNRNLVFVLIfcLVIFLAEVAASLLGLWLIT-----DNPSAPNYVDQQH-ANASSPDVQKpviit 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 654 --MQYYA-SIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLP 730
Cdd:TIGR01271 921 ptSAYYIfYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLP 1000
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 731 FQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAY 810
Cdd:TIGR01271 1001 LTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAF 1080
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 811 NKRQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPSAyAGLAISYAVQLTGLFQFTV 890
Cdd:TIGR01271 1081 GRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGE-VGIILTLAMNILSTLQWAV 1159
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 891 RLASETEARFTSVERINHYI-------------KTLSLEAPARIKNKAPPHDWPQEGEVTFENAEMRYRENLPLVLKKVS 957
Cdd:TIGR01271 1160 NSSIDVDGLMRSVSRVFKFIdlpqeeprpsgggGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLS 1239
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 958 FTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFNQY 1037
Cdd:TIGR01271 1240 FSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQW 1318
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1038 TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE 1117
Cdd:TIGR01271 1319 SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 1118 AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMFAAAE 1173
Cdd:TIGR01271 1399 SFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSAAD 1453
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
934-1154 |
4.76e-137 |
|
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: 414.58 E-value: 4.76e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 934 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKL 1013
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1093
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1094 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1154
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
656-1171 |
1.82e-115 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 371.03 E-value: 1.82e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 656 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 735
Cdd:COG1132 62 LLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 736 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLLILFSLLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQ 814
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRLaLIVLLVLPLLLLVLRLFGR-RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 815 EFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLI---SIALITTTGLMIVLmHGQIPSAYAGLAISYAVQLTGLFQFTVR 891
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALVLLVGGLLVL-SGSLTVGDLVAFILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 892 LASETEARFTSVERINHYiktlsLEAPARIKNKAPPHD-WPQEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVG 970
Cdd:COG1132 300 VLNQLQRALASAERIFEL-----LDEPPEIPDPPGAVPlPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 971 RTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALE 1047
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1048 RTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI 1127
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1720387222 1128 AHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFAA 1171
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELLARG-GLYARLYRL 574
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
321-503 |
3.22e-109 |
|
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: 340.22 E-value: 3.22e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNS 400
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 401 VLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLK-SK 479
Cdd:cd03250 100 VIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNK 179
|
170 180
....*....|....*....|....
gi 1720387222 480 TVLFVTHQLQYLVDCDEVIFMKEG 503
Cdd:cd03250 180 TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
602-910 |
6.11e-104 |
|
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: 329.46 E-value: 6.11e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVYQGnrsfvsdsmkdnpfmQYYASIYALSMAVMLILKAIRGVVFVK 681
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG---------------YYLGVYAALLVLASVLLVLLRWLLFVL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 682 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 761
Cdd:cd18580 66 AGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 762 GPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWL 841
Cdd:cd18580 146 PPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 842 AVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 910
Cdd:cd18580 226 GLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
14-211 |
1.16e-102 |
|
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: 325.67 E-value: 1.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 14 EKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 93
Cdd:cd18592 90 DKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 94 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFHLT 173
Cdd:cd18592 170 ITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLT 249
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720387222 174 AAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRF 211
Cdd:cd18592 250 AAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
655-1170 |
1.53e-100 |
|
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: 334.88 E-value: 1.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 655 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVR 728
Cdd:COG2274 190 QDLSTLWVLAIGLLLallfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 729 LPFQAEMFIQNVILVFFCVGMIA---GVFPWFLVAVGPLLILFSLL-HIVSRVLIRELKRLDNITQSpflsHITSSIQGL 804
Cdd:COG2274 269 LTGSLLTALLDLLFVLIFLIVLFfysPPLALVVLLLIPLYVLLGLLfQPRLRRLSREESEASAKRQS----LLVETLRGI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 805 ATIHAYNKRQEFLHRYQELLDDNQAPFFlftcAMRWLAVRLDLISIAL--ITTTGLMIV----LMHGQIP-------SAY 871
Cdd:COG2274 345 ETIKALGAESRFRRRWENLLAKYLNARF----KLRRLSNLLSTLSGLLqqLATVALLWLgaylVIDGQLTlgqliafNIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 872 AGLAISYAVQLTGLFQftvRLAsetEARfTSVERINHYIKtLSLEAPARIKNKAPPHdwpQEGEVTFENAEMRYRENLPL 951
Cdd:COG2274 421 SGRFLAPVAQLIGLLQ---RFQ---DAK-IALERLDDILD-LPPEREEGRSKLSLPR---LKGDIELENVSFRYPGDSPP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL 1031
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 ---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1108
Cdd:COG2274 570 tlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1109 LLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 1170
Cdd:COG2274 648 AIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK-GLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
930-1154 |
5.00e-99 |
|
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: 312.81 E-value: 5.00e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 930 WPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADL 1009
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1010 RSKLAIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALerthmkeciaqlplklesEVMENGDNFSVGERQLLCIARALLR 1089
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1090 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1154
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
602-909 |
1.76e-87 |
|
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: 284.76 E-value: 1.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVYQGNRSfvsdsmkdnpfmqYYASIYALSMAVMLILKAIRGVVFVK 681
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRD-------------YRLGVYGALGLGQAIFVFLGSLALAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 682 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 761
Cdd:cd18603 68 GCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 762 GPLLILFsllHIVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAM 838
Cdd:cd18603 148 IPLAILY---FFIQRFYVatsRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSN 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 839 RWLAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 909
Cdd:cd18603 225 RWLAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
602-909 |
1.06e-85 |
|
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: 279.75 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNST-VYQGnrsfvsdsmkdnpfmqyyasIYALSMAVMLILKAIRGVVFV 680
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQgFYIG--------------------IYAGLGVLQAIFLFLFGLLLA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 681 KGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVA 760
Cdd:cd18606 61 YLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 761 VGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRW 840
Cdd:cd18606 141 LPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRW 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 841 LAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 909
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
602-910 |
2.10e-83 |
|
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: 274.02 E-value: 2.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNstvyqgnrsfvsDSMKDNPFMQYYASIYALSMAVMLILKAIRGVVFVK 681
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNS------------FFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 682 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVilvFFCVGMIAGV---FPWFL 758
Cdd:cd18605 69 GGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL---FGLLGYLVVIcyqLPWLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 759 VAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAM 838
Cdd:cd18605 146 LLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 839 RWLAVRLDLISIALITTTGLMIVLMH---GQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 910
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
602-910 |
1.94e-82 |
|
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: 271.26 E-value: 1.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVYQGNRSfvsdsmkdnpfMQYYASIYALSMAVMLILKAIRGVVFVK 681
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVS-----------VLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 682 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 761
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 762 GPLLILFSLlhiVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAM 838
Cdd:cd18604 150 VVLAALYVY---IGRLYLrasRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 839 RWLAVRLDLISIALITTTGLMIVLMHGqIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 910
Cdd:cd18604 227 RWLSVRIDLLGALFSFATAALLVYGPG-IDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
598-909 |
2.84e-79 |
|
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: 263.03 E-value: 2.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 598 GPLAFLVIMVLFMLNVGSTAFSTWWLSYWI----KQGSGNSTVYQGNRSFVSDSMKDNpfmQYYASIYALSMAVMLILKA 673
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWAnleeKLNDTTDRVQGENSTNVDIEDLDR---DFNLGIYAGLTAATFVFGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 674 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGV 753
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 754 FPWFLVAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFL 833
Cdd:cd18601 158 NPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 834 FTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 909
Cdd:cd18601 238 FLATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
934-1165 |
1.80e-77 |
|
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: 255.99 E-value: 1.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 934 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKL 1013
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1093
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1094 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRF 1165
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
592-1161 |
1.72e-74 |
|
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: 258.15 E-value: 1.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 592 YIQAAGGPLAFLVIMVLfmLNVGSTAFSTWWLSYWIkqgsgnSTVYQGNRSFVSdsmkdnpfmqyyASIYALSMAVMLIL 671
Cdd:COG4988 11 LARGARRWLALAVLLGL--LSGLLIIAQAWLLASLL------AGLIIGGAPLSA------------LLPLLGLLLAVLLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 672 KAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV---R-LP--FQAeMFIQNVI 741
Cdd:COG4988 71 RALlawlRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfaRyLPqlFLA-ALVPLLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 742 LVF-FCVGMIAGVFpwfLVAVGPLLILF-SLLHIVSRVLIRelKRLDNITQspfLS-HITSSIQGLATIHAYNKRQEFLH 818
Cdd:COG4988 150 LVAvFPLDWLSGLI---LLVTAPLIPLFmILVGKGAAKASR--RQWRALAR---LSgHFLDRLRGLTTLKLFGRAKAEAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 819 RYQELLDDnqapfflFTCA-MRWLavRLDLISIA---LITTTGLMIV-------LMHGQIpSAYAGLAIsyaVQLTGLFQ 887
Cdd:COG4988 222 RIAEASED-------FRKRtMKVL--RVAFLSSAvleFFASLSIALVavyigfrLLGGSL-TLFAALFV---LLLAPEFF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 888 FTVR-LASETEARFTSV---ERInhyIKTLSLEAPARIKNKAPPhDWPQEGEVTFENAEMRYRENLPlVLKKVSFTIKPK 963
Cdd:COG4988 289 LPLRdLGSFYHARANGIaaaEKI---FALLDAPEPAAPAGTAPL-PAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 964 EKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFN-QYTEDQI 1042
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEEL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1043 WDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC 1122
Cdd:COG4988 444 EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR 523
|
570 580 590
....*....|....*....|....*....|....*....
gi 1720387222 1123 TMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1161
Cdd:COG4988 524 TVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
602-909 |
2.11e-74 |
|
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: 249.06 E-value: 2.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVYQGNrsfvSDSMKDNPFMQYYASIYALSMAVMLILKAIRGVVFVK 681
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNI----TSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 682 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 761
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 762 GPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWL 841
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 842 AVRLDLISiALITTTGLMIVL---MHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 909
Cdd:cd18602 237 GIRLDYLG-AVIVFLAALSSLtaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
683-1170 |
1.29e-70 |
|
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: 247.37 E-value: 1.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 683 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD-----VRLPFqaemfIQNVILVFFCVGMIAGVFPWF 757
Cdd:COG4987 83 TLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrVLLPL-----LVALLVILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 758 LVAVGPLLILFSLL-----HIVSRVLIRELKRLdnitQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQApff 832
Cdd:COG4987 158 ALVLALGLLLAGLLlpllaARLGRRAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 833 lftcAMRWLAvRLDLISIALIT-TTGLMIVLM---------HGQIPSAYAG------LAISYAVQ-LTGLFQFTVRLASe 895
Cdd:COG4987 231 ----AQRRLA-RLSALAQALLQlAAGLAVVAVlwlaaplvaAGALSGPLLAllvlaaLALFEALApLPAAAQHLGRVRA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 896 tearftSVERINHyiktlSLEAPARIKNKAPPHDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSG 975
Cdd:COG4987 305 ------AARRLNE-----LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 976 KSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMK 1052
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1053 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLH 1132
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
490 500 510
....*....|....*....|....*....|....*...
gi 1720387222 1133 TVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 1170
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
934-1158 |
1.84e-69 |
|
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: 232.12 E-value: 1.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 934 GEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKL 1013
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSGTVRSNLDPFNQY-TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1092
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 1093 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLL 1158
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
936-1169 |
2.45e-63 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 215.17 E-value: 2.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAI 1015
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1090
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1091 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMF 1169
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMW 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
657-1175 |
3.33e-63 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 226.14 E-value: 3.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 657 YASIYALSMAVMLILKAIRGvvfvkgtlrassrlhdELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 736
Cdd:TIGR02203 72 FVSTYLLSWVSNKVVRDIRV----------------RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 737 IQNVILVFFCVGMIAgVFPWFLVAVgpLLILFSLLHIVSRVLIRELKRLDNITQSPF--LSHITS-SIQGLATIHAYNKR 813
Cdd:TIGR02203 136 VRETLTVIGLFIVLL-YYSWQLTLI--VVVMLPVLSILMRRVSKRLRRISKEIQNSMgqVTTVAEeTLQGYRVVKLFGGQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 814 QEFLHRYQELlddnqapfflfTCAMRWLAVRLD------------LISIALITTtgLMIVLMHGQIPSAYAGLAISYAVQ 881
Cdd:TIGR02203 213 AYETRRFDAV-----------SNRNRRLAMKMTsagsisspitqlIASLALAVV--LFIALFQAQAGSLTAGDFTAFITA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 882 LTGLFQFTVRLA---SETEARFTSVERINHYIKT-LSLEAPARIKNKApphdwpqEGEVTFENAEMRYRENLPLVLKKVS 957
Cdd:TIGR02203 280 MIALIRPLKSLTnvnAPMQRGLAAAESLFTLLDSpPEKDTGTRAIERA-------RGDVEFRNVTFRYPGRDRPALDSIS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 958 FTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL---DPf 1034
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1035 NQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQET 1114
Cdd:TIGR02203 432 EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAA 511
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1115 IREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAMFAAAENK 1175
Cdd:TIGR02203 512 LERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG--LYAQLHNMQFR 570
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
936-1147 |
7.71e-63 |
|
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: 211.09 E-value: 7.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAI 1015
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILI 1095
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1096 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQ 1147
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
936-1168 |
4.56e-62 |
|
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: 211.32 E-value: 4.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAI 1015
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1090
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1091 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAM 1168
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGG--VYAK 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-526 |
2.16e-61 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 220.81 E-value: 2.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 18 GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTgfLGSAVFILFyPAMMFVSRLTAYFRRKCVAATDD 97
Cdd:COG1132 118 GDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR--LALIVLLVL-PLLLLVLRLFGRRLRKLFRRVQE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 98 RVQKMN----EVLTYIKFIKMYA----WVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIasVVTFSVHMTLG 169
Cdd:COG1132 195 ALAELNgrlqESLSGIRVVKAFGreerELERFREANEELRRANLRAARLSALFFPLMELLGNLGLAL--VLLVGGLLVLS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 170 FHLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLflMEEVHMIKNKPASPHIK-----IEMKNATLAWD 244
Cdd:COG1132 273 GSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL--LDEPPEIPDPPGAVPLPpvrgeIEFENVSFSYP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 245 sshssiqnspkltpkmkkdkratrgkkeksrqlqhtehqavlaeqkghllldsDERPspeeeegkqihtgslrlqrTLYN 324
Cdd:COG1132 351 -----------------------------------------------------GDRP-------------------VLKD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNILFGK 391
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 392 -EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNs 470
Cdd:COG1132 439 pDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE- 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 471 AIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 526
Cdd:COG1132 518 ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
321-503 |
5.08e-61 |
|
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: 207.95 E-value: 5.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVS-----------------GTFAYVAQQAWILNATL 383
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 463
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720387222 464 GNHIFNSAIRKRLK--SKTVLFVTHQLQYLVDCDEVIFMKEG 503
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
915-1150 |
3.41e-60 |
|
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: 218.15 E-value: 3.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 915 LEAPARIKNK--APPHDwPQEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGG 992
Cdd:COG5265 336 LDQPPEVADApdAPPLV-VGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSG 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 993 CIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVM 1067
Cdd:COG5265 414 RILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1068 ENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQ 1147
Cdd:COG5265 490 ERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGR 569
|
...
gi 1720387222 1148 VVE 1150
Cdd:COG5265 570 IVE 572
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
659-1171 |
9.52e-59 |
|
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: 213.02 E-value: 9.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 659 SIYALSMAVMLILKAIRGVVFVKGTL---RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 735
Cdd:TIGR02204 59 RYFAFLLVVALVLALGTAARFYLVTWlgeRVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSM 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 736 FIQNVILVFFCVGMIAGVFP---WFLVAVGPLlILFSLLHIVSRVliRELKRLDNITQSPFLSHITSSIQGLATIHAYNK 812
Cdd:TIGR02204 139 ALRNALMCIGGLIMMFITSPkltSLVLLAVPL-VLLPILLFGRRV--RKLSRESQDRIADAGSYAGETLGAIRTVQAFGH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 813 RQEFLHRYQELLDDNqapfflFTCAMRWLAVRLDLISIAL-ITTTGLMIVL-------MHGQIPSAYAGLAISYAVQLTG 884
Cdd:TIGR02204 216 EDAERSRFGGAVEKA------YEAARQRIRTRALLTAIVIvLVFGAIVGVLwvgahdvIAGKMSAGTLGQFVFYAVMVAG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 885 LFQFTVRLASETEARFTSVERINHYIKTLS-LEAPAriKNKAPPHdwPQEGEVTFENAEMRY--RENLPlVLKKVSFTIK 961
Cdd:TIGR02204 290 SIGTLSEVWGELQRAAGAAERLIELLQAEPdIKAPA--HPKTLPV--PLRGEIEFEQVNFAYpaRPDQP-ALDGLNLTVR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 962 PKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFN-QYTED 1040
Cdd:TIGR02204 365 PGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpDATDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1041 QIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFA 1120
Cdd:TIGR02204 445 EVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1121 DCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSndSSRFYAMFAA 1171
Cdd:TIGR02204 525 GRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA--KGGLYARLAR 573
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
294-519 |
1.15e-56 |
|
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: 206.53 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 294 LLDSDERPSPEEEEGKQIHTG-SLRLQ----------RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGS 362
Cdd:COG4988 314 LLDAPEPAAPAGTAPLPAAGPpSIELEdvsfsypggrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 363 IAVSGT-------------FAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGAN 428
Cdd:COG4988 394 ILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITER 508
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ-ALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
250
....*....|.
gi 1720387222 509 GTHEELMNLNG 519
Cdd:COG4988 553 GTHEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
936-1161 |
1.26e-55 |
|
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: 193.14 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKL 1013
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALL 1088
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1089 RHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1161
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-527 |
3.11e-54 |
|
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: 202.76 E-value: 3.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 15 KSLGELINicsndgqRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGS---AVFILFYPAMMFVSRLTAYFRRKC 91
Cdd:COG2274 250 RSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPplaLVVLLLIPLYVLLGLLFQPRLRRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 92 VAATDDRVQKMN----EVLTYIKFIKMYA--------WVKAFSQCVqKIREEERRILEKAGYFQSITVGVAPIVVVIASV 159
Cdd:COG2274 323 SREESEASAKRQsllvETLRGIETIKALGaesrfrrrWENLLAKYL-NARFKLRRLSNLLSTLSGLLQQLATVALLWLGA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 160 vtFSV---HMTLGfHLTAAQAFtVVTVFNSMT-FALKVTpfsvkSLSEASVAVDRFKSLFLME-EVHMIKNKPASPHIK- 233
Cdd:COG2274 402 --YLVidgQLTLG-QLIAFNIL-SGRFLAPVAqLIGLLQ-----RFQDAKIALERLDDILDLPpEREEGRSKLSLPRLKg 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 234 -IEMKNATLawdsshssiqnspkltpkmkkdkratrgkkeksrqlqhtehqavlaeqkghllldsdeRPSPEEEEgkqih 312
Cdd:COG2274 473 dIELENVSF----------------------------------------------------------RYPGDSPP----- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 313 tgslrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWIL 379
Cdd:COG2274 490 --------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLF 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 380 NATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:COG2274 562 SGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 459 LDAHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 527
Cdd:COG2274 642 LDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
659-1160 |
1.73e-53 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 200.33 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 659 SIYALSM--AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 736
Cdd:TIGR00958 203 AIFFMCLlsIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 737 IQNVILVFFCVGMIAGVFPWF----LVAVGPLLILFSLLHIVSRVLIRELKrlDNITQSPFLSHitSSIQGLATIHAY-N 811
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 812 KRQEfLHRYQELLDDnqapfflftcaMRWLAVRLDLISIALITTTGLM------IVL-------MHGQIPSayaGLAIS- 877
Cdd:TIGR00958 359 EEGE-ASRFKEALEE-----------TLQLNKRKALAYAGYLWTTSVLgmliqvLVLyyggqlvLTGKVSS---GNLVSf 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 878 --YAVQLTGLFQFTVRLASETEARFTSVERINHYI-KTLSLEAPARIknkAPPHDwpqEGEVTFENAEMRY--RENLPlV 952
Cdd:TIGR00958 424 llYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdRKPNIPLTGTL---APLNL---EGLIEFQDVSFSYpnRPDVP-V 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLD 1032
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1033 -PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLI 1111
Cdd:TIGR00958 577 yGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1720387222 1112 QETirEAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:TIGR00958 657 QES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
934-1149 |
4.08e-53 |
|
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: 185.49 E-value: 4.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 934 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKL 1013
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSGTVRSNLDPFNQYTEDQ-IWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1092
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1093 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVV 1149
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
295-531 |
3.03e-52 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 185.06 E-value: 3.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 295 LDSDERPSPEEEEGKQIHTGSLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQ 374
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 375 QAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDD 454
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 455 PLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDyatiFNNLLLG 531
Cdd:cd03291 186 PFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD----FSSKLMG 258
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
934-1163 |
4.76e-52 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 184.29 E-value: 4.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 934 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGIRISDIGLADLRSKL 1013
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-IQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1093
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1094 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSS 1163
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
936-1162 |
1.36e-50 |
|
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: 178.83 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAI 1015
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1092
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1093 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1162
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
14-210 |
1.26e-49 |
|
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: 177.68 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 14 EKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 93
Cdd:cd18579 92 ETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 94 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFHLT 173
Cdd:cd18579 172 ATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNPLT 251
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720387222 174 AAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 210
Cdd:cd18579 252 AAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
324-522 |
4.80e-49 |
|
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: 184.20 E-value: 4.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNILFG 390
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 391 K-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 469
Cdd:COG4987 433 RpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 470 sAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:COG4987 513 -DLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
694-1161 |
8.00e-49 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 184.07 E-value: 8.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 694 LFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD----------VRlpfQAEMFIQNVILVFFcvgmiagvFPWFLVavgp 763
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssgalitvVR---EGASIIGLFIMMFY--------YSWQLS---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 764 lLILFSLLHIVSrVLIREL-KRLDNIT---QSPfLSHITSS----IQGLATIHAYNKRQEFLHRYQELLDDnqapfflft 835
Cdd:PRK11176 169 -LILIVIAPIVS-IAIRVVsKRFRNISknmQNT-MGQVTTSaeqmLKGHKEVLIFGGQEVETKRFDKVSNR--------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 836 caMRWLAVRL---DLIS---IALITTTGLMIVLMHGQIPSAYAGL-AISYAVQLTGLFQFTVRLASETE--ARFtsvERI 906
Cdd:PRK11176 237 --MRQQGMKMvsaSSISdpiIQLIASLALAFVLYAASFPSVMDTLtAGTITVVFSSMIALMRPLKSLTNvnAQF---QRG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 907 NHYIKTL----SLEAPariKNKAPPHDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMA 982
Cdd:PRK11176 312 MAACQTLfailDLEQE---KDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 983 LFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLD--PFNQYTEDQIWDALERTHMKECIAQLPL 1060
Cdd:PRK11176 389 LTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDN 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1061 KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRI 1140
Cdd:PRK11176 469 GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEI 548
|
490 500
....*....|....*....|.
gi 1720387222 1141 MVLAQGQVVEFDTPSVLLSND 1161
Cdd:PRK11176 549 LVVEDGEIVERGTHAELLAQN 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
795-1171 |
4.08e-47 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 179.00 E-value: 4.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 795 SHITSSIQGLATIHAYNKRQ---EFLHRYQELLDDNQAPfflftcAMRWLAVRLDL------ISIALITTTGLMIV---- 861
Cdd:PRK13657 196 AHVSDAIGNVSVVQSYNRIEaetQALRDIADNLLAAQMP------VLSWWALASVLnraastITMLAILVLGAALVqkgq 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 862 LMHGQIPS--AYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEAPARIKnkapphdwpqeGEVTFE 939
Cdd:PRK13657 270 LRVGEVVAfvGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVK-----------GAVEFD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 940 NAEMRYrENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQE 1019
Cdd:PRK13657 339 DVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1020 PVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKIL 1094
Cdd:PRK13657 418 AGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1095 ILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE---FDTpsvlLSNDSSRFYAMFAA 1171
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAALLRA 569
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
662-1143 |
4.48e-47 |
|
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: 177.48 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 662 ALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDvrlPFQAEMFI 737
Cdd:TIGR02857 47 LGALALVLLLRAllgwLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALD---GYFARYLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 738 QNVILVFFCVGMIAGVFP--W----FLVAVGPLLILFSLL--HIVSRVLIRELKRLDNITqspflSHITSSIQGLATIHA 809
Cdd:TIGR02857 124 QLVLAVIVPLAILAAVFPqdWisglILLLTAPLIPIFMILigWAAQAAARKQWAALSRLS-----GHFLDRLRGLPTLKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 810 YNKRqeflHRYQELLDDNQAPF-----------FLFTCAMRWLAVrldlISIALITTT-GLMivLMHGQIPSAYAGLAIS 877
Cdd:TIGR02857 199 FGRA----KAQAAAIRRSSEEYrertmrvlriaFLSSAVLELFAT----LSVALVAVYiGFR--LLAGDLDLATGLFVLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 878 YAVQltglFQFTVR-LASETEARFTSVERINHyIKTLsLEAPARIKNKAPPHDWPQEGEVTFENAEMRYrENLPLVLKKV 956
Cdd:TIGR02857 269 LAPE----FYLPLRqLGAQYHARADGVAAAEA-LFAV-LDAAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 957 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL---DP 1033
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1034 fnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQE 1113
Cdd:TIGR02857 422 --DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
490 500 510
....*....|....*....|....*....|
gi 1720387222 1114 TIREAFADCTMLTIAHRLHTVLGSDRIMVL 1143
Cdd:TIGR02857 500 ALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
699-1169 |
2.14e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.83 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 699 LRSPMKFFDTTPTGRILNRFSKDMdEVdVRlpfqaEMFIQNVILVFFCVGMIAGVfpwfLVAVGPL--------LILFSL 770
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT-EV-IR-----DLYVTVVATVLRSAALIGAM----LVAMFSLdwrmalvaIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 771 LHIV-------SRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYNKRQEFLHRyqeLLDDNQAPFflftcAMR 839
Cdd:PRK10790 178 VLVVmviyqrySTPIVRRVRA--------YLADINDgfneVINGMSVIQQFRQQARFGER---MGEASRSHY-----MAR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 840 WLAVRLD------LISI--ALITTtGLMivLMHGQIPSAYAGLAISYA-VQLTG-----LFQFTVRLASETEArFTSVER 905
Cdd:PRK10790 242 MQTLRLDgfllrpLLSLfsALILC-GLL--MLFGFSASGTIEVGVLYAfISYLGrlnepLIELTTQQSMLQQA-VVAGER 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 906 InhyiktlsLEAPARIKNKAPPHDWP-QEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALF 984
Cdd:PRK10790 318 V--------FELMDGPRQQYGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 985 RLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLES 1064
Cdd:PRK10790 389 GYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1065 EVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLA 1144
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
490 500
....*....|....*....|....*
gi 1720387222 1145 QGQVVEFDTPSVLLSNdSSRFYAMF 1169
Cdd:PRK10790 549 RGQAVEQGTHQQLLAA-QGRYWQMY 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
925-1148 |
1.80e-45 |
|
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: 163.80 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 925 APPHdwpQEGEVTFENAEMRYReNLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRIS 1002
Cdd:cd03248 4 APDH---LKGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1003 DIGLADLRSKLAIIPQEPVLFSGTVRSNLD-PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLL 1081
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1082 CIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1148
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
953-1171 |
5.60e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 169.64 E-value: 5.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG-----GCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTV 1027
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSL------LNALLGflpyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 RSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1104
Cdd:PRK11174 440 RDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1105 TETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE---FDTpsvlLSNDSSRFYAMFAA 1171
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
683-1131 |
2.49e-43 |
|
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: 166.38 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 683 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR--LPfqaemfiqnvILVFFCVGMIA-GVFPW 756
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVRviVP----------AGVALVVGAAAvAAIAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 757 FLVAVGPLLILFSLLH--IVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYNKRQEFLHRYQEL------LD 825
Cdd:TIGR02868 151 LSVPAALILAAGLLLAgfVAPLVSLRAARAAEQALArlrGELAAQLTDALDGAAELVASGALPAALAQVEEAdreltrAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 826 DNQApfflftcamRWLAVRLDLISIALITTTGLMIVL-----MHGQIPSAYagLAISYAVQLT---GLFQFTVRLASETE 897
Cdd:TIGR02868 231 RRAA---------AATALGAALTLLAAGLAVLGALWAggpavADGRLAPVT--LAVLVLLPLAafeAFAALPAAAQQLTR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 898 ARfTSVERINHyiktlSLEAPARIKNKAPPHDWPQ-EGEVTFENAEMRYR-ENLPLVLKKVSFTIKPKEKIGIVGRTGSG 975
Cdd:TIGR02868 300 VR-AAAERIVE-----VLDAAGPVAEGSAPAAGAVgLGKPTLELRDLSAGyPGAPPVLDGVSLDLPPGERVAILGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 976 KSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMK 1052
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLA 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1053 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL 1131
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
685-1159 |
2.63e-43 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 168.98 E-value: 2.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 685 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKdMDEVDVRLpfqAEMFIQNVILVFFC----VGMIAGVFPWFLVA 760
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRIL---SGSTLTTLLSGIFAllnlGLMFYYSWKLALVA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 761 VGPLLILFSLLHIVSRVLIRELKRLDNItQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRW 840
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLEL-SGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 841 LAVrldLISIALITTTGLMIVLMHGQIPSAYAGLA--ISYAVQLTglfQFTVRLASETEARFTSVERINHYIKTLS-LEA 917
Cdd:TIGR03797 361 LTV---FNAVLPVLTSAALFAAAISLLGGAGLSLGsfLAFNTAFG---SFSGAVTQLSNTLISILAVIPLWERAKPiLEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 918 PARIK-NKAPPHDWpqEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSG----- 991
Cdd:TIGR03797 435 LPEVDeAKTDPGKL--SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRL--LLGfetpe 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 992 -GCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENG 1070
Cdd:TIGR03797 507 sGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGG 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1071 DNFSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliQETIREAFA--DCTMLTIAHRLHTVLGSDRIMVLAQGQV 1148
Cdd:TIGR03797 587 GTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRV 662
|
490
....*....|.
gi 1720387222 1149 VEFDTPSVLLS 1159
Cdd:TIGR03797 663 VQQGTYDELMA 673
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
317-503 |
3.94e-43 |
|
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: 154.85 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATL 383
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNILfgkefdeerynsvlnscclrpdlailpnsdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 463
Cdd:cd03228 93 RENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720387222 464 GNHIFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEG 503
Cdd:cd03228 132 EALILE-ALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
322-522 |
5.50e-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: 153.93 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHI 467
Cdd:cd03251 98 YGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 468 FNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:cd03251 177 VQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
322-526 |
8.08e-42 |
|
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: 153.54 E-value: 8.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNIL 388
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKE--FDEERYNSVLnSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 466
Cdd:cd03253 97 YGRPdaTDEEVIEAAK-AAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTERE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 467 IFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 526
Cdd:cd03253 176 IQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
696-1167 |
8.28e-41 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 161.83 E-value: 8.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 696 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemfIQNVIL-VFFCVGMIAGVfPWFLVAVGPLLILFSLLHIV 774
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDA---------LASTILsLFLDMWILVIV-GLFLVRQNMLLFLLSLLSIP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 775 SRVLI-----RELKRLDN---ITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCA---MRWLAV 843
Cdd:TIGR01193 307 VYAVIiilfkRTFNKLNHdamQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAdqgQQAIKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 844 RLDLISIALITTTGLMIVLMH----GQIpSAYAGLaISYavqLTGLFQFTVRLASETEARFTSVERINH-YIKTLSLEAP 918
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGkltlGQL-ITFNAL-LSY---FLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 919 ARIKNKAPPHdwpqeGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG 998
Cdd:TIGR01193 462 KKRTELNNLN-----GDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 999 IRISDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFNQ--YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVG 1076
Cdd:TIGR01193 536 FSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1077 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREaFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1156
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
490
....*....|.
gi 1720387222 1157 LLsnDSSRFYA 1167
Cdd:TIGR01193 695 LL--DRNGFYA 703
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
275-500 |
3.57e-40 |
|
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: 157.06 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 275 RQLQ---HTEHQAVLAEQKGHLLLDSDERPSPEEEEGKQIHTGSLRLQ----------RTLYNIDLEIEEGKLVGICGSV 341
Cdd:TIGR02857 278 RQLGaqyHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSgvsvaypgrrPALRPVSFTVPPGERVALVGPS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 342 GSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCL 407
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGL 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 408 RPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLKSKTVLFVTHQ 487
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHR 516
|
250
....*....|...
gi 1720387222 488 LQYLVDCDEVIFM 500
Cdd:TIGR02857 517 LALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
321-519 |
7.36e-40 |
|
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: 147.76 E-value: 7.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNI 387
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 466
Cdd:cd03254 98 RLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 467 IfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 519
Cdd:cd03254 178 I-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
586-910 |
1.18e-39 |
|
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: 150.34 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 586 WSVYWVYIQAAGGPLAFLV-IMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVYQGNRSFVSDSMKDNPFMQYyasIYALS 664
Cdd:cd18600 3 WNTYLRYITSHKSLIFVLIlCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFY---IYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 665 MAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF 744
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 745 FCVGMIAGVFPWFLVAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELL 824
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 825 DDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPSAyAGLAISYAVQLTGLFQFTVRLASETEARFTSVE 904
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGR-VGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
....*.
gi 1720387222 905 RINHYI 910
Cdd:cd18600 319 RIFKFI 324
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
944-1148 |
1.84e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 145.73 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 944 RYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLF 1023
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 SGTVRSNLD-PFN----QYTEDQIWDALERthmkeciaqlpLKLESEVME-NGDNFSVGERQLLCIARALLRHCKILILD 1097
Cdd:COG4619 87 GGTVRDNLPfPFQlrerKFDRERALELLER-----------LGLPPDILDkPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1098 EATAAMDTETDLLIQETIREAFADC--TMLTIAH------RLhtvlgSDRIMVLAQGQV 1148
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
321-505 |
8.00e-39 |
|
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: 144.27 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNI 387
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 466
Cdd:cd03245 99 TLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720387222 467 IFnSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 505
Cdd:cd03245 179 LK-ERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
279-527 |
8.15e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 153.85 E-value: 8.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 279 HTEHQAVLAEQKGHLLLDSDERPSPEEEEGKQIHTG-----------SLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTS 347
Cdd:PRK11174 312 HAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPvtieaedleilSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 348 LVSAILGQMTLlEGSIAVSGT-------------FAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAI 413
Cdd:PRK11174 392 LLNALLGFLPY-QGSLKINGIelreldpeswrkhLSWVGQNPQLPHGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 414 LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLKSKTVLFVTHQLQYLVD 493
Cdd:PRK11174 471 LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV-MQALNAASRRQTTLMVTHQLEDLAQ 549
|
250 260 270
....*....|....*....|....*....|....
gi 1720387222 494 CDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 527
Cdd:PRK11174 550 WDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
712-1168 |
9.60e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 153.44 E-value: 9.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 712 GRILNRFSKDMDEVD---VRL--PFQAEMFiqnVILVffcvgmIAGVFPWF-----LVAVGPLLILFSLLHIVSRVLIRE 781
Cdd:PRK11160 117 GDLLNRLVADVDTLDhlyLRLisPLVAALV---VILV------LTIGLSFFdltlaLTLGGILLLLLLLLPLLFYRLGKK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 782 LKRLDNITQSPFLSHITSSIQGLATIHAYNKrqefLHRYQELLDDNQApfflftcamRWLA-----VRLDLISIAL-ITT 855
Cdd:PRK11160 188 PGQDLTHLRAQYRVQLTEWLQGQAELTLFGA----EDRYRQQLEQTEQ---------QWLAaqrrqANLTGLSQALmILA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 856 TGLMIVLMhgqipSAYAGLAISYAVQ---LTGLFQFTVRLASET----EARF-------TSVERINHYIktlslEAPARI 921
Cdd:PRK11160 255 NGLTVVLM-----LWLAAGGVGGNAQpgaLIALFVFAALAAFEAlmpvAGAFqhlgqviASARRINEIT-----EQKPEV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 922 KNKAPPHDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRI 1001
Cdd:PRK11160 325 TFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1002 SDIGLADLRSKLAIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMkECIAQLPLKLESEVMENGDNFSVGER 1078
Cdd:PRK11160 405 ADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQ 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1079 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLL 1158
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
490
....*....|
gi 1720387222 1159 SNDsSRFYAM 1168
Cdd:PRK11160 562 AQQ-GRYYQL 570
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
952-1151 |
2.21e-36 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 137.64 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---IRISDIGLADLRSKLAIIPQEPvlfsgtvR 1028
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRRKEIQMVFQDP-------M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLDPfnQYT-EDQIWDALE--RTHMKECIAQLPLKLESEVMENGDN--------FSVGERQLLCIARALLRHCKILILD 1097
Cdd:cd03257 93 SSLNP--RMTiGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1098 EATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 1151
Cdd:cd03257 171 EPTSALDVSVqaqilDLLKK--LQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
322-522 |
4.31e-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: 136.90 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKE--FDEERyNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNH 466
Cdd:cd03249 99 YGKPdaTDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES-EK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 467 IFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
322-510 |
5.87e-36 |
|
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: 136.08 E-value: 5.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNIL 388
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIf 468
Cdd:cd03244 100 PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720387222 469 NSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 510
Cdd:cd03244 179 QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
414-1143 |
1.67e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 147.48 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 414 LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIFNSAIR--KRLKSKTVLFVTHQLQYL 491
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 492 -------------------VDCDEVIFMKEGC----------------------------ITERGTHEELM-NLNGDYAT 523
Cdd:PTZ00265 644 ryantifvlsnrergstvdVDIIGEDPTKDNKennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMkNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 524 IFNNlllgetppveinskkEATGSQKSQDKGPKPGSVKKEKAVKSEE---------GQLVQVEEKGQG--SVPWSVYWVY 592
Cdd:PTZ00265 724 MINN---------------QKVSSKKSSNNDNDKDSDMKSSAYKDSErgydpdemnGNSKHENESASNkkSCKMSDENAS 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 593 IQAAGGPLAFL---------------------------VIMVLFMLNVGSTAFSTWWLSYwikqGSGNSTVYqgnrSFVS 645
Cdd:PTZ00265 789 ENNAGGKLPFLrnlfkrkpkapnnlrivyreifsykkdVTIIALSILVAGGLYPVFALLY----AKYVSTLF----DFAN 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 646 DSMKDNPFmqyyaSIYALSMAV-MLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDT---TPtGRILNRFSKD 721
Cdd:PTZ00265 861 LEANSNKY-----SLYILVIAIaMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRD 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 722 MDEVDVRLPFQAEMFIQNVILvfFCVGMIAGVFPWFLVA---VGPLLILFSLLHIVSRVLIR---ELKRL---------- 785
Cdd:PTZ00265 935 VHLLKTGLVNNIVIFTHFIVL--FLVSMVMSFYFCPIVAavlTGTYFIFMRVFAIRARLTANkdvEKKEInqpgtvfayn 1012
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 786 --DNITQSP-FLshITSSIQGLATIHAYNKRQEFLHRYQELLD-------------------DNQAPFFLFTCAMrWLAV 843
Cdd:PTZ00265 1013 sdDEIFKDPsFL--IQEAFYNMNTVIIYGLEDYFCNLIEKAIDysnkgqkrktlvnsmlwgfSQSAQLFINSFAY-WFGS 1089
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 844 RLdlISIALITTTGLMIVLMHGQIPSAYAGLAISyavqltglfqftvrLASETEARFTSVERINHYIKTLSL-----EAP 918
Cdd:PTZ00265 1090 FL--IRRGTILVDDFMKSLFTFLFTGSYAGKLMS--------------LKGDSENAKLSFEKYYPLIIRKSNidvrdNGG 1153
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 919 ARIKNKAPPhdwpqEGEVTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL------- 989
Cdd:PTZ00265 1154 IRIKNKNDI-----KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhiv 1227
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 990 -----------------------------------------------SGGCIKIDGIRISDIGLADLRSKLAIIPQEPVL 1022
Cdd:PTZ00265 1228 fknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML 1307
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1023 FSGTVRSNLDpFNQ--YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1100
Cdd:PTZ00265 1308 FNMSIYENIK-FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEAT 1386
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1720387222 1101 AAMDTETDLLIQETIREA--FADCTMLTIAHRLHTVLGSDRIMVL 1143
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
18-210 |
1.70e-35 |
|
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: 137.20 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 18 GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDD 97
Cdd:cd18597 100 GKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 98 RVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFHLTAAQA 177
Cdd:cd18597 180 RVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPANI 259
|
170 180 190
....*....|....*....|....*....|...
gi 1720387222 178 FTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 210
Cdd:cd18597 260 FSSLALFNVLRMPLMFLPLALSSLADALVALKR 292
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
321-526 |
2.24e-35 |
|
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: 143.32 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNI 387
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFGK--EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 465
Cdd:TIGR02203 427 AYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 466 HIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 526
Cdd:TIGR02203 507 LV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
953-1101 |
2.25e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 131.62 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSG-TVRSNL 1031
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1032 -------DPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1101
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
322-522 |
2.39e-35 |
|
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: 134.92 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNIL 388
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKE-FDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHI 467
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEHA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 468 FNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
15-210 |
3.97e-35 |
|
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: 136.47 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 15 KSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAA 94
Cdd:cd18596 112 ASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 95 TDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVH-MTLGFHLT 173
Cdd:cd18596 192 RDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYtLVMGQELT 271
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720387222 174 AAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 210
Cdd:cd18596 272 ASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDR 308
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
322-521 |
8.66e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 141.39 E-value: 8.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI-------------AVSGTFAYVAQQAWILNATLRDNIL 388
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 467
Cdd:PRK10789 411 LGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 468 FNSaIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDY 521
Cdd:PRK10789 491 LHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
939-1148 |
1.32e-34 |
|
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: 130.41 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQ 1018
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 EPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILDE 1098
Cdd:cd03246 84 DDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1099 ATAAMDTETDLLIQETIREA-FADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1148
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
936-1150 |
3.36e-34 |
|
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: 129.36 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGlADLRSKLAI 1015
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmenGDNFSVGERQLLCIARALLRHCKILI 1095
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1096 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1150
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
910-1150 |
7.52e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 138.69 E-value: 7.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 910 IKTLSLEAPARIKNKAP-PHdwpQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 988
Cdd:PRK10789 290 IRAMLAEAPVVKDGSEPvPE---GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 989 LSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESE 1065
Cdd:PRK10789 367 VSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1066 VMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQ 1145
Cdd:PRK10789 445 VGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQH 524
|
....*
gi 1720387222 1146 GQVVE 1150
Cdd:PRK10789 525 GHIAQ 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
666-1151 |
1.11e-33 |
|
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: 137.96 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 666 AVMLILKAIRGVVFVkgtlRASSRLHDEL----FRRILRSPMKFFDTTPTgRILNrfskDMDEVdvrlpfqaEMFI-QNV 740
Cdd:COG4618 71 AVMGLLDAVRSRILV----RVGARLDRRLgprvFDAAFRAALRGGGGAAA-QALR----DLDTL--------RQFLtGPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 741 ILVFF----CVGMIAGVF---PWF-LVAVGPLLILFSL---LHIVSRVLIRELKRLDNITQSpflsHITSSIQGLATIHA 809
Cdd:COG4618 134 LFALFdlpwAPIFLAVLFlfhPLLgLLALVGALVLVALallNERLTRKPLKEANEAAIRANA----FAEAALRNAEVIEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 810 -----------YNKRQEFLhRYQELLDDNQAPFFLFTCAMR------------WLAVRLDLisialitTTGLMI---VLM 863
Cdd:COG4618 210 mgmlpalrrrwQRANARAL-ALQARASDRAGGFSALSKFLRlllqsavlglgaYLVIQGEI-------TPGAMIaasILM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 864 hgqipsayaGLAISYAVQLTGLFQFTVRlaseteARfTSVERINHYIKTLSLEaPARIKNKAPphdwpqEGEVTFENAEM 943
Cdd:COG4618 282 ---------GRALAPIEQAIGGWKQFVS------AR-QAYRRLNELLAAVPAE-PERMPLPRP------KGRLSVENLTV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 944 RYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLF 1023
Cdd:COG4618 339 VPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 SGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1103
Cdd:COG4618 419 DGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1720387222 1104 DTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVVEF 1151
Cdd:COG4618 499 DDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
916-1160 |
3.57e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.42 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 916 EAPARIKNKAPPHDWPQEGE--VTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS 990
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 991 GGCIKIDGIRISDIG---LADLRSKLAIIPQEPVlfsgtvrSNLDPFnqYT-EDQIWDALE------RTHMKECIAQLpL 1060
Cdd:COG1123 319 SGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPY-------SSLNPR--MTvGDIIAEPLRlhgllsRAERRERVAEL-L 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1061 K---LESEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHR 1130
Cdd:COG1123 389 ErvgLPPDLADrYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHD 464
|
250 260 270
....*....|....*....|....*....|.
gi 1720387222 1131 LHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:COG1123 465 LAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
14-210 |
5.09e-33 |
|
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: 129.90 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 14 EKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 93
Cdd:cd18595 91 KSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 94 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITV---GVAPIVVVIASVVTFsVHMTLGF 170
Cdd:cd18595 171 LKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSflwTCAPFLVSLATFATY-VLSDPDN 249
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720387222 171 HLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 210
Cdd:cd18595 250 VLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKR 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
602-886 |
6.19e-32 |
|
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: 126.22 E-value: 6.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTvyqgnrsfvSDSMKDNPFMQYYASIYALsmavMLILKAIRGVVFVK 681
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD---------PETQALNVYSLALLLLGLA----QFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 682 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVIlVFFCVGMIAGVFPWFL--- 758
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLA-TIVGGIIVMFYYGWKLtlv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 759 -VAVGPLLILFSLlhIVSRVLiRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCA 837
Cdd:pfam00664 147 lLAVLPLYILVSA--VFAKIL-RKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 838 MRWLAVRLDLI---SIALITTTGlMIVLMHGQIPSAYAGLAISYAVQLTGLF 886
Cdd:pfam00664 224 NGLSFGITQFIgylSYALALWFG-AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
16-211 |
1.44e-31 |
|
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: 125.82 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 16 SLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAAT 95
Cdd:cd18594 94 TTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 96 DDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFHLTAA 175
Cdd:cd18594 174 DERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTAR 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720387222 176 QAFTVVTVFNS--MTFALKVtPFSVKSLSEASVAVDRF 211
Cdd:cd18594 254 KVFTVISLLNAlrMTITRFF-PESIQTLSESRVSLKRI 290
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
322-522 |
1.53e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 131.68 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlaslrnqVALVSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKEfdeERYNsvlnscclRPDL--------AI-----LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:PRK11176 439 YART---EQYS--------REQIeeaarmayAMdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 456 LSALDAHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:PRK11176 508 TSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
936-1160 |
1.96e-31 |
|
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: 130.41 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGIRISDIGLADLRSK 1012
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1013 LAIIPQEPvlfsgtvRSNLDPFNqyTEDQIWDALE-----RTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIAR 1085
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALEnlglsRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1086 ALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
322-522 |
6.02e-30 |
|
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: 127.55 E-value: 6.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWI---LNATLRDNILFGKEFDEery 398
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLrrqMGVVLQENVLFSRSIRD--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 399 nsvlNSCCLRPDLAI------------------LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:TIGR01846 550 ----NIALCNPGAPFehvihaaklagahdfiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 461 AHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:TIGR01846 626 YE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
322-522 |
6.39e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 127.92 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 467
Cdd:TIGR00958 577 YGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 468 FNSairKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
322-501 |
1.66e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.25 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------FAYVAQQA---WILNATLRDNIL-- 388
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 ------FGKEFDEERYNSVLNScclrpdLAILpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERV---GLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720387222 462 HvGNHIFNSAIRK-RLKSKTVLFVTHQLQYLVD-CDEVIFMK 501
Cdd:cd03235 166 K-TQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
938-1147 |
2.06e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 116.80 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 938 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIP 1017
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1018 QEP--VLFSGTVRSNL--DPFN-QYTEDQIW----DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1088
Cdd:cd03225 82 QNPddQFFGPTVEEEVafGLENlGLPEEEIEerveEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1089 RHCKILILDEATAAMDTETDLLIQETIREaFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQ 1147
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
307-522 |
2.33e-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: 125.83 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 307 EGKQIHTGSLRLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI-------------AVSGTFAYV 372
Cdd:TIGR03796 479 ELRNITFGYSPLEPPLIeNFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEIlfdgipreeipreVLANSVAMV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 373 AQQAWILNATLRDNI-LFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYI 451
Cdd:TIGR03796 559 DQDIFLFEGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 452 LDDPLSALDAHVgNHIFNSAIRKRlkSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:TIGR03796 639 LDEATSALDPET-EKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYA 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
286-488 |
2.38e-29 |
|
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: 124.40 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 286 LAEQKGHLLLDSDERPSPEEEEGKQIHTGSLRL-----QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLE 360
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAgypgaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 361 GSIAVSG-------------TFAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERG 426
Cdd:TIGR02868 390 GEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 427 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLKSKTVLFVTHQL 488
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLAALSGRTVVLITHHL 530
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
937-1147 |
2.78e-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: 114.65 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 937 TFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAII 1016
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1017 PQepvlfsgtvrsnldpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILIL 1096
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1097 DEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTV-LGSDRIMVLAQGQ 1147
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
936-1147 |
5.60e-29 |
|
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: 115.26 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRY---RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGirisdigladlrsK 1012
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1013 LAIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1092
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1093 ILILDEATAAMDTET-DLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQ 1147
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
322-522 |
1.02e-28 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 123.01 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLV-----------SAIL--GQ----MTL--LEGSIAVsgtfayVAQQAWILNAT 382
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfydvtsGRILidGQdirdVTQasLRAAIGI------VPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:COG5265 448 IAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 462 HVGNHIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:COG5265 528 RTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-516 |
1.33e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------FAYVAQQA---WILNATLRDNILFG 390
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 391 --------KEFDEERYNSVLNScclrpdLAILpnsDLTE-----IGErganLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDladrpIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 458 ALDAHVGNHIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErGTHEELMN 516
Cdd:COG1121 169 GVDAATEEALY--ELLRELRRegKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
319-522 |
2.06e-28 |
|
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: 121.73 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRD 385
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldpaelrarMALVPQDPVLFAASVME 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGK--EFDEERYNSVLNScclRPDLAI--LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:TIGR02204 433 NIRYGRpdATDEEVEAAARAA---HAHEFIsaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 462 HvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYA 569
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
317-516 |
2.73e-28 |
|
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: 114.90 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQ-------- 375
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQDpyaslhpr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 376 ---AWILNATLRdniLFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRSIYIL 452
Cdd:COG1124 96 htvDRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL----------DRYPHQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 453 DDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 516
Cdd:COG1124 163 DEPTSALDVSVQAEILNllKDLREERGL-TYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
952-1159 |
3.57e-28 |
|
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: 114.52 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPvlfsgtvRSNL 1031
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP-------YASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 DPF---------------NQYTEDQIWDALERTHMKECIA-QLPLKLesevmengdnfSVGERQLLCIARALLRHCKILI 1095
Cdd:COG1124 93 HPRhtvdrilaeplrihgLPDREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1096 LDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:COG1124 162 LDEPTSALDVSVqaeilNLL--KDLREER-GLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
319-509 |
4.76e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 111.64 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI------------AVSGTFAYVAQQAWILNATLRDN 386
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlekALSSLISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 IlfgkefdeerynsvlnscclrpdlailpnsdlteigerGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 466
Cdd:cd03247 95 L--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720387222 467 IFnSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 509
Cdd:cd03247 137 LL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-522 |
7.05e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 120.31 E-value: 7.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 305 EEEGKQIHTGSLRL-----------QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----- 368
Cdd:PRK11160 328 TTSTAAADQVSLTLnnvsftypdqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiady 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 369 --------FAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNscclRPDLAILPNSDL---TEIGERGANLSGGQRQR 436
Cdd:PRK11160 408 seaalrqaISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQ----QVGLEKLLEDDKglnAWLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 437 ISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
....*.
gi 1720387222 517 LNGDYA 522
Cdd:PRK11160 563 QQGRYY 568
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
293-527 |
7.40e-28 |
|
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: 121.00 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 293 LLLDSDERPSPEEEEGKQIHtGSLRLQRTLY----------NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGS 362
Cdd:TIGR01193 452 YLVDSEFINKKKRTELNNLN-GDIVINDVSYsygygsnilsDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 363 IAVSGT-------------FAYVAQQAWILNATLRDNILFG--KEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGA 427
Cdd:TIGR01193 531 ILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 428 NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIrkRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 507
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
250 260
....*....|....*....|
gi 1720387222 508 RGTHEELMNLNGDYATIFNN 527
Cdd:TIGR01193 689 QGSHDELLDRNGFYASLIHN 708
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
936-1161 |
2.81e-27 |
|
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: 112.06 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAI 1015
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVL-FSGTVR--------SNLDPFNQYTED---QIWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCI 1083
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryPHLGLFGRPSAEdreAVEEALERTGLEH-LADRPV----------DELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1084 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
.
gi 1720387222 1161 D 1161
Cdd:COG1120 229 E 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
322-505 |
3.46e-27 |
|
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: 109.23 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 fgkefdeerynsvlnscclrpdlailpnsdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIF 468
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720387222 469 NSAIRK-RLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 505
Cdd:cd03246 136 NQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
319-503 |
3.91e-27 |
|
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: 108.49 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTfayvaQQAWILNATLRDNILFgkefdeery 398
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 399 nsvlnscclRPDLailpnsdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGnHIFNSAIRKRLKS 478
Cdd:cd00267 78 ---------VPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAEE 129
|
170 180
....*....|....*....|....*..
gi 1720387222 479 -KTVLFVTHQLQYLVD-CDEVIFMKEG 503
Cdd:cd00267 130 gRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
16-210 |
6.87e-27 |
|
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: 111.93 E-value: 6.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 16 SLGELINICSNDGQRMFEAAAVGSLLAGGPV--VAILGMIYNVIilGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 93
Cdd:cd18593 95 TVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLqlIAVIYILWFEI--GWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 94 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFHLT 173
Cdd:cd18593 173 RTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILT 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720387222 174 AAQAFTVVTVFNS----MTFALkvtPFSVKSLSEASVAVDR 210
Cdd:cd18593 253 AERVFVTMALYNAvrltMTLFF---PFAIQFGSELSVSIRR 290
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
313-516 |
1.01e-26 |
|
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: 116.39 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 313 TGSLRLQR-----------TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------------- 368
Cdd:COG4618 328 KGRLSVENltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 369 FAYVAQQAWILNATLRDNI-LFGkEFDEERynsVLNSCclrpDLA-----I--LPNSDLTEIGERGANLSGGQRQRISLA 440
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIaRFG-DADPEK---VVAAA----KLAgvhemIlrLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 441 RALYSDRSIYILDDPLSALDAhVGNHIFNSAIRkRLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDD-EGEAALAAAIR-ALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
286-515 |
1.86e-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: 115.52 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 286 LAEQKGHLLLDS-DERPSPEEeegkqihtgslrlQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIA 364
Cdd:TIGR01842 310 LPEPEGHLSVENvTIVPPGGK-------------KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 365 VSG-------------TFAYVAQQAWILNATLRDNIL-FGKEFDEErynSVLNSCCLRP--DLAI-LPNSDLTEIGERGA 427
Cdd:TIGR01842 377 LDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPE---KIIEAAKLAGvhELILrLPDGYDTVIGPGGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 428 NLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIrKRLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 505
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EGEQALANAI-KALKARgiTVVVITHRPSLLGCVDKILVLQDGRI 531
|
250
....*....|
gi 1720387222 506 TERGTHEELM 515
Cdd:TIGR01842 532 ARFGERDEVL 541
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
938-1161 |
2.34e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.08 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 938 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIP 1017
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1018 QEPvlfsgtvrsnlDpfNQY----TEDQIWDALE-----RTHMKECIAQLPLKLEsevMEN-----GDNFSVGERQLLCI 1083
Cdd:PRK13632 90 QNP-----------D--NQFigatVEDDIAFGLEnkkvpPKKMKDIIDDLAKKVG---MEDyldkePQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1084 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1161
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
322-505 |
3.74e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.21 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 F-----GKEFDEERYNSVLNSCCLRPDLAilpNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHv 463
Cdd:COG4619 96 FpfqlrERKFDRERALELLERLGLPPDIL---DKPVER-------LSGGERQRLALIRALLLQPDVLLLDEPTSALDPE- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720387222 464 gN-HIFNSAIRKRLKSK--TVLFVTH---QLQYLvdCDEVIFMKEGCI 505
Cdd:COG4619 165 -NtRRVEELLREYLAEEgrAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
46-210 |
4.10e-26 |
|
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: 110.40 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 46 VVAILGMIYNViiLGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCV 125
Cdd:cd18591 145 IIVGLILLYLK--LGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 126 QKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTL-GFHLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEA 204
Cdd:cd18591 223 QEARRKELKLLLKDAVYWSLMTFLTQASPILVTLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINA 302
|
....*.
gi 1720387222 205 SVAVDR 210
Cdd:cd18591 303 VVSTRR 308
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-516 |
4.16e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.23 E-value: 4.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------------FAYVAQQAWI-LNATLRDNILF- 389
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLRFf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 ------GKEFDEERYNSVLNSCclrpdlailpnsDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAh 462
Cdd:COG1131 98 arlyglPRKEARERIDELLELF------------GLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 463 VGNHIFNSAIRkRLKS--KTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELMN 516
Cdd:COG1131 165 EARRELWELLR-ELAAegKTVLLSTHYLeeaERL--CDRVAIIDKGRIVADGTPDELKA 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
322-525 |
9.49e-26 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 113.83 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIdintvtreslrksIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKE--FDEERYNSVLNSCCLRPDLAILPNSDlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 466
Cdd:TIGR01192 431 LGREgaTDEEVYEAAKAAAAHDFILKRSNGYD-TLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEAR 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 467 IFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF 525
Cdd:TIGR01192 510 VKN-AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-503 |
1.00e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 106.40 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------------FAYVAQQawILNATL 383
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkvglvFQNPDDQ--FFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNILFGKE---FDEERYNSVLNSCCLRPDLAILPNSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:cd03225 94 EEEVAFGLEnlgLPEEEIEERVEEALELVGLEGLRDRSP-------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720387222 461 AHVGNHIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEG 503
Cdd:cd03225 167 PAGRRELL--ELLKKLKAegKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
322-522 |
1.29e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 113.13 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKE--FDEERYNSVLNSCCLrpDLaILPNSD--LTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 464
Cdd:PRK13657 431 VGRPdaTDEEMRAAAERAQAH--DF-IERKPDgyDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 465 NHIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:PRK13657 508 AKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
952-1157 |
1.63e-25 |
|
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: 106.11 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDG--IRISDIGLADLRSKLAIIPQEPVLFS 1024
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegeVLLDGkdIYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1025 GTVRSNLDpfnqYTeDQIWDALERTHMKECIAQLpLK---LESEVME--NGDNFSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:cd03260 95 GSIYDNVA----YG-LRLHGIKLKEELDERVEEA-LRkaaLWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1100 TAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVL 1157
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
324-509 |
2.03e-25 |
|
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: 104.44 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIavsgtfayvaqqawilnatlrdnILFGKEFDEerynsvLN 403
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-----------------------LLDGKDLAS------LS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 404 SCCLRPDLAILPNS----DLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KRLK 477
Cdd:cd03214 68 PKELARKIAYVPQAlellGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlARER 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720387222 478 SKTVLFVTHQL----QYlvdCDEVIFMKEGCITERG 509
Cdd:cd03214 148 GKTVVMVLHDLnlaaRY---ADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
936-1168 |
2.11e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.33 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRIsdiglADLRSKLAI 1015
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQE-------PVlfsgTVR----SNLDP----FNQYTE---DQIWDALERTHMKE----CIAQLplklesevmengdnf 1073
Cdd:COG1121 80 VPQRaevdwdfPI----TVRdvvlMGRYGrrglFRRPSRadrEAVDEALERVGLEDladrPIGEL--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1074 SVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 1151
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHG 220
|
250
....*....|....*..
gi 1720387222 1152 DTPSVLLSNDSSRFYAM 1168
Cdd:COG1121 221 PPEEVLTPENLSRAYGG 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
319-505 |
3.64e-25 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 104.52 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQaWIL--NATLRD 385
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD-YALfpHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFG----KEFDEERYNSVLNScclrpdLAILpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:cd03259 92 NIAFGlklrGVPKAEIRARVREL------LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 461 AHVgnhifNSAIRKRLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCI 505
Cdd:cd03259 163 AKL-----REELREELKElqrelgITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
956-1154 |
4.54e-25 |
|
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: 107.45 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGIRISDIGLADLR----SKLAIIPQEPVlfsgtvr 1028
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLDPFnqYT-EDQIWDALeRTH-------MKECIAQLpLKL-----ESEVMengDN----FSVGERQLLCIARALLRHC 1091
Cdd:COG0444 97 TSLNPV--MTvGDQIAEPL-RIHgglskaeARERAIEL-LERvglpdPERRL---DRypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 1092 KILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTP 1154
Cdd:COG0444 170 KLLIADEPTTALDVTIqaqilNLLKD--LQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelFENP 242
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
322-500 |
4.59e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.94 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------FAYVAQQA----WilnATLRDNILF 389
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW---LTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 G-------KEFDEERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALDA- 461
Cdd:COG1116 104 GlelrgvpKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720387222 462 ---HVGNHIFNsaIRKRLKsKTVLFVTHqlqylvDCDEVIFM 500
Cdd:COG1116 173 treRLQDELLR--LWQETG-KTVLFVTH------DVDEAVFL 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-509 |
5.15e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 104.90 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQQA------ 376
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQDPmsslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 377 -----WILNATLRDN-ILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARALYSDRSI 449
Cdd:cd03257 98 rmtigEQIAEPLRIHgKLSKKEARKEAVLLLLVGVGLPEEVLnRYPHE-----------LSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 450 YILDDPLSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERG 509
Cdd:cd03257 167 LIADEPTSALDVSVQAQILD--LLKKLQEElglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
324-516 |
5.25e-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: 105.51 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWI-LNATLRDNILF 389
Cdd:COG1120 19 DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPApFGLTVRELVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 G-----------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:COG1120 99 GryphlglfgrpSAEDREAVEEALERT------------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 458 ALD-AH---VGNHIfnsairKRL---KSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 516
Cdd:COG1120 167 HLDlAHqleVLELL------RRLareRGRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
939-1149 |
5.39e-25 |
|
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: 102.90 E-value: 5.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQ 1018
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 epvlfsgtvrsnldpfnqytedqiwdALERT---HMKEC-IAQLplklesevmengdnfSVGERQLLCIARALLRHCKIL 1094
Cdd:cd03214 81 --------------------------ALELLglaHLADRpFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1095 ILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRL-HTVLGSDRIMVLAQGQVV 1149
Cdd:cd03214 120 LLDEPTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
653-1144 |
6.65e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 112.82 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 653 FMQYYASIYALSMAVMLILKAIRgVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFskdmdevdvrlpfq 732
Cdd:PTZ00265 111 FILSFISSFCMDVVTTKILKTLK-LEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKF-------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 733 aemfiqnvILVFFCVGMIAGVFPWFLVAVGPLLI----LFSLLHIVSRVLIRELK---RLDNITQSPFLSHITSSIQGLA 805
Cdd:PTZ00265 176 --------ITIFTYASAFLGLYIWSLFKNARLTLcitcVFPLIYICGVICNKKVKinkKTSLLYNNNTMSIIEEALVGIR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 806 TIHAYNKRQEFLHRYQeLLDDNQAPFFLFTCAMRWLAVRLD----LISIALITTTGLMIVL--MHGQIPSA--YAGLAIS 877
Cdd:PTZ00265 248 TVVSYCGEKTILKKFN-LSEKLYSKYILKANFMESLHIGMIngfiLASYAFGFWYGTRIIIsdLSNQQPNNdfHGGSVIS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 878 YAVQ-LTGLFQFTVRLASETEarftsverinhYIKtlSLEAPA---RIKNKAPPHDWPQEGE-------VTFENAEMRY- 945
Cdd:PTZ00265 327 ILLGvLISMFMLTIILPNITE-----------YMK--SLEATNslyEIINRKPLVENNDDGKklkdikkIQFKNVRFHYd 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 946 -RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKI-DGIRISDIGLADLRSKLAIIPQEPVLF 1023
Cdd:PTZ00265 394 tRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLF 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 SGTVRSNLDPF-----------NQYTED--------------------------QIWDALERTHMK-------------- 1052
Cdd:PTZ00265 473 SNSIKNNIKYSlyslkdlealsNYYNEDgndsqenknkrnscrakcagdlndmsNTTDSNELIEMRknyqtikdsevvdv 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1053 -------ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTML 1125
Cdd:PTZ00265 553 skkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
570 580
....*....|....*....|.
gi 1720387222 1126 T--IAHRLHTVLGSDRIMVLA 1144
Cdd:PTZ00265 633 TiiIAHRLSTIRYANTIFVLS 653
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
608-910 |
9.67e-25 |
|
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: 105.76 E-value: 9.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 608 LFMLNVGSTAFSTWWLSYWIKQgSGNSTVYQGnrsfvsdsmkdnpfmQYYASIYALSMAVMLILKAIRGVVFVKGTLRAS 687
Cdd:cd18559 7 LVLCNHVFSGPSNLWLLLWFDD-PVNGPQEHG---------------QVYLSVLGALAILQGITVFQYSMAVSIGGIFAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 688 SRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF---IQNVILVFFcvgMIAGVFPWFLVAVgPL 764
Cdd:cd18559 71 RAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWmgpLQNVIGLYL---LILLAGPMAAVGI-PL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 765 LILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRyQELLDDNQAPFFLFTCAMRWLAVR 844
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQ-VDAKRDNELAYLPSIVYLRALAVR 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 845 LDLISIALITTTGLMIVLMHGQIpSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 910
Cdd:cd18559 226 LWCVGPCIVLFASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
939-1155 |
1.09e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQ 1018
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 EP-VLFSG-TVRSNLD--------PFNQYTEdQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1088
Cdd:PRK13635 89 NPdNQFVGaTVQDDVAfglenigvPREEMVE-RVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1089 RHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPS 1155
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
319-533 |
1.92e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 109.81 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRD 385
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 465
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 466 HIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGET 533
Cdd:PRK10790 514 AI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
324-516 |
2.03e-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: 108.84 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQ----QawiLNA-- 381
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVFQdpysS---LNPrm 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLRDNILFG--------KEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRSIYILD 453
Cdd:COG1123 360 TVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDLA----------DRYPHELSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 454 DPLSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 516
Cdd:COG1123 430 EPTSALDVSVQAQILNllRDLQRELG-LTYLFISHDLA-VVRyiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
322-505 |
2.94e-24 |
|
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: 100.55 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVsgtfayvaqqawilnatlrdnilFGKEFDEERyNSV 401
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 402 LNSCCLRPDLAILPnSDLTeiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRKRLKS-KT 480
Cdd:cd03230 72 KRRIGYLPEEPSLY-ENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRELKKEgKT 147
|
170 180
....*....|....*....|....*.
gi 1720387222 481 VLFVTHQLQYLVD-CDEVIFMKEGCI 505
Cdd:cd03230 148 ILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
322-500 |
2.97e-24 |
|
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: 102.16 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------FAYVAQQA----WilnATLRDNILF 389
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 GkefdeerynsvlnscclrPDLAILPNSDLTEIGER---------GAN-----LSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:cd03293 97 G------------------LELQGVPKAEARERAEEllelvglsgFENayphqLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 456 LSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHqlqylvDCDEVIFM 500
Cdd:cd03293 159 FSALDALTREQLQEelLDIWRETG-KTVLLVTH------DIDEAVFL 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-497 |
3.00e-24 |
|
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: 101.79 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLY-NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------------FAYVAQQ-AWILNATLR 384
Cdd:COG4133 14 ERLLFsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILF-----GKEFDEERYNSVLnscclrpdlAILpnsDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEAL---------EAV---GLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720387222 459 LDAHvGNHIFNSAIRKRLKS-KTVLFVTHQLQYLVDCDEV 497
Cdd:COG4133 162 LDAA-GVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
324-520 |
3.64e-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: 102.63 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGtFAYVAQQAWILNA--------------TLRDNI-L 388
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQigvlpderglydrlTVRENIrY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FG---KEFDEERYNSVLNscclrpdlaILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVG 464
Cdd:COG4555 98 FAelyGLFDEELKKRIEE---------LIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 465 NHIFNSAIRkRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNLNGD 520
Cdd:COG4555 168 RRLLREILR-ALKKegKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-514 |
3.84e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.23 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGqmtlLE----GSIAVSGT--F----------AYVAQQAwilnA---- 381
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGRdlFtnlpprerrvGFVFQHY----Alfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 -TLRDNILFGkefdeerynsvlnscclrpdLAILPNS---------------DLTEIGER-GANLSGGQRQRISLARALY 444
Cdd:COG1118 90 mTVAENIAFG--------------------LRVRPPSkaeirarveellelvQLEGLADRyPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 445 SDRSIYILDDPLSALDAHVgnhifnsaiRKRLKSK----------TVLFVTHQLQ--YLVdCDEVIFMKEGCITERGTHE 512
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKV---------RKELRRWlrrlhdelggTTVFVTHDQEeaLEL-ADRVVVMNQGRIEQVGTPD 219
|
..
gi 1720387222 513 EL 514
Cdd:COG1118 220 EV 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
319-516 |
8.02e-24 |
|
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: 101.42 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQQAWILNA- 381
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLRDNILF-----GKEFDEERYNSV---LNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILD 453
Cdd:cd03261 93 TVFENVAFplrehTRLSEEEIREIVlekLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 454 DPLSALDAhVGNHIFNSAIR--KRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
898-1130 |
8.67e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 898 ARFTS-VERINHYIKtlSLEAPARIKNKAPPHDWPQEGEVTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGK 976
Cdd:COG4178 326 AEWRAtVDRLAGFEE--ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 977 SSLgmalFRLveLSG------GCIKI-DGIRIsdigladlrsklAIIPQEPVLFSGTVRSNL---DPFNQYTEDQIWDAL 1046
Cdd:COG4178 403 STL----LRA--IAGlwpygsGRIARpAGARV------------LFLPQRPYLPLGTLREALlypATAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1047 ERTHMKECIAQLplkleSEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT 1126
Cdd:COG4178 465 EAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
....
gi 1720387222 1127 IAHR 1130
Cdd:COG4178 540 VGHR 543
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
938-1146 |
8.99e-24 |
|
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: 100.69 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 938 FENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRIsdiglADLRSKLAIIP 1017
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1018 QE-------PVLFSGTVRSNLDP----FNQYTEDQ---IWDALERTHMKE----CIAQLplklesevmengdnfSVGERQ 1079
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEladrQIGEL---------------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1080 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGS-DRIMVLAQG 1146
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
953-1150 |
1.07e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 106.69 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGIRISDIG---LADLRSKLAIIPQEPvlFSG---- 1025
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 -TV-----------RSNLDPfnQYTEDQIWDALERTHmkeciaqlplkLESEVM-----EngdnFSVGERQLLCIARALL 1088
Cdd:COG4172 379 mTVgqiiaeglrvhGPGLSA--AERRARVAEALEEVG-----------LDPAARhryphE----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1089 RHCKILILDEATAAMdtetDLLIQETIREAFADC------TMLTIAHRLHTV--LgSDRIMVLAQGQVVE 1150
Cdd:COG4172 442 LEPKLLVLDEPTSAL----DVSVQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
936-1147 |
2.09e-23 |
|
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: 98.41 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIG--LADLRSKL 1013
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSG-TVRSNLdpfnqytedqiwdalerthmkeciaQLPLklesevmengdnfSVGERQLLCIARALLRHCK 1092
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------------------ALGL-------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1093 ILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1147
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
324-457 |
2.44e-23 |
|
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: 97.33 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNA-TLRDNILF 389
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 390 GKEFdEERYNSVLNScclRPDLAI--LPNSDL--TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:pfam00005 83 GLLL-KGLSKREKDA---RAEEALekLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
318-510 |
2.45e-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: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 318 LQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLR 384
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNI-LFGKEFDEERYNSVlnscclrpdlailpnsdltEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 463
Cdd:cd03369 100 SNLdPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 464 gNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 510
Cdd:cd03369 161 -DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
939-1148 |
3.28e-23 |
|
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: 97.85 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGlADLRSKLAIIPQ 1018
Cdd:cd03230 4 RNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 EPVLFSG-TVRSNLDpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILD 1097
Cdd:cd03230 81 EPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1098 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1148
Cdd:cd03230 121 EPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
936-1160 |
2.01e-22 |
|
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: 97.27 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGIRISDIGLADL 1009
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerpTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1010 ---RSKLAIIPQEPVLFSG-TVRSNLD-PFnqytedQIWdALERTHMKECIAQLpLK---LESEVMENGDNFSVGERQLL 1081
Cdd:cd03258 78 rkaRRRIGMIFQHFNLLSSrTVFENVAlPL------EIA-GVPKAEIEERVLEL-LElvgLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1082 CIARALLRHCKILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1155
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETtqsilALLRD--INREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 1720387222 1156 VLLSN 1160
Cdd:cd03258 227 EVFAN 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
309-503 |
2.34e-22 |
|
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: 96.79 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 309 KQIHTGSLRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------------FAY 371
Cdd:cd03255 8 KTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 372 VAQQAWILNA-TLRDNILFGKEF-------DEERYNSVLNSCCLRPDLAILPNsdlteigergaNLSGGQRQRISLARAL 443
Cdd:cd03255 87 VFQSFNLLPDlTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 444 YSDRSIYILDDPLSALDAHVGNHIFNsAIRK--RLKSKTVLFVTHQLQYLVDCDEVIFMKEG 503
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVME-LLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
315-509 |
3.09e-22 |
|
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: 96.21 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 315 SLRLQRTLYNIDLEIE---EGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------------FAYVAQ 374
Cdd:cd03297 3 CVDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 375 QAWIL-NATLRDNILFGKEFDEERYNSVlnscclRPDlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYIL 452
Cdd:cd03297 83 QYALFpHLNVRENLAFGLKRKRNREDRI------SVD-ELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 453 DDPLSALDAHVGNHIFNSaIRKRLKS--KTVLFVTH---QLQYLvdCDEVIFMKEGCITERG 509
Cdd:cd03297 156 DEPFSALDRALRLQLLPE-LKQIKKNlnIPVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
956-1150 |
4.06e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.04 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIG---LADLRSKLAIIPQEPvlfsgtvRSNLD 1032
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-------YASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1033 PfnQYT-EDQIWDALE------RTHMKECIAQLPLK--LESEVM-----EngdnFSVGERQLLCIARALLRHCKILILDE 1098
Cdd:COG4608 110 P--RMTvGDIIAEPLRihglasKAERRERVAELLELvgLRPEHAdryphE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1099 ATAAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRL----HTvlgSDRIMVLAQGQVVE 1150
Cdd:COG4608 184 PVSAL----DVSIQaqvlnllEDLQDEL-GLTYLFISHDLsvvrHI---SDRVAVMYLGKIVE 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
322-503 |
4.36e-22 |
|
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: 94.56 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIavsgtfayvaqqaWILNATLRDNILFGKEFdEERYNSV 401
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-------------LIDGEDLTDLEDELPPL-RRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 402 LNSCCLRPDLAILPNsdlteIGERganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI--FNSAIRKRLKsK 479
Cdd:cd03229 82 FQDFALFPHLTVLEN-----IALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVraLLKSLQAQLG-I 152
|
170 180
....*....|....*....|....*
gi 1720387222 480 TVLFVTHQLQYLVD-CDEVIFMKEG 503
Cdd:cd03229 153 TVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
322-515 |
6.09e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 95.86 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG------TFAYVAQQAWIL---------NATLRDN 386
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRKVGLVfqnpddqlfAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFG-------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:COG1122 97 VAFGpenlglpREEIRERVEEALELV------------GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 459 LDAHVGNHIFNsAIRK-RLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 515
Cdd:COG1122 165 LDPRGRRELLE-LLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
322-514 |
7.03e-22 |
|
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: 95.73 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQQAWILNA-TLR 384
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSSrTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILF-------GKEFDEERYNSVLNscclrpdlailpnsdLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 453
Cdd:cd03258 101 ENVALpleiagvPKAEIEERVLELLE---------------LVGLEDKAdaypAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 454 DPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:cd03258 166 EATSALDPETTQSILAllRDINRELGL-TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
320-516 |
8.18e-22 |
|
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: 95.87 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFA-----------YVAQQ-AWILNATLRDNI 387
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFGKEFDEERYnsvlnscclRPDLA--------ILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:cd03296 96 AFGLRVKPRSE---------RPPEAeirakvheLLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 459 LDAHVgnhifnsaiRKRLKS----------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03296 167 LDAKV---------RKELRRwlrrlhdelhVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
320-522 |
1.05e-21 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 101.57 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI-------------AVSGTFAYVAQQAWILNATLRDN 386
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqdlagldvqAVRRQLGVVLQNGRLMSGSIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD----AH 462
Cdd:TIGR03797 547 IAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtqAI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 463 VgnhifnSAIRKRLKSkTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 522
Cdd:TIGR03797 627 V------SESLERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
322-505 |
1.34e-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: 94.85 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNIL 388
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FG---KEFDE-----ERYNSVLNscclrpdLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:cd03248 110 YGlqsCSFECvkeaaQKAHAHSF-------ISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720387222 461 AHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 505
Cdd:cd03248 183 AE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
952-1164 |
2.71e-21 |
|
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: 94.11 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRI---SDIGLADLRSKLAIIPQEPVLFSG-TV 1027
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGMLFQSGALFDSlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 RSNLD-PFNQYTEDQIWDALERThmKECIAQLPLKLESEVMEngDNFSVGERQLLCIARALLRHCKILILDEATAAMD-- 1104
Cdd:cd03261 95 FENVAfPLREHTRLSEEEIREIV--LEKLEAVGLRGAEDLYP--AELSGGMKKRVALARALALDPELLLYDEPTAGLDpi 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1105 --TETDLLIQeTIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1164
Cdd:cd03261 171 asGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
952-1149 |
3.75e-21 |
|
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: 91.34 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGirisdigladlrsklaiipqEPVLFSGtvrsnl 1031
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFAS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 dpfnqytedqIWDALErtHMKECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAM-DTETDLL 1110
Cdd:cd03216 69 ----------PRDARR--AGIAMVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720387222 1111 IqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:cd03216 122 F-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
320-516 |
4.20e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.44 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILG---QMTLLEGSIAVSGT-------------FAYVAQQAWI-LN-A 381
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMTqLNpV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLRDNILFGKEFD----EERYNSVLnscclrpdlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:COG1123 100 TVGDQIAEALENLglsrAEARARVL---------ELLEAVGLERRLDRYpHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 457 SALDAHVGNHIFnSAIRK--RLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:COG1123 171 TALDVTTQAEIL-DLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
952-1150 |
5.64e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--IRISDIGLAdLRSKLAIIPQEPVLFSG-TVR 1028
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA-QAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLdpF--NQYTEDQI--WDALERThMKECIAQL--PLKLESEVMEngdnFSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:COG1129 98 ENI--FlgREPRRGGLidWRAMRRR-ARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1103 M-DTETDLLIqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:COG1129 171 LtEREVERLF-RIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
309-507 |
7.98e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.41 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 309 KQIHTGSLRLqRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSaILGqmTLL---EGSIAVSGT----------------- 368
Cdd:COG1136 12 KSYGTGEGEV-TALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILG--GLDrptSGEVLIDGQdisslserelarlrrrh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 369 FAYVAQQAWIL-NATLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQR 436
Cdd:COG1136 88 IGFVFQFFNLLpELTALENVALplllagvSRKERRERARELL---------------ERVGLGDRLdhrpSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 437 ISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHQLQYLVDCDEVIFMKEGCITE 507
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLEllRELNRELG-TTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
936-1148 |
7.99e-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: 92.17 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE-LSGGCIKIDGI---RISDIGLADL 1009
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTdisKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1010 R-SKLAIIPQEPVLFSG-TVRSNLD-------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQL 1080
Cdd:cd03255 80 RrRHIGFVFQSFNLLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1081 LCIARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1148
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
936-1130 |
9.78e-21 |
|
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: 90.29 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGirisdigladlRSKLAI 1015
Cdd:cd03223 1 IELENLSLATPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSGTVRsnldpfnqyteDQI---WDalerthmkeciaqlplklesevmengDNFSVGERQLLCIARALLRHCK 1092
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720387222 1093 ILILDEATAAMDTETDLLIQETIREAFAdcTMLTIAHR 1130
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
952-1160 |
1.54e-20 |
|
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: 91.73 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAD-LRSKLAIIPQEPVLFSG-TVRS 1029
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NL--------DPFNQYTEDQIWDALERthMKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEATA 1101
Cdd:cd03224 95 NLllgayarrRAKRKARLERVYELFPR--LKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1102 ----AMDTEtdllIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:cd03224 162 glapKIVEE----IFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
320-514 |
1.59e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.75 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQaWIL--NATLRDN 386
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQS-YALypHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFG-------KEFDEERYNSVLnscclrpdlAILpnsDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:COG3839 96 IAFPlklrkvpKAEIDRRVREAA---------ELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 459 LDAHVGNH----IfnSAIRKRLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:COG3839 164 LDAKLRVEmraeI--KRLHRRLGT-TTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
936-1117 |
1.72e-20 |
|
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: 91.00 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGlADLRSKLAI 1015
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSG-TVRSNLDpF------NQYTEDQIWDALERTHMKECiAQLPLKlesevmengdNFSVGERQLLCIARALL 1088
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-ADLPVR----------QLSAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 1720387222 1089 RHCKILILDEATAAMDTETDLLIQETIRE 1117
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
936-1173 |
1.87e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.98 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAI 1015
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSG-TVRSN--LDP-FNQYTEDQIwdaleRTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHC 1091
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKI-----RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1092 KILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEFDTPS 1155
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFK-------------RLQQELGktivfvthdideafrlADRIAIMKNGEIVQVGTPD 221
|
250
....*....|....*...
gi 1720387222 1156 VLLSNDSSRFYAMFAAAE 1173
Cdd:cd03295 222 EILRSPANDFVAEFVGAD 239
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
936-1150 |
2.39e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.88 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDI---GLADLRSK 1012
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1013 LAIIPQE-PVLFSGTVRSNL---------DPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1082
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgkSR--KEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1083 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREafADCTMLtIA-HRLHTVLGSD-RIMVLAQGQVVE 1150
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsweimELL--EEINR--RGTTVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
322-514 |
8.33e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILF 389
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 GKEFDEERYnsvlnscclRPDLAI--------LPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:PRK10851 98 GLTVLPRRE---------RPNAAAikakvtqlLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 461 AHVgnhifnsaiRKRLKS---------K-TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK10851 169 AQV---------RKELRRwlrqlheelKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
324-514 |
1.03e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.08 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQAwilnA-----TLRDNI 387
Cdd:COG3842 23 DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDY----AlfphlTVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFG-------KEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:COG3842 99 AFGlrmrgvpKAEIRARVAELL---------------ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 457 SALDAHVGNH----IFNsaIRKRLKsKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:COG3842 164 SALDAKLREEmreeLRR--LQRELG-ITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
315-515 |
1.29e-19 |
|
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: 92.09 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 315 SLRLQR---TLyNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------------FAYVAQ 374
Cdd:COG4148 6 DFRLRRggfTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 375 QAwILNATL--RDNILFG-----KEFDEERYNSVLnscclrpdlailpnsDLTEIG---ERG-ANLSGGQRQRISLARAL 443
Cdd:COG4148 85 EA-RLFPHLsvRGNLLYGrkrapRAERRISFDEVV---------------ELLGIGhllDRRpATLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 444 YSDRSIYILDDPLSALDAHvgnhifnsaiRK--------RLKSKT---VLFVTHQL---QYLvdCDEVIFMKEGCITERG 509
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLA----------RKaeilpyleRLRDELdipILYVSHSLdevARL--ADHVVLLEQGRVVASG 216
|
....*.
gi 1720387222 510 THEELM 515
Cdd:COG4148 217 PLAEVL 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
315-520 |
2.13e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.66 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 315 SLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYVAQ-------QAWILNA--T 382
Cdd:COG3840 8 TYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAErpvsmlfQENNLFPhlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFGkefdeerynsvlnsccLRPDL-----------AILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIY 450
Cdd:COG3840 88 VAQNIGLG----------------LRPGLkltaeqraqveQALERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 451 ILDDPLSALD--------AHVgnhifnSAIRKRLKSkTVLFVTHQLQylvD----CDEVIFMKEGCITERGTHEELMNLN 518
Cdd:COG3840 152 LLDEPFSALDpalrqemlDLV------DELCRERGL-TVLMVTHDPE---DaariADRVLLVADGRIAADGPTAALLDGE 221
|
..
gi 1720387222 519 GD 520
Cdd:COG3840 222 PP 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
952-1152 |
2.99e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 87.57 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISdiGLADLRSKLAIIPQEPVLFSG-TVRSN 1030
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LDpF--------NQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:cd03259 93 IA-FglklrgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1103 MDTETDLLIQETIREAFA--DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1152
Cdd:cd03259 161 LDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
953-1146 |
3.25e-19 |
|
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: 87.77 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSK----LAIIPQEPVLFSGTVR 1028
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNL---DPFNQYTEDQIWDALErthMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1105
Cdd:cd03290 97 ENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720387222 1106 E-TDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQG 1146
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
952-1148 |
3.59e-19 |
|
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: 87.20 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISD--IGLADLRSKLAIIPQEPVLFSG-TVR 1028
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLdpfnqyTEDQIW--------------DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKIL 1094
Cdd:cd03262 95 ENI------TLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1095 ILDEATAAMDTEtdlLIQE---TIREAFAD-CTMLTIAHRlhtvLG-----SDRIMVLAQGQV 1148
Cdd:cd03262 158 LFDEPTSALDPE---LVGEvldVMKDLAEEgMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
15-211 |
4.65e-19 |
|
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: 88.76 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 15 KSLGELINICSNDGQRMfeAAAVGSL--LAGGPV-VAI-LGMIY---NVIILGptgflGSAVFILFYPAMMFVSRLTAYF 87
Cdd:cd18598 92 FSTGEIVNLMSTDADRI--VNFCPSFhdLWSLPLqIIVaLYLLYqqvGVAFLA-----GLVFALVLIPINKWIAKRIGAL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 88 RRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITV---GVAPIVVviaSVVTFSV 164
Cdd:cd18598 165 SEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVyfwATTPVLI---SILTFAT 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 165 HMTLGFHLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRF 211
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
936-1168 |
5.30e-19 |
|
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: 87.83 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSL-GMALFRLVELSGGCIKIDGIRISDIGLADLRSKLA 1014
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1015 II---------PQEPVL------FSGTVrsnlDPFNQYTEDQI---WDALERTHMKECIAQLPLKLesevmengdnfSVG 1076
Cdd:COG1119 82 LVspalqlrfpRDETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-----------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1077 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF-D 1152
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAgP 226
|
250
....*....|....*.
gi 1720387222 1153 TPSVLLSNDSSRFYAM 1168
Cdd:COG1119 227 KEEVLTSENLSEAFGL 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
319-514 |
5.78e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.88 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAIlgqmTLLE---------GSIAVSGTFAYVAQQAWILNatLRDNILF 389
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeagtirvGDITIDTARSLSQQKGLIRQ--LRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 -GKEFDEERYNSVLNSCCLRP--------DLAI-LPNSDLTEIGERGAN------LSGGQRQRISLARALYSDRSIYILD 453
Cdd:PRK11264 90 vFQNFNLFPHRTVLENIIEGPvivkgepkEEATaRARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 454 DPLSALDAHVGNHIFNSaIRKRLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:PRK11264 170 EPTSALDPELVGEVLNT-IRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
936-1159 |
8.98e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.86 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLP-LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLA 1014
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1015 IIPQepvlfsgtvrsnlDPFNQYT----EDQIWDALE-----RTHMKECIAQlplKLESEVMENGDN-----FSVGERQL 1080
Cdd:PRK13650 85 MVFQ-------------NPDNQFVgatvEDDVAFGLEnkgipHEEMKERVNE---ALELVGMQDFKEreparLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1081 LCIARALLRHCKILILDEATAAMDTETDL-LIQ--ETIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1157
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLeLIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
..
gi 1720387222 1158 LS 1159
Cdd:PRK13650 228 FS 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
322-514 |
9.61e-19 |
|
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: 86.47 E-value: 9.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAI-----LGQMTLLEGSIAVSG---------------TFAYVAQQAWILNA 381
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLRDNILFG--------KEFDEERYNSVLnscclrpDLAILPNsdltEIGER--GANLSGGQRQRISLARALYSDRSIYI 451
Cdd:cd03260 96 SIYDNVAYGlrlhgiklKEELDERVEEAL-------RKAALWD----EVKDRlhALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 452 LDDPLSALDAhVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 514
Cdd:cd03260 165 LDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
952-1155 |
9.72e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGIRISDIG---LADLRSKLAIIPQEPvlfsgtvR 1028
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLDPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMEN-----------GDNFSVGERQLLCIARALLRHCKILILD 1097
Cdd:PRK15134 373 SSLNP--RLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgldpetrhryPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1098 EATAAMDTETD-----LL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTPS 1155
Cdd:PRK15134 451 EPTSSLDKTVQaqilaLLksLQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVEqgdcervFAAPQ 518
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
939-1155 |
1.06e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.80 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISD--IGLADLRSKL 1013
Cdd:PRK13637 6 ENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEP--VLFSGTVRSNLD--PFN-QYTEDQIWDALERThMKEciaqlpLKLESEVMENGDNF--SVGERQLLCIARA 1086
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAfgPINlGLSEEEIENRVKRA-MNI------VGLDYEDYKDKSPFelSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1087 LLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI--AHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1155
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlvSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
660-1150 |
1.19e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 92.35 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 660 IYALSMAVMLILKAIRGVVFVKGTLRASSRLHDEL----FRRILRSPMKFFDTTPTGRILNRFSKDMDEVDvrlpfQAEM 735
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLvaaiFHKSLRLTHEARKNFASGKVTNMITTDANALQ-----QIAE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 736 FIQNVILVFFCVgMIAGVFPWFLVAVGPL---LILFsLLHIVSRVLIRELKRL--DNITQSPFLSHITSSI-QGLATIHA 809
Cdd:PLN03232 417 QLHGLWSAPFRI-IVSMVLLYQQLGVASLfgsLILF-LLIPLQTLIVRKMRKLtkEGLQWTDKRVGIINEIlASMDTVKC 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 810 YNKRQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFT 889
Cdd:PLN03232 495 YAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNML 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 890 VRLASETEARFTSVERINHYIktLSLEapaRIKNKAPPHDwPQEGEVTFENAEMRYRENLPL-VLKKVSFTIKPKEKIGI 968
Cdd:PLN03232 575 PNLLSQVVNANVSLQRIEELL--LSEE---RILAQNPPLQ-PGAPAISIKNGYFSWDSKTSKpTLSDINLEIPVGSLVAI 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 969 VGRTGSGKSSLGMALfrLVELSGgcikidgiriSDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALER 1048
Cdd:PLN03232 649 VGGTGEGKTSLISAM--LGELSH----------AETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDV 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1049 THMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTE-TDLLIQETIREAFADCTMLTI 1127
Cdd:PLN03232 717 TALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLV 796
|
490 500
....*....|....*....|...
gi 1720387222 1128 AHRLHTVLGSDRIMVLAQGQVVE 1150
Cdd:PLN03232 797 TNQLHFLPLMDRIILVSEGMIKE 819
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
936-1149 |
1.22e-18 |
|
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: 85.88 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDiGLADLRSKL 1013
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSG-TVRSNLDPFNQYTedqiwdALERTHMKECIAQLPLKLE-SEVME-NGDNFSVGERQLLCIARALLRH 1090
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLY------GLKGDELTARLEELADRLGmEELLDrRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1091 CKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
322-503 |
1.44e-18 |
|
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: 84.91 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTL--LEGSIAVSGT----------FAYVAQQ-AWILNATLRDNIL 388
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FgkefdeerynsvlnSCCLRpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF 468
Cdd:cd03213 105 F--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720387222 469 NSAIRKRLKSKTVLFVTHQLQYLV--DCDEVIFMKEG 503
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
952-1161 |
2.40e-18 |
|
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: 85.42 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADL-RSKLAIIPQEPVLFSG-TVRS 1029
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLD--PFNQYTEDQIWDALERTH-----MKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1103 mdtetdL--LIQETIREAFAD-----CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1161
Cdd:COG0410 167 ------LapLIVEEIFEIIRRlnregVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
952-1160 |
2.52e-18 |
|
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: 85.57 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGIRISDIGlADLRSKLAIIP--QEPVLFSG 1025
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 -TVRSNL----------DPFNQYTEDQIWDALERTHmkECIAQLPLkleSEVM-ENGDNFSVGERQLLCIARALLRHCKI 1093
Cdd:cd03219 90 lTVLENVmvaaqartgsGLLLARARREEREARERAE--ELLERVGL---ADLAdRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1094 LILDEATAAM-DTETDLLIqETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:cd03219 165 LLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
310-524 |
2.85e-18 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 86.12 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 310 QIHTGSLR----LQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYV 372
Cdd:cd03288 21 KIHDLCVRyennLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 373 AQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYIL 452
Cdd:cd03288 101 LQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 453 DDPLSALDAHVGNhIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELM-NLNGDYATI 524
Cdd:cd03288 181 DEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-516 |
3.25e-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: 85.43 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQAWIL-NATLRDNI-- 387
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEENIal 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 ---LFG--KEFDEERYNSVLNSCCLRPdlailpnsdlTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:cd03295 99 vpkLLKwpKEKIRERADELLALVGLDP----------AEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 462 HVGNHIFNSAIR-KRLKSKTVLFVTHQLQ-YLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03295 169 ITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
322-516 |
3.49e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 85.08 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILF 389
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 G----KEFDEERYNSVLNsccLRPDLAIlpnsdlTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 464
Cdd:cd03299 95 GlkkrKVDKKEIERKVLE---IAEMLGI------DHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 465 nhifNSAIRKRLK------SKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03299 165 ----KEKLREELKkirkefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
952-1160 |
4.17e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 85.48 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGIRISdiGL-ADLRSKLAI-----IPQepv 1021
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDIT--GLpPHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1022 LFSG-TVRSN-----------------LDPFNQYTE-----DQIWDALERTHMKECIAQLPlklesevmengDNFSVGER 1078
Cdd:COG0411 90 LFPElTVLENvlvaaharlgrgllaalLRLPRARREerearERAEELLERVGLADRADEPA-----------GNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1079 QLLCIARALLRHCKILILDEATAAM-DTETDLLIqETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1154
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTP 237
|
....*.
gi 1720387222 1155 SVLLSN 1160
Cdd:COG0411 238 AEVRAD 243
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
315-515 |
5.08e-18 |
|
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: 87.09 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 315 SLRLQRTLYN----IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------------FAYVA 373
Cdd:TIGR02142 2 SARFSKRLGDfsldADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 374 QQAWIL-NATLRDNILFGKEF--------DEERYNSVLNsccLRPDLAILPNSdlteigerganLSGGQRQRISLARALY 444
Cdd:TIGR02142 82 QEARLFpHLSVRGNLRYGMKRarpserriSFERVIELLG---IGHLLGRLPGR-----------LSGGEKQRVAIGRALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 445 SDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSKT---VLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 515
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDDPRKYEIL--PYLERLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
322-498 |
7.33e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG--TFAYVAQQ---AWILNATLRDNI---LFGKEF 393
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 394 DEERYN----SVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 469
Cdd:NF040873 88 LWRRLTrddrAAVDDALERVGLADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 1720387222 470 SAIRKRLKSKTVLFVTHQLQYLVDCDEVI 498
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
321-509 |
7.94e-18 |
|
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: 83.46 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-----------TFAYVAQQ-AWILNATLRDNIL 388
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FG-------KEFDEERYNSVlnscclrpdlailpnSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:cd03301 95 FGlklrkvpKDEIDERVREV---------------AELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 458 ALDAHVgnhifNSAIRKRLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERG 509
Cdd:cd03301 160 NLDAKL-----RVQMRAELKRlqqrlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
314-500 |
9.44e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.53 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 314 GSLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------FAYVAQQ----AWiLNA 381
Cdd:COG4525 15 GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadRGVVFQKdallPW-LNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 tlRDNILFGKefdeeRYNSVLNSCCLRPDLAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:COG4525 94 --LDNVAFGL-----RLRGVPKAERRARAEELLALVGLADFARRRiWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720387222 461 AhvgnhifnsAIRKRLKS----------KTVLFVTHqlqylvDCDEVIFM 500
Cdd:COG4525 167 A---------LTREQMQEllldvwqrtgKGVFLITH------SVEEALFL 201
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
931-1170 |
1.66e-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: 83.60 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 931 PQEGEVTFENAEMRYRENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGIRISDI 1004
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1005 GladlrSKLAIIPQEPVLFs-gTVRSN---------LDPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfS 1074
Cdd:COG1116 79 G-----PDRGVVFQEPALLpwlTVLDNvalglelrgVPK--AERRERARELLELVGLAGFEDAYPHQL-----------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1075 VGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAH------RLhtvlgSDRIMVLAQ- 1145
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
250 260 270
....*....|....*....|....*....|.
gi 1720387222 1146 -GQV-----VEFDTPSVLLSNDSSRFYAMFA 1170
Cdd:COG1116 216 pGRIveeidVDLPRPRDRELRTSPEFAALRA 246
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
322-516 |
1.79e-17 |
|
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: 83.85 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------------FAYVAQQ-AWILNATL 383
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNILFG-------KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 457 SALDahvgnhifnSAIRKRLKS----------KTVLFVTHqlqylvDCDEVI-------FMKEGCITERGTHEELMN 516
Cdd:cd03294 189 SALD---------PLIRREMQDellrlqaelqKTIVFITH------DLDEALrlgdriaIMKDGRLVQVGTPEEILT 250
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
18-210 |
2.16e-17 |
|
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: 84.19 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 18 GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDD 97
Cdd:cd18559 95 GELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 98 RVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFH--LTAA 175
Cdd:cd18559 175 RYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLagLVAL 254
|
170 180 190
....*....|....*....|....*....|....*
gi 1720387222 176 QAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 210
Cdd:cd18559 255 KVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
322-514 |
2.20e-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: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQQ-AWILNATLR 384
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGKEfdeeRYNSVLNSCCLRPD-------LAILPNSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:cd03256 97 ENVLSGRL----GRRSTWRSLFGLFPkeekqraLAALERVGLLDkAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 457 SALD---AHVGNHIFNSAIRKrlKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:cd03256 173 ASLDpasSRQVMDLLKRINRE--EGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
657-1098 |
3.25e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 86.39 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 657 YASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMD---EVDVRLPFqa 733
Cdd:COG4615 50 LLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 734 emFIQNVILVFFCVGMIAgvfpW-----FLVAVGPLLILFSLLHIVSRVLIRELKRLDNiTQSPFLSHITSSIQGLA--T 806
Cdd:COG4615 128 --LLQSVALVLGCLAYLA----WlspplFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLFKHFRALLEGFKelK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 807 IHAyNKRQEFLHRY-----QELLDDNQAPFFLFTCAMRWlavrldlISIALITTTGLmIVLMHGQIPSAYAGLAISYAvq 881
Cdd:COG4615 201 LNR-RRRRAFFDEDlqptaERYRDLRIRADTIFALANNW-------GNLLFFALIGL-ILFLLPALGWADPAVLSGFV-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 882 LTGLF------QFTVRLASETEARfTSVERINHYikTLSLEAPARIKNKAPPHDWPQE-GEVTFENAEMRYR---ENLPL 951
Cdd:COG4615 270 LVLLFlrgplsQLVGALPTLSRAN-VALRKIEEL--ELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPgedGDEGF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFsgtvRSNL 1031
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1032 DPFNQYTEDQIWDALERthmkeciaqlpLKLESEVMENGDNF-----SVGERQLLCIARALLRHCKILILDE 1098
Cdd:COG4615 423 GLDGEADPARARELLER-----------LELDHKVSVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
324-539 |
3.91e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYVAQ-------QAWIL--NATLRDNILFGK 391
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQrdicmvfQSYALfpHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 392 EF----DEERYNSVlnscclRPDLAILpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvgnh 466
Cdd:PRK11432 104 KMlgvpKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 467 ifnsaIRKRLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL---------MNLNGDyATIFN 526
Cdd:PRK11432 171 -----LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpasrfmASFMGD-ANIFP 244
|
250
....*....|...
gi 1720387222 527 NLLLGETppVEIN 539
Cdd:PRK11432 245 ATLSGDY--VDIY 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
953-1150 |
4.03e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.45 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRI---SDIGLADLRSKLAIIPQEPVlfsgtvrS 1029
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLDPfNQYTEDQIWDALeRTH-----------MKECIAQLPLKLEsEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1098
Cdd:PRK10261 413 SLDP-RQTVGDSIMEPL-RVHgllpgkaaaarVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1099 ATAAMDTET-----DLL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:PRK10261 490 AVSALDVSIrgqiiNLLldLQRDFGIAY-----LFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
298-487 |
5.24e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 298 DERPSPEEEEGKQIHTGSLRLQ----RTLY-NIDLEIEEGKLVGICGSVGSGKTSLVSAILGqmtlL----EGSIAV--S 366
Cdd:COG4178 350 EAASRIETSEDGALALEDLTLRtpdgRPLLeDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 367 GTFAYVAQQAWILNATLRDNILF---GKEFDEERYNSVLNSCCLrPDLAilpnSDLTEIGERGANLSGGQRQRISLARAL 443
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLA----ERLDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720387222 444 YSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLKSKTVLFVTHQ 487
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALY-QLLREELPGTTVISVGHR 543
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
937-1171 |
7.59e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.95 E-value: 7.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 937 TFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADlRsKLAII 1016
Cdd:COG3840 3 RLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1017 PQEPVLFSG-TVRSN----LDPFNQYTEDQ---IWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1088
Cdd:COG3840 77 FQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1089 RHCKILILDEATAAMD----TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSS 1163
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*...
gi 1720387222 1164 rfyAMFAA 1171
Cdd:COG3840 224 ---PALAA 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
952-1149 |
7.84e-17 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.90 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGIRISDIglaDLRSKLAIIPQEPVLFSG-TVR 1028
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLdpfnQYTedqiwdalerthmkeciAQLplklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1108
Cdd:cd03213 101 ETL----MFA-----------------AKL------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720387222 1109 LLIQETIRE-AFADCTMLTIAHRLHTVLGS--DRIMVLAQGQVV 1149
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
315-509 |
9.96e-17 |
|
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: 80.23 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 315 SLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYVAQQAwiLNATLRDNILFGK 391
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP--VSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 392 EFDEERYnsvlnscclrpDLAILPNSDLTEIgERGA-------------------NLSGGQRQRISLARALYSDRSIYIL 452
Cdd:cd03298 85 LTVEQNV-----------GLGLSPGLKLTAE-DRQAievalarvglaglekrlpgELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 453 DDPLSALDAHVGNHIFNSAIRKRLKSK-TVLFVTHQLQYLVDCDE-VIFMKEGCITERG 509
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
952-1180 |
1.80e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.22 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIkPKEKIGIV-GRTGSGKSSLGMALFRLVELSGGCIkidgirisdigLADlRSkLAIIPQEPVLFSGTVRSN 1030
Cdd:PTZ00243 675 LLRDVSVSV-PRGKLTVVlGATGSGKSTLLQSLLSQFEISEGRV-----------WAE-RS-IAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-DL 1109
Cdd:PTZ00243 741 ILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgER 820
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1110 LIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQvVEFdtpsvllSNDSSRF-----YAMFAA--AENKVAVKG 1180
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR-VEF-------SGSSADFmrtslYATLAAelKENKDSKEG 890
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
322-516 |
1.90e-16 |
|
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: 81.05 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILgQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNI- 387
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFGKEFDEERYNsVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhI 467
Cdd:cd03289 99 PYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-----I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 468 FNSAIRKRLKSK----TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03289 173 TYQVIRKTLKQAfadcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
324-516 |
1.99e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 80.02 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQQAwilnA-----T 382
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrrrIGMLFQGG----AlfdslT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFG-KEF----DEERYNSVLNScclrpdlailpnsdLTEIGERGAN------LSGGQRQRISLARALYSDRSIYI 451
Cdd:COG1127 99 VFENVAFPlREHtdlsEAEIRELVLEK--------------LELVGLPGAAdkmpseLSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 452 LDDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:COG1127 165 YDEPTAGLDPITSAVIDEliRELRDELGL-TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
936-1163 |
2.51e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.57 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIkPKEK-IGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLA 1014
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNI-PKGQwTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1015 IIPQEPV-LFSGT-----VRSNLDPFNQYTEDqiwdalerthMKECIAQLpLKlESEVMENGDN----FSVGERQLLCIA 1084
Cdd:PRK13648 87 IVFQNPDnQFVGSivkydVAFGLENHAVPYDE----------MHRRVSEA-LK-QVDMLERADYepnaLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1085 RALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1162
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 1720387222 1163 S 1163
Cdd:PRK13648 235 E 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
952-1160 |
2.55e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.08 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDG--IRISDIGLADLRSKLAIIPQEPVLFS 1024
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGedIYDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1025 GTV---------------RSNLDpfnqytedqiwDALERThmkeciaqlpLK---LESEV----MENGDNFSVGERQLLC 1082
Cdd:COG1117 106 KSIydnvayglrlhgiksKSELD-----------EIVEES----------LRkaaLWDEVkdrlKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1083 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSV 1156
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQ 239
|
....
gi 1720387222 1157 LLSN 1160
Cdd:COG1117 240 IFTN 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
307-506 |
2.62e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 78.84 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 307 EGKQIHTGSLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG----------TFAYVAQQA 376
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 377 wilnatlrDNILFGkefdeeryNSVLNSCCLRPDLA---------ILPNSDLTEIGERG-ANLSGGQRQRISLARALYSD 446
Cdd:cd03226 81 --------DYQLFT--------DSVREELLLGLKELdagneqaetVLKDLDLYALKERHpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 447 RSIYILDDPLSALDAH----VGNHIfnsairKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT 506
Cdd:cd03226 145 KDLLIFDEPTSGLDYKnmerVGELI------RELAAqgKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
936-1168 |
2.70e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.42 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIG-LADLRSKLA 1014
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1015 IIPQEP-VLFSG-TVRSNLdPFNqyTEDQIWDALE-RTHMKECIAQlpLKLESEVMENGDNFSVGERQLLCIARALLRHC 1091
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL-AFG--PENLCLPPIEiRKRVDRALAE--IGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1092 KILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1168
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
319-516 |
2.85e-16 |
|
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: 79.59 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDN 386
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNyALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFG-------KEFDEERYNSVLnscclrpDLAilpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:cd03300 93 IAFGlrlkklpKAEIKERVAEAL-------DLV-----QLEGYANRKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 459 LDAHVGNHIFN--SAIRKRLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03300 161 LDLKLRKDMQLelKRLQKELGI-TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
308-507 |
3.33e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 308 GKQIHTGSLRL----QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---------------- 367
Cdd:PRK10419 10 SHHYAHGGLSGkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 368 TFAYVAQQA-----------WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQR 436
Cdd:PRK10419 90 DIQMVFQDSisavnprktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL----------DKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 437 ISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSKT---VLFVTHQLQyLVD--CDEVIFMKEGCITE 507
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVI--RLLKKLQQQFgtaCLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
319-534 |
3.58e-16 |
|
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: 79.85 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG----------------TFAYVAQQA------ 376
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 377 -----WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRSIYI 451
Cdd:TIGR02769 104 rmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDA----------DKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 452 LDDPLSALDAHVGNHIFnsAIRKRLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMNLNGDYATIFN 526
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVIL--ELLRKLQQAfgtAYLFITHDLR-LVQsfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQ 250
|
....*...
gi 1720387222 527 NLLLGETP 534
Cdd:TIGR02769 251 SAVLPEHP 258
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
322-563 |
4.60e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQQAWILNATLRD 385
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklvgIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGKEfdeerynsvlnSCCLRP-DLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:PRK13644 98 DLAFGPE-----------NLCLPPiEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 459 LDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEelmnlngdyaTIFNNL---LLGETPP 535
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE----------NVLSDVslqTLGLTPP 236
|
250 260 270
....*....|....*....|....*....|
gi 1720387222 536 --VEINSKKEATGSQKSQDKGPKPGSVKKE 563
Cdd:PRK13644 237 slIELAENLKMHGVVIPWENTSSPSSFAEE 266
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
953-1149 |
4.93e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgM-ALFRLVELSGGCIKIDG--IRISDIGLAdLRSKLAIIPQEPVLFSG-TVR 1028
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSPRDA-IALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNL----DPFNQYTEDqiWDALeRTHMKECIAQLPLKL--ESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:COG3845 99 ENIvlglEPTKGGRLD--RKAA-RARIRELSERYGLDVdpDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1103 M-DTETDLLIqETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:COG3845 172 LtPQEADELF-EILRR-LAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
936-1150 |
5.15e-16 |
|
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: 78.28 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGladlrSKL 1013
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFS-GTVRSN--LDPfnqytEDQIWDALE-RTHMKECIAQLPLKlesevmENGDNF----SVGERQLLCIAR 1085
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGL-----ELQGVPKAEaRERAEELLELVGLS------GFENAYphqlSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1086 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLH-TVLGSDRIMVLAQ--GQVVE 1150
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
952-1149 |
6.39e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAdLRSKLAI--IPQEPVLFSG-TVR 1028
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLD---PFNQytedqiwDALERthMKECIAQLPLKLESEVmeNGDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 1104
Cdd:PRK15439 105 ENILfglPKRQ-------ASMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 1105 TETDLLIQEtIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:PRK15439 174 AETERLFSR-IRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
952-1161 |
7.59e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 7.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVL-FSGTVRS- 1029
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 ---NLDPFNQ-YTEDQ--IWDALERThmkECIA-------QLplklesevmengdnfSVGERQLLCIARAL--LRHC--- 1091
Cdd:PRK13548 97 vamGRAPHGLsRAEDDalVAAALAQV---DLAHlagrdypQL---------------SGGEQQRVQLARVLaqLWEPdgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1092 -KILILDEATAAMdtetDLLIQETIreafadctmLTIAHR------------LH----TVLGSDRIMVLAQGQVVEFDTP 1154
Cdd:PRK13548 159 pRWLLLDEPTSAL----DLAHQHHV---------LRLARQlaherglavivvLHdlnlAARYADRIVLLHQGRLVADGTP 225
|
....*..
gi 1720387222 1155 SVLLSND 1161
Cdd:PRK13548 226 AEVLTPE 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
322-505 |
1.20e-15 |
|
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: 77.18 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWilnATLRDNIlfGKEFdeERYN-- 399
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI---NELRQKV--GMVF--QQFNlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 400 ---SVLNSCCLRPDLAI-LPNSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:cd03262 89 phlTVLENITLAPIKVKgMSKAEAEERALEllekvGladkadaypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 462 HVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCI 505
Cdd:cd03262 169 ELVGEVLD--VMKDLAEEgmTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
322-516 |
1.21e-15 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 77.47 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQ-QAWILNATLRDN 386
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFG-----KEFDEERYNSVlnscclrpdLAILPNsdLTEI-GERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:cd03224 96 LLLGayarrRAKRKARLERV---------YELFPR--LKERrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 461 AHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
322-514 |
1.42e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAIlgqmTLLE----GSIAVSGT--------------------FayvaQQAW 377
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGVdltalserelraarrkigmiF----QHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ILNA-TLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYS 445
Cdd:COG1135 93 LLSSrTVAENVALpleiagvPKAEIRKRVAELL---------------ELVGLSDKAdaypSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 446 DRSIYILDDPLSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHQLqylvD-----CDEVIFMKEGCITERGTHEEL 514
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDllKDINRELG-LTIVLITHEM----DvvrriCDRVAVLENGRIVEQGPVLDV 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
319-515 |
1.61e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWI-LNATLR 384
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGKEFDEERYN-------SVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:PRK09536 96 QVVEMGRTPHRSRFDtwtetdrAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 458 ALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 515
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
936-1160 |
2.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.92 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLV---ELSGGCIKIDGIRISDIGLADLRSK 1012
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1013 LAIIPQepvlfsgtvrsnlDPFNQY----TEDQIWDALE-----RTHMKECIAQLplkLESEVMEN-----GDNFSVGER 1078
Cdd:PRK13640 86 VGIVFQ-------------NPDNQFvgatVGDDVAFGLEnravpRPEMIKIVRDV---LADVGMLDyidsePANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1079 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1156
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
....
gi 1720387222 1157 LLSN 1160
Cdd:PRK13640 230 IFSK 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
322-503 |
2.67e-15 |
|
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: 74.77 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTfayvaqqawilnatlrdnilfgkefdEERYNSv 401
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 402 lnscclrPDLAIlpnsdlteigERGAN----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLK 477
Cdd:cd03216 69 -------PRDAR----------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF--KVIRRLR 129
|
170 180
....*....|....*....|....*....
gi 1720387222 478 S--KTVLFVTHQLQYLVD-CDEVIFMKEG 503
Cdd:cd03216 130 AqgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
326-509 |
2.82e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.05 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 326 DLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQAWIL-NATLRDNILFG--- 390
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 391 ----KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 466
Cdd:TIGR01277 98 glklNAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 467 IFnsAIRKRL---KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 509
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
324-487 |
3.32e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYVAQQAWIL---NA-----TLRDNILFGKE 392
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLghrNAmkpalTVAENLEFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 393 FdeerynsvLNSCCLRPD--LAILPNSDLTEIgeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNS 470
Cdd:PRK13539 100 F--------LGGEELDIAaaLEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAE 168
|
170
....*....|....*...
gi 1720387222 471 AIRKRLKSK-TVLFVTHQ 487
Cdd:PRK13539 169 LIRAHLAQGgIVIAATHI 186
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
310-516 |
5.24e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 76.41 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 310 QIHTGSLRLQR--TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------FAYVAQQ------ 375
Cdd:COG4167 15 KYRTGLFRRQQfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdYKYRCKHirmifq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 376 ------------AWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARA 442
Cdd:COG4167 95 dpntslnprlniGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHAnFYPHM-----------LSSGQKQRVALARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 443 LYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKRLKSKTVlFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 516
Cdd:COG4167 164 LILQPKIIIADEALAALDMSVRSQIINlmLELQEKLGISYI-YVSQHLG-IVKhiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-503 |
5.68e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 74.39 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 316 LRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVA----QQAW 377
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ILNATLRDNILfgkefdeerynsvlnscclrpdLAILpnsdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:cd03215 90 VLDLSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 458 ALDahVG--NHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 503
Cdd:cd03215 134 GVD--VGakAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
939-1174 |
6.64e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 75.45 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYREnlpLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGIRIS----DI-GLADLRSKL 1013
Cdd:cd03299 4 ENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVL-------LETIAGFIKPDSGKILlngkDItNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSgtvrsnldpfNQYTEDQIWDALE-RTHMKEciaqlplKLESEVME-------------NGDNFSVGERQ 1079
Cdd:cd03299 74 SYVPQNYALFP----------HMTVYKNIAYGLKkRKVDKK-------EIERKVLEiaemlgidhllnrKPETLSGGEQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1080 LLCIARALLRHCKILILDEATAAMDTET-DLLIQE--TIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1155
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDVRTkEKLREElkKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPE 215
|
250
....*....|....*....
gi 1720387222 1156 VLLSNDSSRFYAMFAAAEN 1174
Cdd:cd03299 216 EVFKKPKNEFVAEFLGFNN 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
322-503 |
9.45e-15 |
|
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: 72.48 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--FAYVAQqawilnatlrdnilfgkefdeeryn 399
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 400 svlnscclrpdlailpnsdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDahvgnhIFN-SAIRKRLKS 478
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD------LESiEALEEALKE 115
|
170 180
....*....|....*....|....*....
gi 1720387222 479 --KTVLFVTHQlQYLVD--CDEVIFMKEG 503
Cdd:cd03221 116 ypGTVILVSHD-RYFLDqvATKIIELEDG 143
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
952-1156 |
9.79e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 74.78 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDI---GLADLRS-KLAIIPQ--------- 1018
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRArHVGFVFQsfqllptlt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 --EPVLFSGTVRSNLDPFNQYTEdqiwdALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1096
Cdd:COG4181 107 alENVMLPLELAGRRDARARARA-----LLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1097 DEATAAMDTET-----DLLIQETiREAFAdcTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1156
Cdd:COG4181 171 DEPTGNLDAATgeqiiDLLFELN-RERGT--TLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
939-1159 |
1.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRY-RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIP 1017
Cdd:PRK13642 8 ENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1018 QEP-VLFSGTVRSNLDPFNQytEDQiwdALERTHMKECI--AQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKIL 1094
Cdd:PRK13642 88 QNPdNQFVGATVEDDVAFGM--ENQ---GIPREEMIKRVdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1095 ILDEATAAMD----TETDLLIQEtIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHE-IKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
322-516 |
1.07e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.80 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG------TFAYVAQQAWI---------LNATLRDN 386
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIGIifqnpdnqfIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIGERGA------NLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:PRK13632 105 IAFGLE----------NKKVPPKKMKDIIDDLAKKVGMEDYldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 461 AHVGNHI--FNSAIRKRlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK13632 175 PKGKREIkkIMVDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
654-889 |
1.14e-14 |
|
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: 75.89 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 654 MQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqA 733
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------N 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 734 EMFIQNVILVFFCVGMIAGVF----------PWFLVAVGPLLILFSLLH-IVSRVLIRELKRLdnitqspfLSHITS--- 799
Cdd:cd18544 113 ELFTSGLVTLIGDLLLLIGILiamfllnwrlALISLLVLPLLLLATYLFrKKSRKAYREVREK--------LSRLNAflq 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 800 -SIQGLATIHAYNKRQEFLHRYQELlddNQApffLFTCAMRwlAVRLDLI---SIALITTTGLMIVLMHGqipsayAGLA 875
Cdd:cd18544 185 eSISGMSVIQLFNREKREFEEFDEI---NQE---YRKANLK--SIKLFALfrpLVELLSSLALALVLWYG------GGQV 250
|
250
....*....|....
gi 1720387222 876 ISYAVQLTGLFQFT 889
Cdd:cd18544 251 LSGAVTLGVLYAFI 264
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
950-1160 |
1.40e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 950 PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIG-LADLRSK------------LAII 1016
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKagmvfqnpdnqiVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1017 PQEPVLFSgtvRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1096
Cdd:PRK13633 103 VEEDVAFG---PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 1097 DEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
320-505 |
1.61e-14 |
|
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: 74.23 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQM---TLLEGSIAVSGT----------FAYVAQQ-AWILNATLRD 385
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQprkpdqfqkcVAYVRQDdILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILF------GKEFDEERYNSVLNSCCLRpDLAIlpnsdlTEIG-ERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:cd03234 101 TLTYtailrlPRKSSDAIRKKRVEDVLLR-DLAL------TRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 459 LDAHVGNHIFNSAIRKRLKSKTVLFVTHQ-----LQYLvdcDEVIFMKEGCI 505
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
322-517 |
1.62e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.91 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-TFAYVAQQAWILNA-----------TLRDNILF 389
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 GkefdeerynsvlnsccLRpdLAILPNSD-------------LTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:PRK09452 110 G----------------LR--MQKTPAAEitprvmealrmvqLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 456 LSALDAHVGNHIFNSAirKRLKSK---TVLFVTH-QLQYLVDCDEVIFMKEGCITERGT----HEELMNL 517
Cdd:PRK09452 172 LSALDYKLRKQMQNEL--KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEEPKNL 239
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
902-1179 |
2.00e-14 |
|
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: 78.45 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 902 SVERINHYIKTLSLEaPARIKNKAPPhdwPQEG-EVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLG 980
Cdd:TIGR00957 606 SLKRLRIFLSHEELE-PDSIERRTIK---PGEGnSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 981 MALFRLVELSGGCIKIDGirisdigladlrsKLAIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPL 1060
Cdd:TIGR00957 682 SALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPS 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1061 KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI---REAFADCTMLTIAHRLHTVLGS 1137
Cdd:TIGR00957 749 GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQV 828
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720387222 1138 DRIMVLAQGQVVEFDTPSVLLSNDSS--RFYAMFAAAENKVAVK 1179
Cdd:TIGR00957 829 DVIIVMSGGKISEMGSYQELLQRDGAfaEFLRTYAPDEQQGHLE 872
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-500 |
2.00e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI-----AVSGTFA---YVAQQAWILN-ATLRDNILF 389
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkPVEGPGAergVVFQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 GKEF----DEERYNSVLnscclrpdlAILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 464
Cdd:PRK11248 94 GLQLagveKMQRLEIAH---------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720387222 465 NHIFNSAIRK-RLKSKTVLFVTHqlqylvDCDEVIFM 500
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITH------DIEEAVFM 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
946-1169 |
2.11e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.61 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 946 RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRS----KLAIIPQEPV 1021
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1022 LFSG-TVRSNldpfNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1100
Cdd:PRK10070 117 LMPHmTVLDN----TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1101 AAMDTETDLLIQETI--REAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 1169
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
369-516 |
2.61e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 369 FAYVAQQAWILNATLRDNILFGKE-FDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDR 447
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 448 SIYILDDPLSALDAHVGNHIFNSAIRKRLKS-KTVLFVTHQLQYLVDCDEVIFM----KEGCITE-RGTHEELMN 516
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLS 1452
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
952-1150 |
2.95e-14 |
|
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: 74.46 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDI---GLADLRSKLAIIPQE-PVLFSG-- 1025
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 TVRSNL-DPFNQYTEdqiwdaLERTHMKECIAQL--PLKLESEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEATA 1101
Cdd:TIGR02769 106 TVRQIIgEPLRHLTS------LDESEQKARIAELldMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1102 AMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:TIGR02769 180 NLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
649-906 |
3.04e-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: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 649 KDNPFMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVR 728
Cdd:cd07346 33 GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 729 LPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIH 808
Cdd:cd07346 113 VSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 809 AYNKRQEFLHRYQELLDDNqapFFLFTCAMRWLAvrLDLISIALITTTGLMIVL-------MHGQIPSAYAGLAISYAVQ 881
Cdd:cd07346 193 AFAAEEREIERFREANRDL---RDANLRAARLSA--LFSPLIGLLTALGTALVLlyggylvLQGSLTIGELVAFLAYLGM 267
|
250 260
....*....|....*....|....*
gi 1720387222 882 LTGLFQFTVRLASETEARFTSVERI 906
Cdd:cd07346 268 LFGPIQRLANLYNQLQQALASLERI 292
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
322-517 |
3.10e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.58 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFayvaqqAWIL--------NATLRDNILFG--- 390
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLelgagfhpELTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 391 ----KEFDEERYNSVLnscclrpdlailpnsDLTEIGE------RgaNLSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 461 AHvgnhiFN----SAIRKRLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNL 517
Cdd:COG1134 179 AA-----FQkkclARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
952-1175 |
3.35e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.03 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGiRISdigladlrsklaIIPQEPVLFSGTVRSNL 1031
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RIS------------FSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 DPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDlli 1111
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE--- 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1112 qetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENK 1175
Cdd:TIGR01271 585 ----KEIFESCLCKLMSNK-------TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
337-514 |
3.87e-14 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 74.84 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 337 ICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-FAYVAQ---------QAWIL--NATLRDNILFG----KEFDEERYNS 400
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdVTNVPPhlrhinmvfQSYALfpHMTVEENVAFGlkmrKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 401 VLnscclrpdlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNS--AIRKRLk 477
Cdd:TIGR01187 81 VL---------EALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLElkTIQEQL- 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720387222 478 SKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:TIGR01187 151 GITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
317-487 |
4.36e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.01 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------------FAYVAQQAWILNA-T 382
Cdd:TIGR01189 10 RGERMLFeGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFGKEFDEERYNSVLNScclrpdlailpnsdLTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIEDA--------------LAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1720387222 457 SALDAHvGNHIFNSAIRKRL-KSKTVLFVTHQ 487
Cdd:TIGR01189 156 TALDKA-GVALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
325-503 |
5.77e-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: 72.31 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---------TFAYVAQQAWI-LNATLRDNILF----- 389
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVYlaqlk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 --GKEFDEERYNSVLNscclRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHI 467
Cdd:cd03269 99 glKKEEARRRIDEWLE----RLELSEYANKRVEE-------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVEL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720387222 468 FNSAIRK-RLKSKTVLFVTHQLQyLVD--CDEVIFMKEG 503
Cdd:cd03269 167 LKDVIRElARAGKTVILSTHQME-LVEelCDRVLLLNKG 204
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
947-1148 |
6.05e-14 |
|
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: 71.31 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 947 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--IRISDIGLAdLRSKLAIIPqepvl 1022
Cdd:cd03215 8 RGLsvKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDA-IRAGIAYVP----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1023 fsgtvrsnldpfnqytEDqiwdaleRTHMKeciaqlpLKLESEVMEN---GDNFSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:cd03215 82 ----------------ED-------RKREG-------LVLDLSVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1100 TAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQV 1148
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
952-1150 |
6.08e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGIRISDIGLADLRSKLAIIPQEP------ 1020
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1021 VLFS----GTVRSNLDPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL 1096
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEK-------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1097 DEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVE 1150
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
324-514 |
6.42e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 72.72 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAIlgqmTLLE----GSIAVSGTfaYVAQQAWILNAtLRDNIlfGKEFdeERYN 399
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCI----NLLEepdsGTITVDGE--DLTDSKKDINK-LRRKV--GMVF--QQFN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 400 -----SVLNSCCLRPdlaI----LPNSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:COG1126 88 lfphlTVLENVTLAP---IkvkkMSKAEAEERAMEllervGladkadaypAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 457 SALD----AHVGNHIfnsairKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:COG1126 165 SALDpelvGEVLDVM------RDLAKEgmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-520 |
6.86e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGtFAYVAQQAW----------------ILNAT 382
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:PRK13635 99 VQDDVAFGLE----------NIGVPREEMVERVDQALRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 457 SALDAhVGNHIFNSAIRkRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGD 520
Cdd:PRK13635 169 SMLDP-RGRREVLETVR-QLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
948-1174 |
1.07e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 72.97 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 948 NLPL----VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGiRISdigladlrsklaIIPQEPVLF 1023
Cdd:cd03291 44 NLCLvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RIS------------FSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 SGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1103
Cdd:cd03291 111 PGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1104 DTETDlliqetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1174
Cdd:cd03291 191 DVFTE-------KEIFESCVCKLMANK-------TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
955-1149 |
1.12e-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: 71.56 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 955 KVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISD----IGLADLRSKLAIIPQEPVLFSG-TVRS 1029
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NL--------DPFNQYTEDQIWDALERTHMKEciaQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1101
Cdd:cd03297 95 NLafglkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1102 AMDTETDLLIQETIREAFAD--CTMLTIAHRLHTV-LGSDRIMVLAQGQVV 1149
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
319-509 |
1.17e-13 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 71.09 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTF------------AYVAQQAWILNATLRDN 386
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILF---GKEFDEERYNSVLNSCCLRpdlailpnsdlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 463
Cdd:cd03268 93 LRLlarLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 464 GNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 509
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
324-514 |
1.57e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILFG- 390
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergVGMVFQSyALYPHLSVAENMSFGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 391 ------KEFDEERYNSVLnscclrpdlAILPNSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA--H 462
Cdd:PRK11000 101 klagakKEEINQRVNQVA---------EVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 463 VGNHIFNSAIRKRLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK11000 170 VQMRIEISRLHKRLGR-TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
953-1152 |
1.62e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGIRI--SDIGLADLRSKLAIIPQEPVLFSG 1025
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 TVRSNLD---PFNQYTEDQIWDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1103 MDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1152
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
952-1150 |
2.48e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.80 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLVEL----SGGCIKIDGIRISDI---GLADLRSKLAIIPQEPVLFS 1024
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLlerpTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1025 G-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVME---------NGDNF----SVGERQLLC 1082
Cdd:COG1135 96 SrTVAEN------------------------VA-LPLEIagvpkaeiRKRVAEllelvglsdKADAYpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1083 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETtrsilDLL--KDINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
952-1164 |
2.79e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.34 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVL-FSGTVR-- 1028
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 ---------SNLDPFNQYTEDQIWDALERTHMKECIAQlPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:PRK09536 98 vemgrtphrSRFDTWTETDRAAVERAMERTGVAQFADR-PV----------TSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1100 TAAMDTETDLLIQETIRE-------AFADCTMLTIAHRLhtvlgSDRIMVLAQGQVVEFDTPSVLLSNDSSR 1164
Cdd:PRK09536 167 TASLDINHQVRTLELVRRlvddgktAVAAIHDLDLAARY-----CDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
952-1147 |
3.52e-13 |
|
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: 70.16 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI-------KIDGIRISDIGLADLRSK--------LAII 1016
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1017 PQ--------EPVLFSGTVRsnldpfnQYTEDQIWDALERTHMKECIAQLPLKlesevmengdNFSVGERQLLCIARALL 1088
Cdd:COG4778 106 PRvsaldvvaEPLLERGVDR-------EEARARARELLARLNLPERLWDLPPA----------TFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1089 RHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1147
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
952-1151 |
3.76e-13 |
|
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: 69.91 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAdLRSKLAIIPQEPVLFSG-TVRSN 1030
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LDPFNqytedqiwdALERTHMKECIAQLPLKLESEVMENGDN-----FSVGERQLLCIARALLRHCKILILDEATAAMDT 1105
Cdd:cd03264 93 LDYIA---------WLKGIPSKEVKARVDEVLELVNLGDRAKkkigsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 1106 ETDLLIQETIREAFADCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF 1151
Cdd:cd03264 164 EERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
956-1160 |
4.00e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---IRISDIGLADLRSKLAIIPQEPvLFSGTVRSNL- 1031
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 ----DPFNQYTEDqiwdaLERTHMKECIAQLPLK---LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1104
Cdd:PRK15079 119 eiiaEPLRTYHPK-----LSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1105 TETDL----LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:PRK15079 194 VSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
936-1169 |
4.08e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 70.34 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGladlrsklai 1015
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVlfsGTVRSNLDPFNQYT-EDQIWDALERTHMKECI------AQLPL-KLESEVMENGDNFSVGERQLLCIARAL 1087
Cdd:cd03300 69 PHKRPV---NTVFQNYALFPHLTvFENIAFGLRLKKLPKAEikervaEALDLvQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1088 LRHCKILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEF 1151
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELK-------------RLQKELGitfvfvthdqeealtmSDRIAVMNKGKIQQI 212
|
250
....*....|....*...
gi 1720387222 1152 DTPSVLLSNDSSRFYAMF 1169
Cdd:cd03300 213 GTPEEIYEEPANRFVADF 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
928-1150 |
4.51e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 928 HDWPQEGEVTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG------- 998
Cdd:PRK10261 5 DELDARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 999 ---IRISDIGLADLR----SKLAIIPQEPVlfsgtvrSNLDPFNQYTEdQIWDALeRTHM----KECIAQLPLKL----- 1062
Cdd:PRK10261 85 rqvIELSEQSAAQMRhvrgADMAMIFQEPM-------TSLNPVFTVGE-QIAESI-RLHQgasrEEAMVEAKRMLdqvri 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1063 -ESEVM--ENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG- 1136
Cdd:PRK10261 156 pEAQTIlsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEi 235
|
250
....*....|....
gi 1720387222 1137 SDRIMVLAQGQVVE 1150
Cdd:PRK10261 236 ADRVLVMYQGEAVE 249
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
939-1164 |
4.97e-13 |
|
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: 69.88 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLaDLRSKLAII-- 1016
Cdd:cd03218 4 ENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1017 PQEPVLFSG-TVRSNLDPFNQYTEDQIWDALERThmKECIAQLplKLESEVMENGDNFSVGERQLLCIARALLRHCKILI 1095
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLSKKEREEKL--EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1096 LDEATAAMDTETDLLIQETIREaFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1164
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKI-LKDRGIgvLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
953-1169 |
5.17e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 70.75 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---IRISDIGLADLRSK--------LAIIPQEPV 1021
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELRELRRKkismvfqsFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1022 L----FSGTVRsNLDPfnQYTEDQIWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILD 1097
Cdd:cd03294 120 LenvaFGLEVQ-GVPR--AEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1098 EATAAMDTetdlLIQETIREAFADC------TMLTIAHRLHTV--LGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 1169
Cdd:cd03294 186 EAFSALDP----LIRREMQDELLRLqaelqkTIVFITHDLDEAlrLG-DRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
952-1150 |
6.09e-13 |
|
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: 72.79 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS----GGCIKIDGIRISDIGLADLR----SKLAIIPQEPVlf 1023
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 sgtvrSNLDPFnqYT-EDQIW-------------------DALERTHMKE---CIAQLPLKLesevmengdnfSVGERQL 1080
Cdd:COG4172 103 -----TSLNPL--HTiGKQIAevlrlhrglsgaaararalELLERVGIPDperRLDAYPHQL-----------SGGQRQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1081 LCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIREAfadctMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVqaqilDLLkdLQRELGMA-----LLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
936-1163 |
6.26e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.74 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDiGLADLRsklaI 1015
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDER----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEpvlfSGTVRSNLDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEV--MENGDNF----SVGERQL 1080
Cdd:PRK09493 75 IRQE----AGMVFQQFYLFPHLT------ALEnvmfgplrvRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1081 LCIARALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRL---HTVlGSdRIMVLAQGQVVEFDT 1153
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKvmQDLAEegMTMVIVTHEIgfaEKV-AS-RLIFIDKGRIAEDGD 219
|
250
....*....|
gi 1720387222 1154 PSVLLSNDSS 1163
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
952-1159 |
6.38e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL-----VELSGGCIKIDG---IRISDIGLADLR-SKLAIIPQEPVL 1022
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGeslLHASEQTLRGVRgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1023 fsgtvrsNLDPFNQyTEDQIWDALE----------RTHMKEC-----IAQLPLKLEsevmENGDNFSVGERQLLCIARAL 1087
Cdd:PRK15134 104 -------SLNPLHT-LEKQLYEVLSlhrgmrreaaRGEILNCldrvgIRQAAKRLT----DYPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1088 LRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-521 |
6.64e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMT----------LLEGSIAVSGTFA-----------YVAQQAWI 378
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLArdirksrantgYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 379 LNA-TLRDNILFGKEFDEERYNSvlnscCLR---PDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRS 448
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRT-----CFSwftREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 449 IYILDDPLSALDAHVGnHIFNSAIR--KRLKSKTVLFVTHQLQY-LVDCDEVIFMKEGCITERGTHEELMNLNGDY 521
Cdd:PRK09984 173 VILADEPIASLDPESA-RIVMDTLRdiNQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFDH 247
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
322-516 |
7.41e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.74 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAI--LGQMT---LLEGSIAVSGTFA----------YVAQQAWIL-NATLRD 385
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdLIVDGLKVNDPKVderlirqeagMVFQQFYLFpHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFG--------KEFDEERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:PRK09493 97 NVMFGplrvrgasKEEAEKQARELLAKVGLAERAHHYP-----------SELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 458 ALDAHVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 516
Cdd:PRK09493 166 ALDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
322-505 |
7.60e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSaILGQMtllegSIAVSGTFAYVAQQAWILN----ATLRDNiLFGKEFdeER 397
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL-----DKPTSGTYRVAGQDVATLDadalAQLRRE-HFGFIF--QR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 398 YNsvlnsccLRPDLAILPNSDLTEI----------------------GER----GANLSGGQRQRISLARALYSDRSIYI 451
Cdd:PRK10535 95 YH-------LLSHLTAAQNVEVPAVyaglerkqrllraqellqrlglEDRveyqPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 452 LDDPLSALDAHVGNHIFnsAIRKRLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 505
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
936-1150 |
9.64e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.99 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGIRI---SDIGL 1006
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLlerpTSGRVLVDGQDLtalSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1007 ADLRSKLAIIPQEPVLFSG-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVMENGD------ 1071
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSrTVFDN------------------------VA-LPLELagtpkaeiKARVTELLElvglsd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1072 -------NFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIreafaDCTMLTIAHRLHTVLG- 1136
Cdd:PRK11153 133 kadrypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRi 207
|
250
....*....|....
gi 1720387222 1137 SDRIMVLAQGQVVE 1150
Cdd:PRK11153 208 CDRVAVIDAGRLVE 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
947-1152 |
9.68e-13 |
|
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: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 947 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--IRISDIGLAdLRSKLAIIP----Q 1018
Cdd:COG1129 260 EGLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDA-IRAGIAYVPedrkG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 EPVLFSGTVRSN--LDPFNQYTEDQIWD-ALERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLRHCK 1092
Cdd:COG1129 339 EGLVLDLSIRENitLASLDRLSRGGLLDrRRERALAEEYIKRLRIKtpsPEQPVG----NLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1093 ILILDEATAAMD----TEtdllIQETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1152
Cdd:COG1129 415 VLILDEPTRGIDvgakAE----IYRLIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgELD 477
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
429-516 |
1.08e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQLQ---YLvdCDEVIFMKE 502
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 1720387222 503 GCITERGTHEELMN 516
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
322-516 |
1.09e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.61 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAY----------VAQQAWILNATLRDNILFgK 391
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 392 EFDEERYNSVLNSCCLRPDLAI-LPNSDLTE----------IGERG-----ANLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLgLSKQEAREravkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 456 LSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 516
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
324-516 |
1.15e-12 |
|
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: 69.34 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEG-SIAVSGT-------------FAYV--AQQAWIL-NATLRDN 386
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrIGLVspALQLRFPrDETVLDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 IL---FG-----KEFDEERYNSVLNScclrpdLAILpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:COG1119 101 VLsgfFDsiglyREPTDEQRERAREL------LELL---GLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 458 ALDAHvGNHIFNSAIRK--RLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 516
Cdd:COG1119 172 GLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
316-517 |
1.22e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 316 LRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYV----AQQAW 377
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVpedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ILNATLRDNILFGkefdeeRYNSVLNSCCLRP------------DLAILPNSDLTEIGergaNLSGGQRQRISLARALYS 445
Cdd:COG1129 342 VLDLSIRENITLA------SLDRLSRGGLLDRrreralaeeyikRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 446 DRSIYILDDPLSALDahVGNH--IFNsAIRKRLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEELMN 516
Cdd:COG1129 412 DPKVLILDEPTRGID--VGAKaeIYR-LIRELAAEgKAVIVISSELPELLGlSDRILVMREGRIVgeldrEEATEEAIMA 488
|
.
gi 1720387222 517 L 517
Cdd:COG1129 489 A 489
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
953-1155 |
1.23e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.88 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--IRISDIGLADLRSKLAIIPQEP--VLFSGTVR 1028
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLD--PFN-QYTEDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEATAAMD- 1104
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1105 ---TETDLLIQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVEFDTPS 1155
Cdd:PRK13636 175 mgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPK 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
322-509 |
1.29e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.33 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGtfayvaQQAWIL--------NATLRDNILFG--- 390
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLglgggfnpELTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 391 ----KEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 462
Cdd:cd03220 112 lglsRKEIDEKIDEII---------------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 463 vgnhiF----NSAIRKRLK-SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 509
Cdd:cd03220 177 -----FqekcQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
952-1164 |
1.43e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.75 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAD-LRSKLAIIPQEPVLFSG-TVRS 1029
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLDPFNQYTEDQIWdaleRTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDL 1109
Cdd:PRK11614 100 NLAMGGFFAERDQF----QERIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1110 LIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1164
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
325-509 |
1.46e-12 |
|
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: 68.16 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAY-----VAQQAWILNA--------TLRDNILF-- 389
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaeARRRLGFVSDstglydrlTARENLEYfa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 ------GKEFdEERYNSVlnscclrpdlailpnSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:cd03266 104 glyglkGDEL-TARLEEL---------------ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 460 DAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 509
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-512 |
1.96e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.86 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 329 IEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGtfAYVAQQAWILNA---------------TLRDNIL-FGKE 392
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARArigvvpqfdnldlefTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 393 FdeeRYNSvlnscclRPDLAILPNsdLTEIGE-------RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 465
Cdd:PRK13536 142 F---GMST-------REIEAVIPS--LLEFARleskadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-AR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720387222 466 HIFNSAIRKRL-KSKTVLFVTHQLQYLVD-CDEVIFMKEGC-ITERGTHE 512
Cdd:PRK13536 209 HLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHA 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-487 |
2.00e-12 |
|
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: 66.41 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI---AVSGTFaYVAQQAWILNATLRDNIlfgkefdeeryns 400
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmpEGEDLL-FLPQRPYLPLGTLREQL------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 401 vlnscclrpdlaILPNSDlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLksKT 480
Cdd:cd03223 85 ------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY-QLLKELG--IT 140
|
....*..
gi 1720387222 481 VLFVTHQ 487
Cdd:cd03223 141 VISVGHR 147
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
315-516 |
2.15e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 68.60 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 315 SLRL-QRT-LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG------------------------T 368
Cdd:COG4559 8 SVRLgGRTlLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrravlpqhsslA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 369 FAYVAQQ-------AWILNATLRDNILfgkefdEErynsvlnscCL-RPDLAILPNSDLTEigerganLSGGQRQRISLA 440
Cdd:COG4559 88 FPFTVEEvvalgraPHGSSAAQDRQIV------RE---------ALaLVGLAHLAGRSYQT-------LSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 441 RAL-------YSDRSIYILDDPLSALD-AHVgNHIFNSAirKRLKSK--TVLFVTHQL----QYlvdCDEVIFMKEGCIT 506
Cdd:COG4559 146 RVLaqlwepvDGGPRWLFLDEPTSALDlAHQ-HAVLRLA--RQLARRggGVVAVLHDLnlaaQY---ADRILLLHQGRLV 219
|
250
....*....|
gi 1720387222 507 ERGTHEELMN 516
Cdd:COG4559 220 AQGTPEEVLT 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
322-514 |
2.18e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILG-QMTLLE--GSIAVSGT----------FAYVAQQAWILNA-TLRDNI 387
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKgsGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFGKEF--------DE--ERYNSVLNscclrpDLAILPNSDlTEIGERGA--NLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:TIGR00955 121 MFQAHLrmprrvtkKEkrERVDEVLQ------ALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 456 LSALDAHVGNHIFnsAIRKRL--KSKTVLFVTHQLQYLVDC--DEVIFMKEGCITERGTHEEL 514
Cdd:TIGR00955 194 TSGLDSFMAYSVV--QVLKGLaqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
322-498 |
2.20e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 388
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 F-----GKEFDEERynsvlnsccLRPDLAI--LPNSDLTEigeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:PRK10247 103 FpwqirNQQPDPAI---------FLDDLERfaLPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720387222 462 HvGNHIFNSAIRKRLKSK--TVLFVTHQLQYLVDCDEVI 498
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
952-1160 |
2.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID------GIRISDIGLADLRSKLAIIPQEPVLFSG 1025
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 -TVRSNLD-PFNQYTedqIWDALE-RTHMKECIAQLPL--KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1100
Cdd:PRK14246 105 lSIYDNIAyPLKSHG---IKEKREiKKIVEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1101 AAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
952-1158 |
2.57e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRI-SDIGLAdlRSKLAIIPQEPVL-FSGTVRS 1029
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLDPFNQYTedqiwdaleRTHMKECIAQLPLKLESEVMENGDNFSV-----GERQLLCIARALLRHCKILILDEATAAMD 1104
Cdd:PRK13536 134 NLLVFGRYF---------GMSTREIEAVIPSLLEFARLESKADARVsdlsgGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1105 TETDLLIQETIREAFA--DCTMLTI-----AHRLhtvlgSDRIMVLAQGQVVEFDTPSVLL 1158
Cdd:PRK13536 205 PHARHLIWERLRSLLArgKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
317-487 |
3.38e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSgtfayVAQQAWILNATLRDNILFGKEFDE 395
Cdd:COG2401 40 VVERYVLrDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 396 ERYnsVLNSCCLrpdlailpnSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAI 472
Cdd:COG2401 115 AVE--LLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLA 183
|
170
....*....|....*
gi 1720387222 473 RKRlkSKTVLFVTHQ 487
Cdd:COG2401 184 RRA--GITLVVATHH 196
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
956-1174 |
3.39e-12 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 69.36 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGiRI-----SDIGLADLRSKLAIIPQEPVLFSG-TVRS 1029
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVlqdsaRGIFLPPHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLdpfnQYTEDQIWDALERTHMKECIAQL---PLkLESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTE 1106
Cdd:COG4148 97 NL----LYGRKRAPRAERRISFDEVVELLgigHL-LDRRP----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1107 T-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1174
Cdd:COG4148 168 RkaeilPYL--ERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGS 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
951-1160 |
3.62e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.88 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 951 LVLKKVSFTIkPKEKI-GIVGRTGSGKSSLGMALFRLVELSGGCiKIDG--------IRISDIGLADLRSKLAIIPQEPV 1021
Cdd:PRK14243 24 LAVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGkvtfhgknLYAPDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1022 LFSGTVRSNLD---PFNQYTEDQiwDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1098
Cdd:PRK14243 102 PFPKSIYDNIAygaRINGYKGDM--DELVERSLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1099 ATAAMDTETDLLIQETIREAFADCTMLTIAHRLH---------------TVLGSDRimvlaQGQVVEFDTPSVLLSN 1160
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQqaarvsdmtaffnveLTEGGGR-----YGYLVEFDRTEKIFNS 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
953-1147 |
3.64e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDGIRISDIGLADL-RSKLAIIPQEPVLF 1023
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKV-----LSGvyphgtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 SG-TVRSNLDPFNQYTEDQI--WDALERtHMKECIAQLPLKL--ESEVMENGdnfsVGERQLLCIARALLRHCKILILDE 1098
Cdd:PRK13549 95 KElSVLENIFLGNEITPGGImdYDAMYL-RAQKLLAQLKLDInpATPVGNLG----LGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1099 ATAAM-DTETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1147
Cdd:PRK13549 170 PTASLtESETAVLL-DIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
936-1160 |
3.86e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.32 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRI----SDIGLAD 1008
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1009 LRSKLAIIPQ--EPVLFSGTVRSNLD--PFN-QYTEDQiwdalERTHMKECIAQLPLkleSEVMENGDNF--SVGERQLL 1081
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfGFSEDE-----AKEKALKWLKKVGL---SEDLISKSPFelSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1082 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1155
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPK 230
|
....*
gi 1720387222 1156 VLLSN 1160
Cdd:PRK13641 231 EIFSD 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
936-1107 |
4.86e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 66.66 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDI---GLADLRSK 1012
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1013 LAIIPQEPVLFSG-TVRSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMENGdnFSVGERQLLCIARALLRHC 1091
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKR--VPAALELVGLSHKHRALPAE--LSGGEQQRVAIARAIVNSP 155
|
170
....*....|....*.
gi 1720387222 1092 KILILDEATAAMDTET 1107
Cdd:cd03292 156 TILIADEPTGNLDPDT 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
324-516 |
5.11e-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: 67.08 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG------------------TFayvaQQAWIL-NATLR 384
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrTF----QIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGKEFDEERYNSVLNSCCLRPDL-----AILpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 456 LSALD----AHVGNHIfnSAIRKRlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03219 171 AAGLNpeetEELAELI--RELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
952-1160 |
5.22e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDG--------IRISDIGLADLRSKLAIIPQEPVLF 1023
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESE-VRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 SGTVRSNLdpfnQYTEDQI-W------DALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL 1096
Cdd:PRK14258 101 PMSVYDNV----AYGVKIVgWrpkleiDDIVESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1097 DEATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVL-----------GSDRImvlaqGQVVEFDTPSVLLSN 1160
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----GQLVEFGLTKKIFNS 246
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
951-1136 |
6.16e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 951 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGiriSDIGLADLRSKLAII----PQEPVLfsgT 1026
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLghrnAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1027 VRSNLD---PFNQYTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAM 1103
Cdd:PRK13539 90 VAENLEfwaAFLGGEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|...
gi 1720387222 1104 DTETDLLIQETIREAFADCTMLTIAhrLHTVLG 1136
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAA--THIPLG 189
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
927-1148 |
6.40e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 927 PHDwpqEGEVTFE-------NAEMRYREnlplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE-LSGGCIKIDG 998
Cdd:PRK13549 252 PHT---IGEVILEvrnltawDPVNPHIK----RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 999 --IRIS------DIGLADL---RSKLAIIPQEPVLFSGTVrSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVM 1067
Cdd:PRK13549 325 kpVKIRnpqqaiAQGIAMVpedRKRDGIVPVMGVGKNITL-AALDRFTGGS--RIDDAAELKTILESIQRLKVKTASPEL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1068 ENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDT----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMV 1142
Cdd:PRK13549 402 AIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLV 477
|
....*.
gi 1720387222 1143 LAQGQV 1148
Cdd:PRK13549 478 MHEGKL 483
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
322-516 |
6.52e-12 |
|
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: 66.54 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQQAWIL-NATLRDN 386
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFpSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFG------KEFDEERYNSVLNsccLRPDLAilpnsdlteigER----GANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:COG0410 99 LLLGayarrdRAEVRADLERVYE---LFPRLK-----------ERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 457 SALDAHVGNHIFNsAIRkRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:COG0410 165 LGLAPLIVEEIFE-IIR-RLNREgvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
320-516 |
7.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.38 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------------TFAYVAQQawILN 380
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglVFQYPEYQ--LFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 381 ATLRDNILFGK----EFDEERYNSVLNSCclrpDLAILPNSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:PRK13637 99 ETIEKDIAFGPinlgLSEEEIENRVKRAM----NIVGLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 457 SALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK13637 173 AGLDPKGRDEILNkiKELHKEYNM-TIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
322-516 |
8.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.13 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTS---LVSAILGQMTLLEGSIAVSGTfAYVAQQAW----------------ILNAT 382
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI-TLTAKTVWdirekvgivfqnpdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:PRK13640 102 VGDDVAFGLE----------NRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 457 SALDAHVGNHIFnSAIRKRLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK13640 172 SMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
319-514 |
9.03e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.35 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLV---SAIL----GQMTLLEGSIA--------------VSGTFAYVAQQaw 377
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlNGLLqptsGTVTIGERVITagkknkklkplrkkVGIVFQFPEHQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ILNATLRDNILFG-------KEFDEERYNSVLNSCCLRPDLaiLPNSDLteigergaNLSGGQRQRISLARALYSDRSIY 450
Cdd:PRK13634 98 LFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEEL--LARSPF--------ELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 451 ILDDPLSALDAHVGNHIFN--SAIRKRlKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEmfYKLHKE-KGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREI 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
936-1149 |
1.09e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLG--MALFRLVElsGGCIKIDGIRISDIGLAdlRSKL 1013
Cdd:PRK10771 2 LKLTDITWLY-HHLPM---RFDLTVERGERVAILGPSGAGKSTLLnlIAGFLTPA--SGSLTLNGQDHTTTPPS--RRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1014 AIIPQEPVLFSG-TVRSN----LDP---FNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIAR 1085
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1086 ALLRHCKILILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
952-1167 |
1.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElsggciKIDGIRIS-DIGLA-----------DLRSKLAIIPQE 1019
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMND------KVSGYRYSgDVLLGgrsifnyrdvlEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1020 PVLFSGTVRSN---------LDPFNQY--------TEDQIWDALerthmKECIAQLPLKLesevmengdnfSVGERQLLC 1082
Cdd:PRK14271 110 PNPFPMSIMDNvlagvrahkLVPRKEFrgvaqarlTEVGLWDAV-----KDRLSDSPFRL-----------SGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1083 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN- 1160
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSp 253
|
250
....*....|
gi 1720387222 1161 ---DSSRFYA 1167
Cdd:PRK14271 254 khaETARYVA 263
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
319-505 |
1.33e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRT-LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILG-----QMTLLEGSIAVsgtfayvaqqawilnATLRDNILFgkE 392
Cdd:PRK11247 24 ERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsAGELLAGTAPL---------------AEAREDTRL--M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 393 FDEER---YNSVLNSCCL------RPD-LAILPNSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:PRK11247 87 FQDARllpWKKVIDNVGLglkgqwRDAaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720387222 462 HvgNHIFNSAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCI 505
Cdd:PRK11247 167 L--TRIEMQDLIESLWQQhgfTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-514 |
1.34e-11 |
|
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: 65.60 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG----TFAYVAQQA-----------WILnaTLRDNIL 388
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQSlgycpqfdalfDEL--TVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 F-----GKEFDEERYNSvlnscclrpdLAILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 462
Cdd:cd03263 98 FyarlkGLPKSEIKEEV----------ELLLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 463 VGNHIFNsAIRKRLKSKTVLFVTHQLQ---YLvdCDEVIFMKEG---CIterGTHEEL 514
Cdd:cd03263 168 SRRAIWD-LILEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGklrCI---GSPQEL 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
314-513 |
1.40e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.59 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 314 GSLRLQrtlynIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------------FAYVAQQA 376
Cdd:PRK11144 11 GDLCLT-----VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 377 WIL-NATLRDNILFG-KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDD 454
Cdd:PRK11144 86 RLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 455 PLSALDAHvgnhifnsaiRKR-----LK--SKTV----LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 513
Cdd:PRK11144 155 PLASLDLP----------RKRellpyLErlAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-488 |
1.41e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAiLGQMTLLEGSIAVSGTFAYVAQQAWI----LNATLRD-NILFGKE- 392
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYErrvnLNRLRRQvSMVHPKPn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 393 -FDEERYNSVLNSCCL---RPDLAI-------LPNSDL-----TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:PRK14258 99 lFPMSVYDNVAYGVKIvgwRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190
....*....|....*....|....*....|...
gi 1720387222 457 SALDAHVGNHIFNSAIRKRLKSK-TVLFVTHQL 488
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
324-514 |
1.47e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 67.00 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGqmtLLEGSIAVSGT-----------------------FAYVAQQA---- 376
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILG---LLPPPGITSGEilfdgedllklsekelrkirgreIQMIFQDPmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 377 -------WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAIL---PNsdlteigergaNLSGGQRQRISLARALYSD 446
Cdd:COG0444 100 npvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 447 RSIYILDDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEEL 514
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQILNllKDLQRELGL-AILFITHDLgvvAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
939-1157 |
1.48e-11 |
|
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: 65.47 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDiGLADLRSKLAIIPQ 1018
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 EPVLFSG-TVRSNLdpfnqYTEDQIWdALERTHMKECIAQLpLKLeSEVMENGD----NFSVGERQLLCIARALLRHCKI 1093
Cdd:cd03265 81 DLSVDDElTGWENL-----YIHARLY-GVPGAERRERIDEL-LDF-VGLLEAADrlvkTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1094 LILDEATAAMDTETDLLIQETIR---EAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1157
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
938-1152 |
1.63e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 938 FENAEMRYreNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLV----ELSGGCIKID-GIRIsdigladlrsk 1012
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRI----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1013 lAIIPQEPVLFSG-TVRSN-LDPFNQYteDQIWDALERTHMKECIAQLPLKLESEVME-----NG--------------- 1070
Cdd:COG0488 64 -GYLPQEPPLDDDlTVLDTvLDGDAEL--RALEAELEELEAKLAEPDEDLERLAELQEefealGGweaearaeeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1071 ----------DNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLLIQEtireafaDCTMLTIAH-R--LH 1132
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY-------PGTVLVVSHdRyfLD 213
|
250 260
....*....|....*....|
gi 1720387222 1133 TVlgSDRIMVLAQGQVVEFD 1152
Cdd:COG0488 214 RV--ATRILELDRGKLTLYP 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
319-516 |
1.64e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.87 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------FAYVAQQAWIL---NA-----TLR 384
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAKRLAILrqeNHinsrlTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGkefdeeRYnsvlnscclrP---------DLAILPNS----DLTEIGERGAN-LSGGQRQRISLARALYSDRSIY 450
Cdd:COG4604 94 ELVAFG------RF----------PyskgrltaeDREIIDEAiaylDLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 451 ILDDPLSALDahvgnhIFNS-AIRKRLKS------KTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 516
Cdd:COG4604 158 LLDEPLNNLD------MKHSvQMMKLLRRladelgKTVVIVLHDInfasCY---ADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
910-1150 |
1.71e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 910 IKTLSLEAP-ARIKNKAPPHDWPQegeVTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 988
Cdd:PRK10522 299 LNKLALAPYkAEFPRPQAFPDWQT---LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 989 LSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTvrsnLDPFNQYTEDQIWDA-LERTHMKEciaqlplKLEsevM 1067
Cdd:PRK10522 375 PQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAH-------KLE---L 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1068 ENGD----NFSVGERQLLCIARALLRHCKILILDEATAAMDTE------TDLL--IQETIREAFAdctmltIAHRLHTVL 1135
Cdd:PRK10522 441 EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLplLQEMGKTIFA------ISHDDHYFI 514
|
250
....*....|....*
gi 1720387222 1136 GSDRIMVLAQGQVVE 1150
Cdd:PRK10522 515 HADRLLEMRNGQLSE 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
317-509 |
1.85e-11 |
|
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: 65.43 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG----------------TFAYVAQQAWILN 380
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkflrrigvVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 381 AtlRDNILFGKE---FDEERYNSVLNSCClrpdlailpnsDLTEIGE------RgaNLSGGQRQRISLARALYSDRSIYI 451
Cdd:cd03267 112 V--IDSFYLLAAiydLPPARFKKRLDELS-----------ELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 452 LDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHqlqYLVD----CDEVIFMKEGCITERG 509
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEyNRERGTTVLLTSH---YMKDiealARRVLVIDKGRLLYDG 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
324-514 |
1.86e-11 |
|
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: 65.08 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG------------TFAYVAQQAWILNA-TLRDNI--- 387
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyih 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 --LFGKEFDE--ERYNSVLNSCclrpdlailpnsDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 462
Cdd:cd03265 98 arLYGVPGAErrERIDELLDFV------------GLLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 463 VGNHIFnSAIRKRLKSK--TVLFVTHqlqYLVD----CDEVIFMKEGCITERGTHEEL 514
Cdd:cd03265 166 TRAHVW-EYIEKLKEEFgmTILLTTH---YMEEaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
320-486 |
2.01e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLY-NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG--TFAYVAQQAWIL-NATLRDNILFG-KEFD 394
Cdd:COG0488 11 RPLLdDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTVLDGdAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 395 E--ERYNSVLNSCCLRPDLAILPNSDLTEIGERGA--------------------------NLSGGQRQRISLARALYSD 446
Cdd:COG0488 91 AleAELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720387222 447 RSIYILDDPLSALDAHvgnhifnsAIR---KRLKS--KTVLFVTH 486
Cdd:COG0488 171 PDLLLLDEPTNHLDLE--------SIEwleEFLKNypGTVLVVSH 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
313-509 |
2.09e-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: 64.52 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 313 TGSLRLQRTLYNIDLEIEEGkLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG------------TFAYVAQQ-AWIL 379
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 380 NATLRDNIlfgkefdeeRYNSVLNSC----CLRPDLAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDD 454
Cdd:cd03264 86 NFTVREFL---------DYIAWLKGIpskeVKARVDEVLELVNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 455 PLSALDahVGNHI-FNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 509
Cdd:cd03264 157 PTAGLD--PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
322-501 |
2.26e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------FAYVAQQA---WILNATLRDNIL 388
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FG-----------KEFDEERYNSVLNscclRPDLAILPNSdltEIGErganLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:PRK15056 103 MGryghmgwlrraKKRDRQIVTAALA----RVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720387222 458 ALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMK 501
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
956-1159 |
2.27e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGG--CIKI--DGIRISDIGLaDLRSK----LAIIPQEPVLFsgTV 1027
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY--PH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 RSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMEN-----GDNFSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1103 MDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
952-1152 |
2.41e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 64.86 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAdlrskLAIIPQ----EPVLFSGTV 1027
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG-----GGFNPEltgrENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 RSNLDPFNQYTEDQIWDALErthMKECIaQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1107
Cdd:cd03220 112 LGLSRKEIDEKIDEIIEFSE---LGDFI-DLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 1108 DLLIQETIREAFADCTMLTIA-HRLHTVLG-SDRIMVLAQGQVVEFD 1152
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
320-516 |
2.47e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGqMTLLEGSIAVSGTFAYVAQ---------------------QAWI 378
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG-LIISETGQTIVGDYAIPANlkkikevkrlrkeiglvfqfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 379 LNATLRDNILFGK----EFDEERYNSVLNSCclrpDLAILPNsdltEIGERGA-NLSGGQRQRISLARALYSDRSIYILD 453
Cdd:PRK13645 104 FQETIEKDIAFGPvnlgENKQEAYKKVPELL----KLVQLPE----DYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 454 DPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
322-524 |
3.04e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTfAYVAQQAWILN----------------ATLRD 385
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWNLRrkigmvfqnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGKEFDEERYNSVLNscclRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 465
Cdd:PRK13642 102 DVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 466 HIFNsaIRKRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATI 524
Cdd:PRK13642 178 EIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-516 |
3.05e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.52 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILG--QMTLLEGSI------------------------AVSGTFAYVA 373
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgepcpVCGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 374 QQAWILNATLRDN------ILFGKEF----DEERYNSVLNS---CCLRPDLAILPNSDLTE---IGER----GANLSGGQ 433
Cdd:TIGR03269 94 VDFWNLSDKLRRRirkriaIMLQRTFalygDDTVLDNVLEAleeIGYEGKEAVGRAVDLIEmvqLSHRithiARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 434 RQRISLARALYSDRSIYILDDPLSALDAHVGNhIFNSAIRKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 510
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
|
....*.
gi 1720387222 511 HEELMN 516
Cdd:TIGR03269 253 PDEVVA 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
956-1148 |
3.07e-11 |
|
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: 67.16 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-GGCIKIDGIRISDIGLAD-LRSKLAIIPQE-------PVLFSG- 1025
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQaIRAGIAMVPEDrkrhgivPILGVGk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 -TVRSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMD 1104
Cdd:TIGR02633 359 nITLSVLKSFCFKM--RIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 1105 T----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 1148
Cdd:TIGR02633 436 VgakyEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
327-525 |
3.20e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 327 LEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTfayvaQQAWILNATLRdnilfgkEFDEERYNSVLNSCC 406
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKISDAELR-------EVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 407 LRPDLAILPNSD--------------------LTEIG-ERGAN-----LSGGQRQRISLARALYSDRSIYILDDPLSALD 460
Cdd:PRK10070 117 LMPHMTVLDNTAfgmelaginaeerrekaldaLRQVGlENYAHsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 461 AHVGNHIFNSAIRKRLK-SKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELM-NLNGDYATIF 525
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILnNPANDYVRTF 264
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
952-1166 |
3.32e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGL-ADLRSKLAIIPQEPVLFSG-TVRS 1029
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLDPFNQYTEDqiwdaLERTHMKECIAQLPLKLESEVMEN--GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1107
Cdd:PRK10895 98 NLMAVLQIRDD-----LSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1108 DLLIQETIrEAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDS-SRFY 1166
Cdd:PRK10895 173 VIDIKRII-EHLRDSGLgvLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHvKRVY 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
310-486 |
3.51e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.04 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 310 QIHTGSLRLqrtLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQmtlLEGSIAVSGtfayvaqQAWI-------LNAT 382
Cdd:COG4136 8 TITLGGRPL---LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASG-------EVLLngrrltaLPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LR------------------DNILFG---KEFDEERYNSVLNScclrpdlaiLPNSDLTEIGERG-ANLSGGQRQRISLA 440
Cdd:COG4136 75 QRrigilfqddllfphlsvgENLAFAlppTIGRAQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720387222 441 RALYSDRSIYILDDPLSALDAH----VGNHIFNSAIRKRLkskTVLFVTH 486
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAAlraqFREFVFEQIRQRGI---PALLVTH 192
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
308-507 |
3.63e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 64.38 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 308 GKQIHTGSLRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--FAyvaqqawiLN----A 381
Cdd:COG4181 15 TKTVGTGAGELT-ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFA--------LDedarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLR-DNILFgkefdeerynsVLNSCCLRPDLAILPN----------SDLTEI----------GERG----ANLSGGQRQR 436
Cdd:COG4181 86 RLRaRHVGF-----------VFQSFQLLPTLTALENvmlplelagrRDARARarallervglGHRLdhypAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 437 ISLARALYSDRSIYILDDPLSALDAHVGNHI----FnsAIRKRLKSkTVLFVTHQLQYLVDCDEVIFMKEGCITE 507
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIidllF--ELNRERGT-TLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
939-1161 |
4.55e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.76 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQ 1018
Cdd:PRK13647 8 EDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1019 EP--VLFSGTVRSNL--DPFNQ-----YTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLR 1089
Cdd:PRK13647 87 DPddQVFSSTVWDDVafGPVNMgldkdEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1090 HCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1161
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRG----QETLMEILDRLhnqgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-516 |
4.78e-11 |
|
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: 64.10 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTF--------------AYVAQQAWIL-NATLRDNIL 388
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgiGYLPQEASIFrKLTVEENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 -------FGKEFDEERYNSVLNscclrpDLAILPNSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:cd03218 98 avleirgLSKKEREEKLEELLE------EFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 462 HVGNHIfnSAIRKRLKSKT--VLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:cd03218 167 IAVQDI--QKIIKILKDRGigVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-514 |
4.79e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.13 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFayvaqqawiLNATLRDNI--LfgkefDEERynsv 401
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---------LDPEDRRRIgyL-----PEER---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 402 lnscCLRPDLAI------------LPNSDLT----------EIGERGA----NLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:COG4152 81 ----GLYPKMKVgeqlvylarlkgLSKAEAKrradewlerlGLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 456 LSALDAhVGNHIFNSAIR-KRLKSKTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEEL 514
Cdd:COG4152 157 FSGLDP-VNVELLKDVIReLAAKGTTVIFSSHQME-LVEelCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
953-1159 |
4.97e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISdIGLADLRS-KLAIIPQEPV---------- 1021
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1022 -LFSGTVRSNLDPFNQYTEDQIWDALERTHM-KECIAQLPLKLESevmengdnfsvGERQLLCIARALLRHCKILILDEA 1099
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1100 TAAMDTETD-------LLIQETIREAFADCTMlTIAHRLHTvlgSDRIMVLAQGQVVEF-DTPSVLLS 1159
Cdd:PRK15112 177 LASLDMSMRsqlinlmLELQEKQGISYIYVTQ-HLGMMKHI---SDQVLVMHQGEVVERgSTADVLAS 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
306-510 |
5.28e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 306 EEGKqIHTGSLRlqrtlyNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTfaYVAQQAWILNATLRD 385
Cdd:PRK11629 16 QEGS-VQTDVLH------NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NIL-FGKEFDEerynsvlnsccLRPDLAILPN--------------------SDLTEIG------ERGANLSGGQRQRIS 438
Cdd:PRK11629 87 QKLgFIYQFHH-----------LLPDFTALENvamplligkkkpaeinsralEMLAAVGlehranHRPSELSGGERQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 439 LARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 510
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
322-493 |
6.05e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.53 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----------------FAYVAQQAWIL-NATLR 384
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRLLpDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILF-----GKEFDE--ERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 453
Cdd:COG2884 98 ENVALplrvtGKSRKEirRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720387222 454 DPLSALDAHVGNHIFN--SAIRKRlkSKTVLFVTHQLQyLVD 493
Cdd:COG2884 163 EPTGNLDPETSWEIMEllEEINRR--GTTVLIATHDLE-LVD 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
322-486 |
6.65e-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: 63.20 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT---------FAYVAQQ--------AWILNATLR 384
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGKEFDE-------ERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 1720387222 458 ALDAHVGNHIFNSAIRKRLKSKTVLFVTH 486
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
322-510 |
6.98e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.21 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAIlgqmTLLE----GSIAVSGT----------------FAYVAQQAWILNA 381
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGQdltalsekelrkarrqIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 -TLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 449
Cdd:PRK11153 97 rTVFDNVALplelagtPKAEIKARVTELL---------------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 450 YILDDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGT 510
Cdd:PRK11153 162 LLCDEATSALDPATTRSILEllKDINRELGL-TIVLITHEMD-VVKriCDRVAVIDAGRLVEQGT 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
955-1153 |
7.43e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 955 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGIRISDI---GLADLRS-KLAIIPQEPVlfsgtv 1027
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLpekELNKLRAeQISMIFQDPM------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 rSNLDPFNQYTEdQIWDAL-------------ERTHMKECIaQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKIL 1094
Cdd:PRK09473 108 -TSLNPYMRVGE-QLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARKRMKMYPHE-FSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1095 ILDEATAAMDTETD----LLIQETIREaFaDCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEFDT 1153
Cdd:PRK09473 184 IADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
952-1155 |
7.49e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE----LSGGCI--------------------------------K 995
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDqyepTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 996 IDGIRISDIGLADLRSKLAIIPQEPVLFSG--TVRSN-LDPFNQ--YT-EDQIWDALERTHMkeciaqlpLKLESEVMEN 1069
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvLEALEEigYEgKEAVGRAVDLIEM--------VQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1070 GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVLG-SDRIMVLAQG 1146
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
....*....
gi 1720387222 1147 QVVEFDTPS 1155
Cdd:TIGR03269 246 EIKEEGTPD 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
310-515 |
8.20e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 310 QIHTGSLRL----QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-------------FAYV 372
Cdd:PRK11231 2 TLRTENLTVgygtKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 373 AQQAWILNA-TLRDNILFGK-----------EFDEERYNSVLNscclRPDLAILPNSDLTEigerganLSGGQRQRISLA 440
Cdd:PRK11231 82 PQHHLTPEGiTVRELVAYGRspwlslwgrlsAEDNARVNQAME----QTRINHLADRRLTD-------LSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 441 RALYSDRSIYILDDPLSALDAhvgNHIFN--SAIRK-RLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELM 515
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDI---NHQVElmRLMRElNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
317-487 |
8.59e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------------FAYVAQQAWI---LN 380
Cdd:PRK13538 11 RDERILFsGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrdeyhqdLLYLGHQPGIkteLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 381 AtlrdnilfgkefdEE--RYNSVLnSCCLRPDLAIlpnSDLTEIGERG------ANLSGGQRQRISLARALYSDRSIYIL 452
Cdd:PRK13538 91 A-------------LEnlRFYQRL-HGPGDDEALW---EALAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720387222 453 DDPLSALD--------AHVGNHIFNSAIrkrlksktVLFVTHQ 487
Cdd:PRK13538 154 DEPFTAIDkqgvarleALLAQHAEQGGM--------VILTTHQ 188
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
952-1159 |
8.91e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSG-TVRSN 1030
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 L----DPFNQY-----TEDQ--IWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:PRK11231 97 VaygrSPWLSLwgrlsAEDNarVNQAMEQTRINH-LADRRL----------TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 1100 TAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
959-1142 |
1.07e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.20 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 959 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGiriSDIGLAdlRSKLAIIPQE-PVLFSGTVRSNLdpfnqy 1037
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTF-------IKMLAGVLKPDE---GDIEIE--LDTVSYKPQYiKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1038 tEDQIWDALERTHMKECIAQlPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE 1117
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*....
gi 1720387222 1118 aFA---DCTMLTIAHRLHTV-LGSDRIMV 1142
Cdd:cd03237 161 -FAennEKTAFVVEHDIIMIdYLADRLIV 188
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
956-1150 |
1.08e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.60 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRI---SDIGLADLRSKLAIIPQEPVlfsgtvrSNLD 1032
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY-------GSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1033 PfNQYTEDQIWDALE----------RTHMKECIAQLPLKLESEV----MengdnFSVGERQLLCIARALLRHCKILILDE 1098
Cdd:PRK11308 107 P-RKKVGQILEEPLLintslsaaerREKALAMMAKVGLRPEHYDryphM-----FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1099 ATAAMDTEtdllIQETIREAFAD------CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:PRK11308 181 PVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
952-1150 |
1.11e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGIRISDIgLADLRSKLAII--PQEPVLFSGtv 1027
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEERARLGIFlaFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 rsnldpfnqytedqiwdalerthmkeciaqlpLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1107
Cdd:cd03217 92 --------------------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720387222 1108 DLLIQETIRE-AFADCTMLTIAH--RLHTVLGSDRIMVLAQGQVVE 1150
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
936-1149 |
1.13e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 62.68 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISdiglADLRSKLAI 1015
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSG-TVRSNLDPFNQ-------YTEDQIWDALERTHMKEciaqlplKLESEVMEngdnFSVGERQLLCIARAL 1087
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYLAQlkglkkeEARRRIDEWLERLELSE-------YANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1088 LRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
658-823 |
1.26e-10 |
|
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: 63.96 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 658 ASIYALSMAVMLILkairGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqAEMFI 737
Cdd:cd18547 52 LGLYLLSALFSYLQ----NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-------SQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 738 QNVILVFFCVGMIAGVF-------PWF-LVAVGPLLILFsllhIVSRVLIRELKRLdNITQSPFLSHITSSIQ----GLA 805
Cdd:cd18547 121 QSLTQLISSILTIVGTLimmlyisPLLtLIVLVTVPLSL----LVTKFIAKRSQKY-FRKQQKALGELNGYIEemisGQK 195
|
170
....*....|....*...
gi 1720387222 806 TIHAYNKRQEFLHRYQEL 823
Cdd:cd18547 196 VVKAFNREEEAIEEFDEI 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
952-1169 |
1.29e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID-GIRISDIgladlRSKLAIIPQEPVLFSGTVRsn 1030
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYV-----PQKLYLDTTLPLTVNRFLR-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LDPFNQytEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDL- 1109
Cdd:PRK09544 92 LRPGTK--KEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVa 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1110 ---LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQgQVVEFDTPSVLLSNdsSRFYAMF 1169
Cdd:PRK09544 159 lydLIDQLRRE--LDCAVLMVSHDLHLVMAkTDEVLCLNH-HICCSGTPEVVSLH--PEFISMF 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
328-487 |
1.31e-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: 65.54 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 328 EIEEGKLVGICGSVGSGKTSLVSaILGQMTLLEG---SIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNS 404
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 405 cclrpDL-AILPNSDLTEIGERGAN----------LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR 473
Cdd:TIGR00954 553 -----DLeQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE 627
|
170
....*....|....
gi 1720387222 474 KRLkskTVLFVTHQ 487
Cdd:TIGR00954 628 FGI---TLFSVSHR 638
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
952-1160 |
1.34e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.56 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--IRISDIGLADLRSKLAIIPQEP--VLFSGTV 1027
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 RSNL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEAT 1100
Cdd:PRK13639 97 EEDVafGPLNlglskEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1101 AAMD----TETDLLIQETIREAfadctmLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:PRK13639 166 SGLDpmgaSQIMKLLYDLNKEG------ITIIISTHDVdlvpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-512 |
1.39e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.72 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLvsaiLGQMTLLEgsIAVSGTFAyVAQQAWILNAT--------LRDNIlfGKEF 393
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSL----LRVLNLLE--MPRSGTLN-IAGNHFDFSKTpsdkaireLRRNV--GMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 394 deERYN-----SVLNSCCLRP--------------DLAILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILD 453
Cdd:PRK11124 89 --QQYNlwphlTVQQNLIEAPcrvlglskdqalarAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 454 DPLSALDAHVGNHIFNsaIRKRLKSK--TVLFVTHQlqylVD-----CDEVIFMKEGCITERGTHE 512
Cdd:PRK11124 167 EPTAALDPEITAQIVS--IIRELAETgiTQVIVTHE----VEvarktASRVVYMENGHIVEQGDAS 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
945-1115 |
1.39e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.42 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 945 YRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFS 1024
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1025 GTVRSNLD-PFnqytedQIW-DALERTHMKECIAQLPLKlESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:PRK10247 95 DTVYDNLIfPW------QIRnQQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170
....*....|...
gi 1720387222 1103 MDTETDLLIQETI 1115
Cdd:PRK10247 168 LDESNKHNVNEII 180
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
903-1152 |
1.40e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 903 VERINHYIKtLSLEAPARIKNKApphdwpqegeVTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSlgma 982
Cdd:COG0488 294 PPRRDKTVE-IRFPPPERLGKKV----------LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 983 LFRL----VELSGGCIKIdGIRIsdigladlrsKLAIIPQEpvlfsgtvRSNLDPfnqytEDQIWDALERTHmkeciaql 1058
Cdd:COG0488 357 LLKLlageLEPDSGTVKL-GETV----------KIGYFDQH--------QEELDP-----DKTVLDELRDGA-------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1059 PLKLESEVME-------NGD-------NFSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliqetiREAFADC-- 1122
Cdd:COG0488 405 PGGTEQEVRGylgrflfSGDdafkpvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAld 476
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720387222 1123 ----TMLTIAH-R--LHTVlgSDRIMVLAQGQVVEFD 1152
Cdd:COG0488 477 dfpgTVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
313-515 |
1.59e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 313 TGSLRLQR--TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVS------GTFAYVAQQ--------- 375
Cdd:PRK15112 18 TGWFRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRirmifqdps 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 376 ---------AWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARALYS 445
Cdd:PRK15112 98 tslnprqriSQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsYYPHM-----------LAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 446 DRSIYILDDPLSALDAHVGNHIFNSAIRKRLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 515
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELQEKQGiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-509 |
1.69e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.67 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG----TFAYVAQQAWIL---------NATLRDNIL-F 389
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVvpqfdnldpDFTVRENLLvF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 390 GKEFD------EERYNSVLnscclrpDLAILPNSDLTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHv 463
Cdd:PRK13537 105 GRYFGlsaaaaRALVPPLL-------EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 464 GNHIfnsaIRKRLKS-----KTVLFVTHqlqylvdcdeviFMKEG-------CITERG 509
Cdd:PRK13537 173 ARHL----MWERLRSllargKTILLTTH------------FMEEAerlcdrlCVIEEG 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
953-1154 |
1.69e-10 |
|
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: 62.48 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGladlrsklaiiPQEPVLFSG------- 1025
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQNysllpwl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 TVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEvmENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1105
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1106 ETDLLIQETIREAFAD--CTMLTIAHRL-HTVLGSDRIMVLAQ------GQVVEFDTP 1154
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEhrVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEVPFP 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
427-516 |
1.73e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 427 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKE 502
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL--ALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQ 501
|
90
....*....|....
gi 1720387222 503 GCITERGTHEELMN 516
Cdd:PRK15134 502 GEVVEQGDCERVFA 515
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
936-1161 |
2.02e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISdiGLADL-RSKLA 1014
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARHaRQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1015 IIPQ----EPVLfsgTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMEngdnFSVGERQLLCIARALLRH 1090
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1091 CKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSVLLSND 1161
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
952-1150 |
2.37e-10 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 61.77 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADL-RSKLAIIPQEPVLFSG-TVRS 1029
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLdpfnqytedQI-WDALERTHMK--ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTE 1106
Cdd:TIGR03410 95 NL---------LTgLAALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 1107 TDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:TIGR03410 166 IIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-515 |
2.40e-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: 64.44 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGqmtLLEGSiavSGTFAYVAQQAWIlNATLRDNILFGKEfdeERYNSVLN 403
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPT---SGEVNVRVGDEWV-DMTKPGPDGRGRA---KRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 404 S-CCLRPDLAILPNsdLT---------EIGERGA-----------------------NLSGGQRQRISLARALYSDRSIY 450
Cdd:TIGR03269 372 QeYDLYPHRTVLDN--LTeaiglelpdELARMKAvitlkmvgfdeekaeeildkypdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 451 ILDDPLSALDAHVGNHIFNSAIRKRLK-SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 515
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
321-516 |
2.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.46 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI------AVSGTFAYVAQQAWIL---------NATLRD 385
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHIGIVfqnpdnqfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGKE-----FDE--ERYNSVLNscclrpDLAILPNSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:PRK13648 104 DVAFGLEnhavpYDEmhRRVSEALK------QVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 459 LDAHVGNHIFNsaIRKRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK13648 173 LDPDARQNLLD--LVRKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
321-514 |
2.55e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.83 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 321 TLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTfAYVAQQAW----------------ILNATLR 384
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvfqnpdnqFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGKE-----FDE--ERYNSVLNSCclrpdlailpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:PRK13650 101 DDVAFGLEnkgipHEEmkERVNEALELV------------GMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 457 SALDAHVGNHIFNS--AIRKRLKsKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK13650 169 SMLDPEGRLELIKTikGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
322-516 |
2.56e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIA------------------------------------- 364
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 365 ----VSGTFAYVAQQawILNATLRDNILFG-------KEFDEERYNSVLNSCCLrpDLAILPNSDLteigergaNLSGGQ 433
Cdd:PRK13651 103 irrrVGVVFQFAEYQ--LFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRSPF--------ELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 434 RQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKRL--KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG- 509
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGd 248
|
....*..
gi 1720387222 510 THEELMN 516
Cdd:PRK13651 249 TYDILSD 255
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
936-1129 |
2.76e-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: 59.77 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLveLSGGCIKIDGIRISDIGLadlrsKLAI 1015
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKST----LLKL--IAGELEPDEGIVTWGSTV-----KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQepvlFSGtvrsnldpfnqytedqiwdalerthmkeciaqlplklesevmengdnfsvGERQLLCIARALLRHCKILI 1095
Cdd:cd03221 68 FEQ----LSG--------------------------------------------------GEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 1720387222 1096 LDEATAAMDTETDLLIQETIREaFaDCTMLTIAH 1129
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-Y-PGTVILVSH 125
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-514 |
2.89e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.43 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 25 SNDGQRMFEAAAVGSLLAGGPVVAILGMIYnVIILGPTGFLGSAVFI----LFYpaMMFVSRLTAYFRRkcVAATDDRVQ 100
Cdd:COG4615 112 TEDVRTISQAFVRLPELLQSVALVLGCLAY-LAWLSPPLFLLTLVLLglgvAGY--RLLVRRARRHLRR--AREAEDRLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 101 K-MNEVLTYIKFIKM--------YAwvKAFSQCVQKIREEERRilekAGYFQSITVGVAPIV--VVIASVVTFSVHMtlg 169
Cdd:COG4615 187 KhFRALLEGFKELKLnrrrrrafFD--EDLQPTAERYRDLRIR----ADTIFALANNWGNLLffALIGLILFLLPAL--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 170 FHLTAAQAFTVVTVF----NSMTFALKVTPfsvkSLSEASVAVDRFKSLFLMEEvhmiknkPASPHikiEMKNATLAWDS 245
Cdd:COG4615 258 GWADPAVLSGFVLVLlflrGPLSQLVGALP----TLSRANVALRKIEELELALA-------AAEPA---AADAAAPPAPA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 246 SHSSIQnspkltpkmkkdkratrgkkeksrqLQHTEHQavlaeqkghllldsdeRPSPEEEEGKQIHtgslrlqrtlyNI 325
Cdd:COG4615 324 DFQTLE-------------------------LRGVTYR----------------YPGEDGDEGFTLG-----------PI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 326 DLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGtfAYVAQQAWilnATLRDNI--------LF------GK 391
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNR---EAYRQLFsavfsdfhLFdrllglDG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 392 EFDEERYNSVLNscclrpDLAIlpnSDLTEIgERGA----NLSGGQRQRISLARALYSDRSIYILD------DPlsalda 461
Cdd:COG4615 427 EADPARARELLE------RLEL---DHKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDewaadqDP------ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 462 hVGNHIFNSAIRKRLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:COG4615 491 -EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
935-1154 |
3.37e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 935 EVTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIdGIRISDIG-----L 1006
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1007 ADLRSKLAIIPQ--EPVLFSGTVRSNL--DPFNQYTEDQiwDALERThmKECIAQlpLKLESEVMENGD-NFSVGERQLL 1081
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDIcfGPMNFGVSEE--DAKQKA--REMIEL--VGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1082 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1154
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
326-524 |
3.39e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 326 DLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYVAQQ-AWIL--------NATLRDNILFGkef 393
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRpVSMLfqennlfsHLTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 394 deerynsvlnsccLRPDL-----------AILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:PRK10771 96 -------------LNPGLklnaaqreklhAIARQMGIEDLLARlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 462 HVGNHIFN----SAIRKRLkskTVLFVTHQLQylvDCDEV----IFMKEGCITERGTHEELMNLNGDYATI 524
Cdd:PRK10771 163 ALRQEMLTlvsqVCQERQL---TLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
952-1150 |
3.58e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDI---GLADLRSKLAIIPQEP---VLFSG 1025
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 TVRSNLD-PFNQYT----EDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEAT 1100
Cdd:PRK10419 107 TVREIIRePLRHLLsldkAERLARASEMLRAVDLDDSVLDKRPPQL-------SGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1101 AAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:PRK10419 180 SNL----DLVLQagvirllKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
957-1149 |
3.74e-10 |
|
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: 60.97 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 957 SFTIKPKEKIGIVGRTGSGKSSLG--MALFrLVELSGGcIKIDGIrisDIGLADL-RSKLAIIPQEPVLFSG-TVRSNLD 1032
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnlIAGF-ETPQSGR-VLINGV---DVTAAPPaDRPVSMLFQENNLFAHlTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1033 ----PFNQYTEDQ---IWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 1104
Cdd:cd03298 93 lglsPGLKLTAEDrqaIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 1105 ---TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:cd03298 162 alrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
648-777 |
5.02e-10 |
|
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: 61.79 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 648 MKDNPFMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV 727
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSD 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1720387222 728 RLPFQAEMFIQNVILVFFCVGMIAGVfPWFLVAVGplLILFSLLHIVSRV 777
Cdd:cd18572 109 PLSTNLNVFLRNLVQLVGGLAFMFSL-SWRLTLLA--FITVPVIALITKV 155
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
959-1142 |
6.46e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 959 TIKPKEKIGIVGRTGSGKSSLGMALfrlvelsGGCIKIDGirisdiGLADLRSKLAIIPQE-PVLFSGTVRSNLDpfnqy 1037
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDE------GEVDPELKISYKPQYiKPDYDGTVEDLLR----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1038 tedQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1116
Cdd:PRK13409 423 ---SITDDLGSSYYKSEIIK-PLQLE-RLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190
....*....|....*....|....*....|
gi 1720387222 1117 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1142
Cdd:PRK13409 498 R-IAeerEATALVVDHDIYMIdYISDRLMV 526
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
322-516 |
6.59e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.72 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-----------------TFAYVAQ--QAWILNAT 382
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFG-KEFdeerynsvlnscclrpdlailpNSDLTEIGERGANL------------------SGGQRQRISLARAL 443
Cdd:PRK13646 103 VEREIIFGpKNF----------------------KMNLDEVKNYAHRLlmdlgfsrdvmsqspfqmSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 444 YSDRSIYILDDPLSALDAHVGNHIFNsaIRKRLK---SKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMR--LLKSLQtdeNKTIILVSHDMnevaRY---ADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
317-487 |
6.65e-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: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLYN-IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------------FAYVAQQAWILNA-T 382
Cdd:cd03231 10 RDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIKTTlS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFGKEFDEEryNSVLNScclrpdlaiLPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:cd03231 90 VLENLRFWHADHSD--EQVEEA---------LARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*..
gi 1720387222 462 HvGNHIFNSAIRKRL-KSKTVLFVTHQ 487
Cdd:cd03231 159 A-GVARFAEAMAGHCaRGGMVVLTTHQ 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
319-516 |
6.70e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.94 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAIlGQMTLLEGSIAVSGTFAY---------------------VAQQAW 377
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ILNATLRDNILFGKEFDEERYNSVLNSCCLRpdlAILPNSDLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 453
Cdd:PRK14239 97 PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 454 DPLSALDAHVGNHIFNSAIrkRLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEELMN 516
Cdd:PRK14239 174 EPTSALDPISAGKIEETLL--GLKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMN 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
325-514 |
6.74e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILFG-- 390
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSVRENMAYGlk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 391 -----KEFDEERynsvlnscclrpdlaILPNSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:PRK11650 103 irgmpKAEIEER---------------VAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 462 HVGNHIfNSAIRK---RLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK11650 168 KLRVQM-RLEIQRlhrRLKT-TSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
265-507 |
7.50e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 265 RATRGKKEKSRQ-----LQHTEHQAVlaEQKGHLLLDSDERPspeeeeGKQIhtgsLRLQ--------RTLY-NIDLEIE 330
Cdd:COG0488 272 KARKAKQAQSRIkalekLEREEPPRR--DKTVEIRFPPPERL------GKKV----LELEglsksygdKTLLdDLSLRID 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 331 EGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--FAYVAQQAWIL--NATLRDNILFGKEFDEERY-NSVLNSC 405
Cdd:COG0488 340 RGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvkIGYFDQHQEELdpDKTVLDELRDGAPGGTEQEvRGYLGRF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 406 CLRPDLAilpnsdLTEIGergaNLSGGQRQRISLARALYSDRSIYILDDP------------LSALDAHVGnhifnsair 473
Cdd:COG0488 420 LFSGDDA------FKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldietlealEEALDDFPG--------- 480
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720387222 474 krlkskTVLFVTHQlQYLVD--CDEVIFMKEGCITE 507
Cdd:COG0488 481 ------TVLLVSHD-RYFLDrvATRILEFEDGGVRE 509
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
956-1174 |
8.23e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.16 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIglADLRSKLAIIPQEPVLFSG-TVRSNLD-- 1032
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIAfg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1033 ------PFNQYTeDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTE 1106
Cdd:PRK11607 116 lkqdklPKAEIA-SRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1107 ----TDLLIQETIREAFADCTMLTiaH---RLHTVLGsdRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1174
Cdd:PRK11607 184 lrdrMQLEVVDILERVGVTCVMVT--HdqeEAMTMAG--RIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
959-1142 |
8.75e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 959 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGirisdiGLADLRSKLAIIPQEPV-LFSGTVRSNLdpfnqy 1037
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTF-------AKILAGVLKPDE------GEVDEDLKISYKPQYISpDYDGTVEEFL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1038 tEDQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1116
Cdd:COG1245 423 -RSANTDDFGSSYYKTEIIK-PLGLE-KLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|
gi 1720387222 1117 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1142
Cdd:COG1245 500 R-FAenrGKTAMVVDHDIYLIdYISDRLMV 528
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
324-514 |
8.99e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.26 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAW----------------ILNATLRDNI 387
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvfqnpdnqIVATIVEEDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 388 LFGKEfdeerynsvlnscclrpDLAILPNsdltEIGERGAN-----------------LSGGQRQRISLARALYSDRSIY 450
Cdd:PRK13633 108 AFGPE-----------------NLGIPPE----EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 451 ILDDPLSALDAHVGNHIFNSAirKRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTI--KELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
324-515 |
1.01e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 61.29 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-FAYVAQQAW------------------------- 377
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrmqmvfqdpyaslnprmtvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 -ILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteigERGAN-LSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:COG4608 116 dIIAEPLRIHGLASKAERRERVAELLELVGLRPEHA-----------DRYPHeFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 456 LSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELM 515
Cdd:COG4608 185 VSALDVSIQAQVLN--LLEDLQDElglTYLFISHDLsvvRHI--SDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
319-500 |
1.07e-09 |
|
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: 58.87 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILgqmtllegsiavsgtfayvaqqawilnatlrdnilfgKEFDEERY 398
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------------------------YASGKARL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 399 NSVLNSCCLRPDLAILPNSDLTEIG------ERGAN-LSGGQRQRISLARALYSD--RSIYILDDPLSALDAHVGNHIFN 469
Cdd:cd03238 51 ISFLPKFSRNKLIFIDQLQFLIDVGlgyltlGQKLStLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLE 130
|
170 180 190
....*....|....*....|....*....|.
gi 1720387222 470 SAIRKRLKSKTVLFVTHQLQYLVDCDEVIFM 500
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
953-1149 |
1.24e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISdiglaDLRSKLA------IIPQE-PVLFSG 1025
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN-----KLDHKLAaqlgigIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 TVRSNLdPFNQYTEDQIW--DALERTHMKECIAQLPLK--LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1101
Cdd:PRK09700 96 TVLENL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1102 AM-DTETD---LLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:PRK09700 175 SLtNKEVDylfLIMNQLRKEGTA---IVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
952-1149 |
1.26e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISdiGLADL-RSKL-AIIPQEPVL---FSGT 1026
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYkRAKYiGRVFQDPMMgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1027 VRSNLdpfnqytedqiwdAL-----------------ERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLR 1089
Cdd:COG1101 99 IEENL-------------ALayrrgkrrglrrgltkkRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1090 HCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVL--GsDRIMVLAQGQVV 1149
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEEnnLTTLMVTHNMEQALdyG-NRLIMMHEGRII 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
315-516 |
1.71e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 315 SLRL-QRT-LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG------------------------T 368
Cdd:PRK13548 9 SVRLgGRTlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarrravlpqhsslS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 369 FAYVAQQ-------AWILNATLRDNILfgkefdeeryNSVLNSCclrpDLAILPNSDLTEigerganLSGGQRQRISLAR 441
Cdd:PRK13548 89 FPFTVEEvvamgraPHGLSRAEDDALV----------AAALAQV----DLAHLAGRDYPQ-------LSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 442 AL------YSDRSIYILDDPLSALD-AHvGNHIFNSAirKRLKSK---TVLFVTHQL----QYlvdCDEVIFMKEGCITE 507
Cdd:PRK13548 148 VLaqlwepDGPPRWLLLDEPTSALDlAH-QHHVLRLA--RQLAHErglAVIVVLHDLnlaaRY---ADRIVLLHQGRLVA 221
|
....*....
gi 1720387222 508 RGTHEELMN 516
Cdd:PRK13548 222 DGTPAEVLT 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
952-1149 |
2.47e-09 |
|
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: 58.88 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSgtvrsNL 1031
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWW-----DL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 DPFNQYTEDQ-IWDaLERTHMKECIAQLP--LKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1108
Cdd:cd03267 111 PVIDSFYLLAaIYD-LPPARFKKRLDELSelLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720387222 1109 LLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:cd03267 190 ENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
953-1149 |
2.64e-09 |
|
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: 60.99 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVELSG---GCIKIDGIRISDIGLADLRSK-LAIIPQEPVLFSG-TV 1027
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 RSNLDPFNQYTE--DQIWDALERTHMKECIAQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKILILDEATAAM-D 1104
Cdd:TIGR02633 96 AENIFLGNEITLpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 1105 TETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:TIGR02633 175 KETEILL-DIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
952-1154 |
2.98e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGiRIS---DIGLA---DL--RsklaiipqEPVLF 1023
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSallELGAGfhpELtgR--------ENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 SGTVrsnldpfNQYTEDQIwdaleRTHMKECIA--------QLPLKlesevmengdNFSVGERQLLCIARALLRHCKILI 1095
Cdd:COG1134 112 NGRL-------LGLSRKEI-----DEKFDEIVEfaelgdfiDQPVK----------TYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1096 LDEATAAMDTE-----TDlLIQETIREAfadCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1154
Cdd:COG1134 170 VDEVLAVGDAAfqkkcLA-RIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
649-865 |
3.02e-09 |
|
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: 59.79 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 649 KDNPFMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 728
Cdd:cd18545 34 GDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 729 lpfqAEMF---IQNVILVFFCVGMIAGV---FPWFL----VAVGPLLILFSllhIVSRVLIRELKRLDNITQSPFLSHIT 798
Cdd:cd18545 111 ----SDLLsngLINLIPDLLTLVGIVIImfsLNVRLalvtLAVLPLLVLVV---FLLRRRARKAWQRVRKKISNLNAYLH 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 799 SSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFflftcaMRwlAVRL-DLI--SIALITTTGLMIVLMHG 865
Cdd:cd18545 184 ESISGIRVIQSFAREDENEEIFDELNRENRKAN------MR--AVRLnALFwpLVELISALGTALVYWYG 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
320-510 |
3.19e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.36 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILG-----QMTLLEGSIAVSGTfayvAQQAWILNATLRDNILFgkEFD 394
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSST----SKQKEIKPVRKKVGVVF--QFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 395 EERY--NSVLNSCCLRPDLAILPNSDLTEIGERGAN---------------LSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:PRK13643 94 ESQLfeETVLKDVAFGPQNFGIPKEKAEKIAAEKLEmvgladefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 458 ALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 510
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
660-828 |
3.54e-09 |
|
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: 59.38 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 660 IYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmdevDVrlpfqaeM 735
Cdd:cd18570 43 IISIGLILLYLFQSllsyIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN------DA-------N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 736 FIQNVI-----------LVFFCVGMIAGVFPW--FLVAVGPLLILFSLLHIVSRVLIRELKRLdNITQSPFLSHITSSIQ 802
Cdd:cd18570 110 KIREAIssttislfldlLMVIISGIILFFYNWklFLITLLIIPLYILIILLFNKPFKKKNREV-MESNAELNSYLIESLK 188
|
170 180
....*....|....*....|....*.
gi 1720387222 803 GLATIHAYNKRQEFLHRYQELLDDNQ 828
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLL 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
936-1162 |
3.56e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.41 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRIS----DIGLAD 1008
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1009 LRSKLAIIPQ--EPVLFSGTVRSNL----DPFNQYTEDqiwdalerthMKECIAQLPLKL--ESEVMENGD-NFSVGERQ 1079
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIifgpKNFKMNLDE----------VKNYAHRLLMDLgfSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1080 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSV 1156
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
....*.
gi 1720387222 1157 LLSNDS 1162
Cdd:PRK13646 233 LFKDKK 238
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
662-826 |
4.03e-09 |
|
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: 59.11 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 662 ALSMAVMLILKAIrgVVFVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 735
Cdd:cd18557 39 ALILLAIYLLQSV--FTFVRYYLfniageRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 736 FIQNVILVFFCVGMIAgVFPWFLVAVgpLLILFSLLHIVSRVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYNK 812
Cdd:cd18557 117 LLRNILQVIGGLIILF-ILSWKLTLV--LLLVIPLLLIASKIYGRYIRKLSKEVQDALAkagQVAEESLSNIRTVRSFSA 193
|
170
....*....|....
gi 1720387222 813 RQEFLHRYQELLDD 826
Cdd:cd18557 194 EEKEIRRYSEALDR 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-527 |
4.62e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.51 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAiLGQMTLLEGSIAVSGTFAY---------------------VAQQAWILN 380
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLIPGARVEGEILLdgediydpdvdvvelrrrvgmVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 381 ATLRDNILFG---------KEFDE--ERynsvlnscCLRpdLAILPNsdltEIGER----GANLSGGQRQRISLARALYS 445
Cdd:COG1117 106 KSIYDNVAYGlrlhgikskSELDEivEE--------SLR--KAALWD----EVKDRlkksALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 446 DRSIYILDDPLSALD----AHVGNHIfnsairKRLKSK-TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEElmnlng 519
Cdd:COG1117 172 EPEVLLMDEPTSALDpistAKIEELI------LELKKDyTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQ------ 239
|
....*...
gi 1720387222 520 dyatIFNN 527
Cdd:COG1117 240 ----IFTN 243
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
939-1150 |
4.99e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.31 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 939 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGIRI--SDIGLADLRS 1011
Cdd:PRK14267 8 VNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1012 KLAIIPQEPVLFSG-TVRSN----------LDPFNQYTEDQIWdALERthmkeciAQLPLKLESEVMENGDNFSVGERQL 1080
Cdd:PRK14267 86 EVGMVFQYPNPFPHlTIYDNvaigvklnglVKSKKELDERVEW-ALKK-------AALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1081 LCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHR-LHTVLGSDRIMVLAQGQVVE 1150
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
15-191 |
5.00e-09 |
|
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: 58.81 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 15 KSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPT-GFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 93
Cdd:pfam00664 95 NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAVFAKILRKLSRKEQK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 94 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVT--FSVHMTLGFH 171
Cdd:pfam00664 175 AVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALAlwFGAYLVISGE 254
|
170 180
....*....|....*....|
gi 1720387222 172 LTAAQAFTVVTVFNSMTFAL 191
Cdd:pfam00664 255 LSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
298-493 |
5.81e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 298 DERPSPEEEEGKQIHTGSlRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYV 372
Cdd:PRK13409 327 EERPPRDESERETLVEYP-DLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 373 AQ----------QAWILNATlrdnilfgKEFDEERYNSVLnsccLRP-DLAILPNSDLTEigerganLSGGQRQRISLAR 441
Cdd:PRK13409 406 PQyikpdydgtvEDLLRSIT--------DDLGSSYYKSEI----IKPlQLERLLDKNVKD-------LSGGELQRVAIAA 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 442 ALYSDRSIYILDDPLSALDAH----VGnhifnSAIRK--RLKSKTVLFVTHQLqYLVD 493
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEqrlaVA-----KAIRRiaEEREATALVVDHDI-YMID 518
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-514 |
5.93e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWILNA-------------------- 381
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLRDNILF---GKEFDEERYNSVLNSCCLRPdlAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:PRK14246 106 SIYDNIAYplkSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 459 LDAhVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
936-1152 |
6.05e-09 |
|
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: 57.65 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADlrSKLAI 1015
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1016 IPQEPVLFSG-TVRSNLD---PFNQYTEDQIwdaLERTHMkecIAQLpLKLESEVMENGDNFSVGERQLLCIARALLRHC 1091
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAfglKLRKVPKDEI---DERVRE---VAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1092 KILILDEATAAMDTEtdlliqetIREAfadctMLTIAHRLHTVLG----------------SDRIMVLAQGQVVEFD 1152
Cdd:cd03301 150 KVFLMDEPLSNLDAK--------LRVQ-----MRAELKRLQQRLGtttiyvthdqveamtmADRIAVMNDGQIQQIG 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
944-1132 |
6.05e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.90 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 944 RYREN--LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGI---RISDIGLADLRS-KLAIIP 1017
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1018 QepvlfsgtvrsnldpFNQYTEDqiWDALERTHMKECIAQLPLK--------------LESEVMENGDNFSVGERQLLCI 1083
Cdd:PRK11629 94 Q---------------FHHLLPD--FTALENVAMPLLIGKKKPAeinsralemlaavgLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1084 ARALLRHCKILILDEATAAMDTET-----DLLIQETIRE--AFADCTM-LTIAHRLH 1132
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNadsifQLLGELNRLQgtAFLVVTHdLQLAKRMS 213
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
670-824 |
6.26e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 58.76 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 670 ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVRLPFQAEMFIQNVILVFFCVGM 749
Cdd:cd18782 57 VLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAV 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 750 IAgVFPWFL----VAVGPLLILFSLLhiVSRVLIRELKRLdNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELL 824
Cdd:cd18782 136 LF-SYSPLLtlvvLATVPLQLLLTFL--FGPILRRQIRRR-AEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRY 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
953-1161 |
6.30e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----------VELSGGCIKIDGIRISDIGLA-----------DLRS 1011
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKSrantgyifqqfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1012 KLAIIpqEPVLFS--GTV---RSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARA 1086
Cdd:PRK09984 100 RLSVL--ENVLIGalGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTL-----------SGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1087 LLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVeFDTPSVLLSND 1161
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNE 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
309-505 |
6.85e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.17 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 309 KQIHTGSLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYVAQQA-WIL----- 379
Cdd:COG1101 9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAkYIGrvfqd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 380 -------NATLRDNILF----GKEF---------DEERYnsvlnscclRPDLAILpnsDL-------TEIGergaNLSGG 432
Cdd:COG1101 89 pmmgtapSMTIEENLALayrrGKRRglrrgltkkRRELF---------RELLATL---GLglenrldTKVG----LLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 433 QRQRISLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKrlKSKTVLFVTHQLQYLVDC-DEVIFMKEGCI 505
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELTEKIVEE--NNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
654-882 |
8.11e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 58.25 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 654 MQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfQ- 732
Cdd:cd18577 46 VNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLI------Qd 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 733 --AE---MFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLLILFSLlhIVSRVLIR-ELKRLDNITQSpfLSHITSS 800
Cdd:cd18577 120 giGEklgLLIQSLSTFIagFIIAFIYS---WkltlVLLATLPLIAIVGG--IMGKLLSKyTKKEQEAYAKA--GSIAEEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 801 IQGLATIHAYNKRQEFLHRYQELLDDnqapfflftcAMRWlAVRLDLISialitttGLMIVLMHGQIPSAYAgLAISYAV 880
Cdd:cd18577 193 LSSIRTVKAFGGEEKEIKRYSKALEK----------ARKA-GIKKGLVS-------GLGLGLLFFIIFAMYA-LAFWYGS 253
|
..
gi 1720387222 881 QL 882
Cdd:cd18577 254 RL 255
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
430-543 |
8.20e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 430 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKRLKSKTVlFVTHQLQyLVD--CDEVIFMKEGCI 505
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNlmMDLQQELGLSYV-FISHDLS-VVEhiADEVMVMYLGRC 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720387222 506 TERGTHEelmnlngdyaTIFNN-------LLLGETPPVEINSKKE 543
Cdd:PRK11308 234 VEKGTKE----------QIFNNprhpytqALLSATPRLNPDDRRE 268
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
298-493 |
9.18e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 298 DERPSPEEEEGKQIHTGSlRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYV 372
Cdd:COG1245 328 EVHAPRREKEEETLVEYP-DLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 373 AQqaWILN-------ATLRDNIlfGKEFDEERYNSVLnsccLRPdLAI--LPNSDLTEigerganLSGGQRQRISLARAL 443
Cdd:COG1245 407 PQ--YISPdydgtveEFLRSAN--TDDFGSSYYKTEI----IKP-LGLekLLDKNVKD-------LSGGELQRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 444 YSDRSIYILDDPLSALDA----HVGnhifnSAIRK--RLKSKTVLFVTHQLqYLVD 493
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVeqrlAVA-----KAIRRfaENRGKTAMVVDHDI-YLID 520
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
602-865 |
9.42e-09 |
|
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: 58.20 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 602 FLVIMVLFMLNVGSTAFSTWWLSYWIkqgsgnstvyqgNRSFVSDSMkdnpfmqyyASIYALSMAVMLILkAIRGVV-FV 680
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLL------------DDIFVEKDL---------EALLLVPLAIIGLF-LLRGLAsYL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 681 KGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVF 754
Cdd:cd18552 59 QTYLmayvgqRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLF-YL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 755 PWFLVAVgpLLILFSLLHIVSRVLIRELKRLDNITQSpFLSHITS----SIQGLATIHAYNKRQEFLHRYQELLDDNqap 830
Cdd:cd18552 138 DWKLTLI--ALVVLPLAALPIRRIGKRLRKISRRSQE-SMGDLTSvlqeTLSGIRVVKAFGAEDYEIKRFRKANERL--- 211
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720387222 831 fflFTCAMRWLAVRlDLIS--IALITTTGLMIVLMHG 865
Cdd:cd18552 212 ---RRLSMKIARAR-ALSSplMELLGAIAIALVLWYG 244
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
320-516 |
1.20e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.44 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWILN---------------ATLR 384
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFG-------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPL 456
Cdd:PRK13647 99 DDVAFGpvnmgldKDEVERRVEEALKAV------------RMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 457 SALDAHVGNHIFnsAIRKRL--KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK13647 167 AYLDPRGQETLM--EILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
319-516 |
1.33e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQQAWILNA-TL 383
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNIL--------FGKEFDEERYNSVL---NSCCLRPDLailpnsdlteigerGANLSGGQRQRISLARALYSDRSIYIL 452
Cdd:PRK10895 96 YDNLMavlqirddLSAEQREDRANELMeefHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 453 D------DPLSALD-AHVGNHIFNSAIrkrlkskTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK10895 162 DepfagvDPISVIDiKRIIEHLRDSGL-------GVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
650-863 |
1.36e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 57.85 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 650 DNPFMQYYASIYALSM----AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTP--TGRILNRFSKDMD 723
Cdd:cd18578 43 DDDELRSEANFWALMFlvlaIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 724 EV----DVRLPfqaeMFIQNVILVFFCVGmIAGVFPWFL----VAVGPLLILFSLLHIvsRVLIR-ELKRLDNITQSpfl 794
Cdd:cd18578 123 DVrglvGDRLG----LILQAIVTLVAGLI-IAFVYGWKLalvgLATVPLLLLAGYLRM--RLLSGfEEKNKKAYEES--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 795 SHITS-SIQGLATIHAYNKRQEFLHRYQELLDDNQ-------------------APFFLFTCAMRWLAVrldLISIALIT 854
Cdd:cd18578 193 SKIASeAVSNIRTVASLTLEDYFLEKYEEALEEPLkkglrralisglgfglsqsLTFFAYALAFWYGGR---LVANGEYT 269
|
....*....
gi 1720387222 855 TTGLMIVLM 863
Cdd:cd18578 270 FEQFFIVFM 278
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
954-1148 |
1.79e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 954 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAD-LRSKLAIIP---QEPVLF------ 1023
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1024 --SGTVRSNLDPFNQYT--EDQIwdaLERTHmkeciAQLPLKLeSEVMENGDNFSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:PRK15439 360 wnVCALTHNRRGFWIKParENAV---LERYR-----RALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1100 TAAMDTETDLLIQETIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQV 1148
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
324-515 |
1.82e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSI--------------AVSGTFAYVAQQ----AWILNATLRD 385
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkdisprspldAVKKGMAYITESrrdnGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGKEFDEERYNSVLN----------SCCLRPDLAILPNSDLTEIGErganLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:PRK09700 361 NMAISRSLKDGGYKGAMGlfhevdeqrtAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 456 LSALDAHVGNHIFnSAIRKRLKS-KTVLFVTHQL-QYLVDCDEVIFMKEGCITE------RGTHEELM 515
Cdd:PRK09700 437 TRGIDVGAKAEIY-KVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQiltnrdDMSEEEIM 503
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
952-1166 |
1.85e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.58 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFR----LVELSGGCIKIDGIRISDIGLaDLRSKLAI--IPQEPVLFSG 1025
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 -TVRSNLDPFNQYTEdqiwdaLERTHMKECIAQLplkLE----SEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:COG1137 93 lTVEDNILAVLELRK------LSKKEREERLEEL---LEefgiTHLRKSkAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1100 TAAMD--TETDllIQETIREafadctmLT---IA-----HRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR-FY 1166
Cdd:COG1137 164 FAGVDpiAVAD--IQKIIRH-------LKergIGvlitdHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPLVRkVY 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
929-1161 |
1.95e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 929 DWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAD 1008
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1009 LRSKLAIIPQE-PVLFSGTVRSnLDPFNQYTedqiWD-------ALERTHMKECIAQLPLK-LESEVMengDNFSVGERQ 1079
Cdd:PRK10575 83 FARKVAYLPQQlPAAEGMTVRE-LVAIGRYP----WHgalgrfgAADREKVEEAISLVGLKpLAHRLV---DSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1080 LLCIARALLRHCKILILDEATAAMD----TETDLLIQETIREafadcTMLTIAHRLHTVLGS----DRIMVLAQGQVVEF 1151
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQE-----RGLTVIAVLHDINMAarycDYLVALRGGEMIAQ 229
|
250
....*....|
gi 1720387222 1152 DTPSVLLSND 1161
Cdd:PRK10575 230 GTPAELMRGE 239
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
322-501 |
2.04e-08 |
|
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: 54.67 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAIlgqmtllegsiavsgtfayvaqqawILNATLRDNILFGKEFDEERYNSV 401
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAI-------------------------GLALGGAQSATRRRSGVKAGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 402 LNSCCLRpdlailpnsdLTEIGerganLSGGQRQRISLARAL----YSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLK 477
Cdd:cd03227 66 AVSAELI----------FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK 130
|
170 180
....*....|....*....|....
gi 1720387222 478 SKTVLFVTHQLQYLVDCDEVIFMK 501
Cdd:cd03227 131 GAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
952-1160 |
2.33e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.30 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRI-SDIGLADLRSKLAIIPQEpvlfSGTVRSN 1030
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQH----VGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEVMENGDN------FSVGERQLLCIARALLRHCKILI 1095
Cdd:PRK11264 94 FNLFPHRT------VLEniiegpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1096 LDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1160
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
643-826 |
2.45e-08 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 56.75 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 643 FVSDSMKDNPFMQYYASIYALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRF 718
Cdd:cd18573 25 VASKESGDIEIFGLSLKTFALALLGVFVVGAAanfgRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 719 SKDMDEVdvrlpfqAEMFIQNV-------ILVFFCVGMiagvfpwfLVAVGPLLILFSLL-----HIVSRVLIRELKRLD 786
Cdd:cd18573 105 SSDTSVV-------GKSLTQNLsdglrslVSGVGGIGM--------MLYISPKLTLVMLLvvppiAVGAVFYGRYVRKLS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720387222 787 NITQSPfLSHITSS----IQGLATIHAYNKRQEFLHRYQELLDD 826
Cdd:cd18573 170 KQVQDA-LADATKVaeerLSNIRTVRAFAAERKEVERYAKKVDE 212
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
955-1159 |
2.59e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 955 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRlVELSGGCIKIDGIRISDIGLADL----RSKL-----AIIPQEPvlfsg 1025
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLspreRRKLvghnvSMIFQEP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 tvRSNLDPfNQYTEDQIWDAL----------ERTHMK-----ECIAQLPLKLESEVMENGD-NFSVGERQLLCIARALLR 1089
Cdd:PRK15093 99 --QSCLDP-SERVGRQLMQNIpgwtykgrwwQRFGWRkrraiELLHRVGIKDHKDAMRSFPyELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1090 HCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
936-1155 |
2.84e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.67 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIG----LAD 1008
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1009 LRSKLAIIPQEP--VLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVGER 1078
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMvglaDEFWEKSPFEL-----------SGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1079 QLLCIARALLRHCKILILDEATAAMDTETDLLIQ---ETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1154
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
.
gi 1720387222 1155 S 1155
Cdd:PRK13643 229 S 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
324-516 |
3.13e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAV----------SGTFAYVAQQAWILNA------------ 381
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFkelrrrvsmvfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 ---------TLRDNILFG-------KEFDEERYNSVLNSCCLRPDLAilpnsdlteigERGA-NLSGGQRQRISLARALY 444
Cdd:PRK13631 124 fpeyqlfkdTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYL-----------ERSPfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 445 SDRSIYILDDPLSALDAHvGNHIFNSAIRKRLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT-HEELMN 516
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTpYEIFTD 266
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
953-1153 |
3.88e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG------GCIKIDG--IRISDIGLAdLRSKLAIIPQE----P 1020
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL------LKILSGnyqpdaGSILIDGqeMRFASTTAA-LAAGVAIIYQElhlvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1021 VLfsgTVRSNLdpfnqytedqiwdalerthmkeCIAQLPLK--------LESEVMEN----GDNF---------SVGERQ 1079
Cdd:PRK11288 93 EM---TVAENL----------------------YLGQLPHKggivnrrlLNYEAREQlehlGVDIdpdtplkylSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 1080 LLCIARALLRHCKILILDEATAAMDT-ETDLLIQeTIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQVVE-FDT 1153
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAEGRvILYVSHRMEEIFAlCDAITVFKDGRYVAtFDD 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
320-484 |
4.08e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWILNA---------------TLR 384
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGKEF-DEERYNSVLNSCC-LRPDLailpnsdLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 462
Cdd:PRK11614 99 ENLAMGGFFaERDQFQERIKWVYeLFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180
....*....|....*....|..
gi 1720387222 463 VGNHIFNSAIRKRLKSKTVLFV 484
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLV 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
952-1154 |
4.90e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.40 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKpKEKI-GIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDigLADLRSKLAIIPQEPVLFSGTVRSN 1030
Cdd:PRK13631 41 ALNNISYTFE-KNKIyFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD--KKNNHELITNPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LDPFNQYTEDQIW-DALERTHMKECIAQLPLKLES--------EVMENGDNF--------SVGERQLLCIARALLRHCKI 1093
Cdd:PRK13631 118 VSMVFQFPEYQLFkDTIEKDIMFGPVALGVKKSEAkklakfylNKMGLDDSYlerspfglSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1094 LILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1154
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
320-503 |
5.10e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILG--QMTLLEGSIAVSGT--------------FAYVAQQ-AWILNAT 382
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFGKEFDEE----RYNSVLNSC-CLRPDLAILPNSDLTEIGERGanlsGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:TIGR02633 95 VAENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 458 ALDAHVGNHIFNsaIRKRLKSKTV--LFVTHQLQYL-VDCDEVIFMKEG 503
Cdd:TIGR02633 171 SLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDG 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
942-1163 |
5.26e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 942 EMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG-----IRISD--IGLAD------ 1008
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDgqLKVADknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1009 LRSKLAIIPQEPVLFSG-TVRSNLdpfnQYTEDQIWdALERTHMKECIAQLPLKL---ESEVMENGDNFSVGERQLLCIA 1084
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHmTVLENV----MEAPIQVL-GLSKQEARERAVKYLAKVgidERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1085 RALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
....
gi 1720387222 1160 NDSS 1163
Cdd:PRK10619 242 NPQS 245
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
666-771 |
6.03e-08 |
|
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: 55.52 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 666 AVMLILKAIRGVV-FVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ 738
Cdd:cd18542 43 LLILGVALLRGVFrYLQGYLaekasqKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720387222 739 NVILVFFCVGMIAGVFP---WFLVAVGPLLILFSLL 771
Cdd:cd18542 123 AVLLFIGALIIMFSINWkltLISLAIIPFIALFSYV 158
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
951-1149 |
6.22e-08 |
|
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: 54.58 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 951 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGIRISDiglADLRSKLAIIPQEPVLFSG-T 1026
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1027 VRSNLdpfnQYTedqiwdALERTHmkECIAQLPLKLESEVMENGD------------NFSVGERQLLCIARALLRHCKIL 1094
Cdd:cd03234 98 VRETL----TYT------AILRLP--RKSSDAIRKKRVEDVLLRDlaltriggnlvkGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1095 ILDEATAAMDTETDLLIQETIREafadctmltIAHRLHTVLGS------------DRIMVLAQGQVV 1149
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQ---------LARRNRIVILTihqprsdlfrlfDRILLLSSGEIV 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
310-503 |
6.94e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.79 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 310 QIHTGSLRLqrtLYNIDLEIEEGKLVGICGSVGSGKTSL--VSAILGQMTLLEGSIAVSG-----TFA----YVAQQ-AW 377
Cdd:cd03232 14 PVKGGKRQL---LNNISGYVKPGTLTALMGESGAGKTTLldVLAGRKTAGVITGEILINGrpldkNFQrstgYVEQQdVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ILNATLRDNILFgkefdeerynsvlnSCCLRpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:cd03232 91 SPNLTVREALRF--------------SALLR-------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 458 ALDAHVGNHIFNsAIRKRLKS-KTVLFVTHQ-----LQYLvdcDEVIFMKEG 503
Cdd:cd03232 138 GLDSQAAYNIVR-FLKKLADSgQAILCTIHQpsasiFEKF---DRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
328-493 |
6.94e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.72 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 328 EIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-TFAYVAQQAWILNATLRDNILFGKEfdeeryNSVLNSCC 406
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSIT------KDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 407 LRPDlaILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDahVGNHIFNSAIRKRL---KSKTVL 482
Cdd:cd03237 95 FKTE--IAKPLQIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMASKVIRRFaenNEKTAF 170
|
170
....*....|....
gi 1720387222 483 FVTHQL---QYLVD 493
Cdd:cd03237 171 VVEHDIimiDYLAD 184
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
662-906 |
7.06e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.59 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 662 ALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVI 741
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 742 LVFFCVGMIAGVFPWFLVAV---GPLLILFSLLH--IVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYNKRQEF 816
Cdd:cd18563 130 MIIGIGVVLFSLNWKLALLVlipVPLVVWGSYFFwkKIRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAFGQEKRE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 817 LHRYQELLDDnqapfflftcamrWLAVRLDLIS--------IALITTTGLMIV-------LMHGQIP----SAYaglaIS 877
Cdd:cd18563 205 IKRFDEANQE-------------LLDANIRAEKlwatffplLTFLTSLGTLIVwyfggrqVLSGTMTlgtlVAF----LS 267
|
250 260
....*....|....*....|....*....
gi 1720387222 878 YAVQLTGLFQFTVRLASETEARFTSVERI 906
Cdd:cd18563 268 YLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
322-507 |
8.67e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGqmtLLEGSiavSGTFAYVAQQAWILN----ATLR-DNILFgkefdee 396
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGS---SGEVSLVGQPLHQMDeearAKLRaKHVGF------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 397 rynsVLNSCCLRPDLAILPNSDLTEI----------------------GER----GANLSGGQRQRISLARALYSDRSIY 450
Cdd:PRK10584 93 ----VFQSFMLIPTLNALENVELPALlrgessrqsrngakalleqlglGKRldhlPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 451 ILDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 507
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSlNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
429-514 |
9.17e-08 |
|
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: 56.23 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSKT---VLFVTHQLQyLVD--CDEVIFMKEG 503
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIL--DLLKDLQRELgmaLLLITHDLG-VVRrfADRVAVMRQG 233
|
90
....*....|.
gi 1720387222 504 CITERGTHEEL 514
Cdd:COG4172 234 EIVEQGPTAEL 244
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
952-1155 |
1.42e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIG---LADLRSK-LAIIPQEPVLFSG-T 1026
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRREhFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1027 VRSNLD-PfnqytedQIWDALERTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1103
Cdd:PRK10535 103 AAQNVEvP-------AVYAGLERKQRLLRAQELlqRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1104 DT---ETDLLIQETIREafADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEfDTPS 1155
Cdd:PRK10535 176 DShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPA 227
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
661-865 |
1.44e-07 |
|
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: 54.41 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 661 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 736
Cdd:cd18576 38 IALLLLGLFLLQAVfsffRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 737 IQNVILVFFCVGMIAGVFP---WFLVAVGPLLILFSLlhIVSRVlIREL--KRLDNITQSpfLSHITSSIQGLATIHAYN 811
Cdd:cd18576 118 LRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAV--LFGRR-IRKLskKVQDELAEA--NTIVEETLQGIRVVKAFT 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 812 KRQEFLHRYQELLDDnqapffLFTCAMRWLAVRLDLIS-IALITTTGLMIVLMHG 865
Cdd:cd18576 193 REDYEIERYRKALER------VVKLALKRARIRALFSSfIIFLLFGAIVAVLWYG 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
324-514 |
1.48e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.41 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYV--AQQAWI------LN----ATLRDNIL 388
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvRFRSPrdAQAAGIaiihqeLNlvpnLSVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKE------FD----EERYNSVLNscclRPDLAILPNsdlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:COG1129 102 LGREprrgglIDwramRRRARELLA----RLGLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 459 LDAHVGNHIFNsAIRkRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:COG1129 171 LTEREVERLFR-IIR-RLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
322-498 |
1.52e-07 |
|
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: 54.16 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQ--MTLLEGSIAVSGTFAYVAQQAWI----------LNATLRDN--- 386
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIdkvividqspIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ---------ILF-----GKEFDEE----RYN-----SVLNSCC------------LRPDLAILPNSDLTEI--GERGANL 429
Cdd:cd03271 91 ytgvfdeirELFcevckGKRYNREtlevRYKgksiaDVLDMTVeealeffenipkIARKLQTLCDVGLGYIklGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 430 SGGQRQRISLARALySDRS----IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVI 498
Cdd:cd03271 171 SGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
950-1150 |
1.61e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.94 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 950 PLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----VELSGGCIKIDGIRISdigLADLRSKL-AIIPQEPvlfs 1024
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA---PCALRGRKiATIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1025 gtvRSNLDPFNQYtedqiwdaleRTHMKECI---------AQLPLKLESEVMENGD--------NFSVGERQLLCIARAL 1087
Cdd:PRK10418 89 ---RSAFNPLHTM----------HTHARETClalgkpaddATLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1088 LRHCKILILDEATaamdTETDLLIQETIREAFADCT------MLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:PRK10418 156 LCEAPFIIADEPT----TDLDVVAQARILDLLESIVqkralgMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
320-516 |
1.72e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYN-IDLEIEEGKLVGICGSVGSGKTSLV------------SAILGQMTLLE-GSIAVSGTFAYVAQQawiLNA---- 381
Cdd:PRK10575 24 RTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLkmlgrhqppsegEILLDAQPLESwSSKAFARKVAYLPQQ---LPAaegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLRDNIL------------FGKEfDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSI 449
Cdd:PRK10575 101 TVRELVAigrypwhgalgrFGAA-DREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 450 YILDDPLSALD-AHvgnHIFNSAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:PRK10575 169 LLLDEPTSALDiAH---QVDVLALVHRLSQErglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
935-1169 |
1.77e-07 |
|
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: 53.50 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 935 EVTFENAEMRYrENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADlrSKLA 1014
Cdd:cd03296 2 SIEVRNVSKRF-GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1015 IIPQEPVLFSG-TVRSNL-----------DPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1082
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1083 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1159
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|
gi 1720387222 1160 NDSSRFYAMF 1169
Cdd:cd03296 227 HPASPFVYSF 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
319-487 |
1.81e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT------------FAYVAQQAWI-LNATLRD 385
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGHRSGInPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGKEFDEEryNSVLNSCCLRPDLAILpnsdlteIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 465
Cdd:PRK13540 94 NCLYDIHFSPG--AVGITELCRLFSLEHL-------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 1720387222 466 HIFNSAIRKRLKSKTVLFVTHQ 487
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
956-1149 |
1.94e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--IRISDIGLAdLRSKLAIIP----QEPVLFSGTVRS 1029
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDA-IRAGIMLCPedrkAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NLD--------PFNQYTeDQIWdalERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLRHCKILILDE 1098
Cdd:PRK11288 351 NINisarrhhlRAGCLI-NNRW---EAENADRFIRSLNIKtpsREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1099 ATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
313-514 |
1.95e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.84 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 313 TGSLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-FAYVAQ---------QAWIL--N 380
Cdd:PRK11607 26 TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPyqrpinmmfQSYALfpH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 381 ATLRDNILFGKEFDEERYNSVLNSCClrpdlAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 460 DahvgnhifnSAIRKRLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK11607 181 D---------KKLRDRMQLEvvdilervgvTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-503 |
2.02e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQQAWILNA-TLR 384
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGKE----------FDEERYNSVLNSCCLRPDLAILPNsdlteigERGANLSGGQRQRISLARALYSDRSIYILDD 454
Cdd:PRK09700 99 ENLYIGRHltkkvcgvniIDWREMRVRAAMMLLRVGLKVDLD-------EKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 455 PLSALDAHVGNHIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEG 503
Cdd:PRK09700 172 PTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
305-512 |
2.22e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.53 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 305 EEEGKQIhtgslrlqrtLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQM--TLLEGSIAVSGTFayvaqqawILNAT 382
Cdd:cd03217 9 SVGGKEI----------LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--------ITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFG--KEFDE-ERYNSVLNSCCLRpdlailpnsdltEIGErgaNLSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:cd03217 71 PEERARLGifLAFQYpPEIPGVKNADFLR------------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 460 DAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYL--VDCDEVIFMKEGCITERGTHE 512
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGDKE 190
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
656-867 |
2.38e-07 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 53.95 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 656 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 735
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 736 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLLILFsllhIVSRVLIRELKRLDNITQSPFlSHITSSIQ----GLATIHAY 810
Cdd:cd18541 121 LVDALFLGVLVLVMMFTISPKLtLIALLPLPLLA----LLVYRLGKKIHKRFRKVQEAF-SDLSDRVQesfsGIRVIKAF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 811 NKRQEFLHRYQELLDDNQApfflftcamRWLA-VRLD---LISIALITTTGLMIVL-------MHGQI 867
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVE---------KNLRlARVDalfFPLIGLLIGLSFLIVLwyggrlvIRGTI 254
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
934-1175 |
2.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 934 GEVTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSlgmalfrLVELSGGCIkidgirISDIG----- 1005
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKST-------MIQLTNGLI------ISETGqtivg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1006 -------------LADLRSKLAIIPQEP--VLFSGTVRSNL--DPFNQYTEDQiwDALERTHMKECIAQLPlklESEVME 1068
Cdd:PRK13645 72 dyaipanlkkikeVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKKVPELLKLVQLP---EDYVKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1069 NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT--ETDL--LIQETIREAFADCTMLTiaHRLHTVLG-SDRIMVL 1143
Cdd:PRK13645 147 SPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDFinLFERLNKEYKKRIIMVT--HNMDQVLRiADEVIVM 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720387222 1144 AQGQVVEFDTPSVLLSN---------DSSRFYAMFAAAENK 1175
Cdd:PRK13645 225 HEGKVISIGSPFEIFSNqelltkieiDPPKLYQLMYKLKNK 265
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
953-1168 |
3.25e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmaLFRLVEL--SGGCIKIDGIRISDIGLADL---RSKLAiiPQEPVLFsgtv 1027
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTL---LARMAGLlpGSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 rsNLDPFnQY---------TEDQIWDALERthmkecIAQLpLKLESEVMENGDNFSVGERQ-------LLCIARALLRHC 1091
Cdd:PRK03695 83 --AMPVF-QYltlhqpdktRTEAVASALNE------VAEA-LGLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1092 KILILDEATAAMD----TETDLLIQETIREAFAdctMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTP-SVLLSNDSSRF 1165
Cdd:PRK03695 153 QLLLLDEPMNSLDvaqqAALDRLLSELCQQGIA---VVMSSHDLnHTLRHADRVWLLKQGKLLASGRRdEVLTPENLAQV 229
|
...
gi 1720387222 1166 YAM 1168
Cdd:PRK03695 230 FGV 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
320-549 |
3.81e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQQAWIL-NATLR 384
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFG---KEFDEERYNSVLN--SCCLRPDLAilpnsdlteigerGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 460 DAHVGNHIFnSAIRKrLKSKTV--LFVTHQLQYLVD-CDEVIFMKEGCITergtheelmnLNGDYATIFNNLLLGETPPV 536
Cdd:PRK15439 172 TPAETERLF-SRIRE-LLAQGVgiVFISHKLPEIRQlADRISVMRDGTIA----------LSGKTADLSTDDIIQAITPA 239
|
250
....*....|...
gi 1720387222 537 EINskKEATGSQK 549
Cdd:PRK15439 240 ARE--KSLSASQK 250
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
953-1150 |
4.09e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDG-------IRIS-DIGLADLRSKLAII 1016
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKV-----LSGvyphgsyeGEILFDGevcrfkdIRDSeALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1017 PQEPV---LFSGTVRSNLDPFNqytedqiWDALERtHMKECIAQLPLKlesevmENGD----NFSVGERQLLCIARALLR 1089
Cdd:NF040905 91 PYLSIaenIFLGNERAKRGVID-------WNETNR-RARELLAKVGLD------ESPDtlvtDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 1090 HCKILILDEATAAMDtETD---LLiqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:NF040905 157 DVKLLILDEPTAALN-EEDsaaLL--DLLLELKAqGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
324-497 |
5.10e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFA--YVAQQAWI--------L--NATLRDNIL 388
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvRIRspRDAIALGIgmvhqhfmLvpNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 FGKEfdeerynsvlNSCCLRPDLAILpNSDLTEIGER-G---------ANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:COG3845 103 LGLE----------PTKGGRLDRKAA-RARIRELSERyGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720387222 459 LDAHVGNHIFnsAIRKRLKS--KTVLFVTHQLqylvdcDEV 497
Cdd:COG3845 172 LTPQEADELF--EILRRLAAegKSIIFITHKL------REV 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
951-1160 |
5.39e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.30 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 951 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISdiGLadlrsklaiiPQEPVLFSGTVRS- 1029
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GL----------PGHQIARMGVVRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 -NLDPFNQYTedqiwdALE------RTHMKECIAQLPLKL------ESEVMENG-----------------DNFSVGERQ 1079
Cdd:PRK11300 87 qHVRLFREMT------VIEnllvaqHQQLKTGLFSGLLKTpafrraESEALDRAatwlervgllehanrqaGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1080 LLCIARALLRHCKILILDEATAAMD-TETDLLiQETI---REAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1154
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNpKETKEL-DELIaelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTP 238
|
....*.
gi 1720387222 1155 SVLLSN 1160
Cdd:PRK11300 239 EEIRNN 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
322-514 |
6.53e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------------TFAYVAQQAWILNAT 382
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDNILFG-KEF----DEERYNSV--LNSCCLRPDLailpnsdlteIGERGANLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:PRK13641 103 VLKDVEFGpKNFgfseDEAKEKALkwLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 456 LSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
325-514 |
7.71e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAvsgtfayvaqqaWiLNATLRDniLFGKEFDEER------Y 398
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA------------W-LGKDLLG--MKDDEWRAVRsdiqmiF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 399 NSVLNSccLRPDLAI-----------LPNSDLTEIGERGANL------------------SGGQRQRISLARALYSDRSI 449
Cdd:PRK15079 105 QDPLAS--LNPRMTIgeiiaeplrtyHPKLSRQEVKDRVKAMmlkvgllpnlinryphefSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 450 YILDDPLSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 514
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVN--LLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
319-498 |
8.25e-07 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.49 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSL----------------VSA----ILGQM-----TLLEG-SIAVS------ 366
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAyarqFLGQMdkpdvDSIEGlSPAIAidqktt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 367 -----GTFAYVAQqawiLNATLRdnILFGKEFDEERYNSvlnscclrpdlailpnsdLTEIG------ERGAN-LSGGQR 434
Cdd:cd03270 88 srnprSTVGTVTE----IYDYLR--LLFARVGIRERLGF------------------LVDVGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 435 QRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVI 498
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
947-1130 |
9.05e-07 |
|
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: 53.21 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 947 ENLPLV-------LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGirisdigladlRSKLAIIPQE 1019
Cdd:TIGR00954 455 ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1020 PVLFSGTVRsnldpfnqyteDQIW--DALERTHMK-------ECIAQLpLKLESEVMENG---------DNFSVGERQLL 1081
Cdd:TIGR00954 524 PYMTLGTLR-----------DQIIypDSSEDMKRRglsdkdlEQILDN-VQLTHILEREGgwsavqdwmDVLSGGEKQRI 591
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 1082 CIARALLRHCKILILDEATAAMDTETDLLIQETIREafADCTMLTIAHR 1130
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
319-498 |
9.19e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTF--AYVAQQAWiLNATLRDNIlfgkefdeE 396
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLY-LDTTLPLTV--------N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 397 RYNSvlnsccLRPDLA---ILPNSDLTE----IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD--AHVGNHI 467
Cdd:PRK09544 88 RFLR------LRPGTKkedILPALKRVQaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQVALYD 161
|
170 180 190
....*....|....*....|....*....|...
gi 1720387222 468 FNSAIRKRLKSkTVLFVTHQLqYLV--DCDEVI 498
Cdd:PRK09544 162 LIDQLRRELDC-AVLMVSHDL-HLVmaKTDEVL 192
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
324-515 |
9.90e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT----FAY--VAQQAWIL--NATLRDNILFGKEFDE 395
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhYASkeVARRIGLLaqNATTPGDITVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 396 ERY-NSVLNSCCLRPD----LAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD-AHVGNHIF 468
Cdd:PRK10253 105 GRYpHQPLFTRWRKEDeeavTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720387222 469 NSAIRKRLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELM 515
Cdd:PRK10253 185 LLSELNREKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
952-1107 |
1.14e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKI-DGIRISDIGLADLRS--KLAIIPQEPVL-FSGTV 1027
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTL--------------LRImAGVDKDFNGEARPQPgiKVGYLPQEPQLdPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1028 RSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSVG 1076
Cdd:TIGR03719 86 RENveegvaeikdaLDRFNEisakYAEpDADFDKLaaEQAELQEIIDAADAwDLDSQLeiaMDalrcpPWDadvtKLSGG 165
|
170 180 190
....*....|....*....|....*....|.
gi 1720387222 1077 ERQLLCIARALLRHCKILILDEATAAMDTET 1107
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
322-528 |
1.14e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWiLNATLR--DNI--------LFGK 391
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSG-LNGQLTgiENIelkglmmgLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 392 EFDEerynsvlnscclrpdlaILPNS-DLTEIG----ERGANLSGGQRQRISLARALYSDRSIYILDDPLSaldahVGNH 466
Cdd:PRK13545 119 KIKE-----------------IIPEIiEFADIGkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 467 IFNSAIRKRL-----KSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNL 528
Cdd:PRK13545 177 TFTKKCLDKMnefkeQGKTIFFISHSLsQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQM 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
303-503 |
1.22e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 303 PEEEEGKQIH---TGSLRLqrtlYNIDLeIEEGKLVGICGSVGSGKTSLVSAILGQMT---------------------- 357
Cdd:PRK13409 72 PEELEEEPVHrygVNGFKL----YGLPI-PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyeeepswdevlkrfrgt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 358 --------LLEGSIAVSGTFAYVAQQAWILNATLRDnILfgKEFDE----ERYNSVLNscclrpdlailpnsdLTEIGER 425
Cdd:PRK13409 147 elqnyfkkLYNGEIKVVHKPQYVDLIPKVFKGKVRE-LL--KKVDErgklDEVVERLG---------------LENILDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 426 G-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDahVGNHIfNSA--IRKRLKSKTVLFVTHQ---LQYLVDCDEVIF 499
Cdd:PRK13409 209 DiSELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRL-NVArlIRELAEGKYVLVVEHDlavLDYLADNVHIAY 285
|
....
gi 1720387222 500 MKEG 503
Cdd:PRK13409 286 GEPG 289
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
956-1150 |
1.25e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIkidGIRISDIGLADL------------RSKLAIIPQEP--- 1020
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYRMRDGQLRDLyalseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1021 ----VLFSGTVRSNLDPF--NQYTE--DQIWDALERTHMKEC-IAQLPlklesevmengDNFSVGERQLLCIARALLRHC 1091
Cdd:PRK11701 102 lrmqVSAGGNIGERLMAVgaRHYGDirATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1092 KILILDEATAAMDTET-----DLLiQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVE 1150
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVqarllDLL-RGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-497 |
1.44e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSL---VSAILGQMTLlEGSIAVSG---TFAYV--AQQAWIL----------NA 381
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTY-EGEIIFEGeelQASNIrdTERAGIAiihqelalvkEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 382 TLRDNILFGKE---FDEERYNSVLNSC--CLRP-DLAILPNsdlTEIGergaNLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:PRK13549 98 SVLENIFLGNEitpGGIMDYDAMYLRAqkLLAQlKLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720387222 456 LSALDAHVGNHIFNsaIRKRLKSKTV--LFVTHQLqylvdcDEV 497
Cdd:PRK13549 171 TASLTESETAVLLD--IIRDLKAHGIacIYISHKL------NEV 206
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
685-865 |
1.71e-06 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 50.95 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 685 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILvffcvgMIAGVFpwFLVAVGPL 764
Cdd:cd18575 66 RVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLL------LIGGLV--MLFITSPK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 765 LILFSLLhIVSRVLI------RELKRLDNITQSPFL---SHITSSIQGLATIHAYNKRQEFLHRYQELLDDNqapfflFT 835
Cdd:cd18575 138 LTLLVLL-VIPLVVLpiilfgRRVRRLSRASQDRLAdlsAFAEETLSAIKTVQAFTREDAERQRFATAVEAA------FA 210
|
170 180 190
....*....|....*....|....*....|.
gi 1720387222 836 CAMRWLAVRLDLISIA-LITTTGLMIVLMHG 865
Cdd:cd18575 211 AALRRIRARALLTALViFLVFGAIVFVLWLG 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
932-1149 |
1.82e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 932 QEGEVTFENAEMRYReNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDiglADLRS 1011
Cdd:PRK15056 3 QQAGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1012 KLAIIPQE-------PVLFSGTVRSN-------LDPFNQYTEDQIWDALERTHMkeciaqlplkLESEVMENGDnFSVGE 1077
Cdd:PRK15056 79 LVAYVPQSeevdwsfPVLVEDVVMMGryghmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1078 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVV 1149
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
659-826 |
1.88e-06 |
|
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: 50.97 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 659 SIYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmDEVDVRlpfqaE 734
Cdd:cd18555 42 NVLGIGILILFLLYGlfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN---SNVYIR-----Q 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 735 MFIQNVI--------LVFFCVGMIagVFPWFL----VAVGPLLILFSLLhivSRVLIRELKRLDNITQSPFLSHITSSIQ 802
Cdd:cd18555 114 ILSNQVIsliidlllLVIYLIYML--YYSPLLtlivLLLGLLIVLLLLL---TRKKIKKLNQEEIVAQTKVQSYLTETLY 188
|
170 180
....*....|....*....|....
gi 1720387222 803 GLATIHAYNKRQEFLHRYQELLDD 826
Cdd:cd18555 189 GIETIKSLGSEKNIYKKWENLFKK 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-520 |
1.92e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGTFAYVAQQAWILNA---------------TLR 384
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqelhlvpemTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGK------EFDEERYNSVLNSCCLRPDLAILPNSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSA 458
Cdd:PRK11288 98 ENLYLGQlphkggIVNRRLLNYEAREQLEHLGVDIDPDTPL-------KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 459 LDAHVGNHIFnSAIRK-RLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITErgTHEELMNLNGD 520
Cdd:PRK11288 171 LSAREIEQLF-RVIRElRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDMAQVDRD 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-514 |
2.25e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.61 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAI-----LGQMTLLEGSIAVSGTFAY--------VAQQAWIL--------NATL 383
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpieVRREVGMVfqypnpfpHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNILFG----------KEFDEeRYNSVLNSCCLRPDLAilpnsdlTEIGERGANLSGGQRQRISLARALYSDRSIYILD 453
Cdd:PRK14267 103 YDNVAIGvklnglvkskKELDE-RVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387222 454 DPLSALDAhVGNHIFNSAIRKRLKSKTVLFVTHQ-LQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK14267 175 EPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
952-1150 |
2.48e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDI---GLADLRSK--------LAIIP--- 1017
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1018 -QEPVLFSGTVRSNLDpfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1096
Cdd:PRK10584 105 aLENVELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1097 DEATAAMDTET-----DLLIQETIREAfadCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1150
Cdd:PRK10584 171 DEPTGNLDRQTgdkiaDLLFSLNREHG---TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
324-499 |
2.63e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAI-----LGQMTLLEGSIAVSGTFAY---------------VAQQAWILNATL 383
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYapdvdpvevrrrigmVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNILFGK-------EFDE--ERynsvlnscCLRPdlAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDD 454
Cdd:PRK14243 108 YDNIAYGAringykgDMDElvER--------SLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 455 PLSALDAhvgnhIFNSAIR---KRLKSK-TVLFVTHQLQ------------------------YLVDCD--EVIF 499
Cdd:PRK14243 178 PCSALDP-----ISTLRIEelmHELKEQyTIIIVTHNMQqaarvsdmtaffnveltegggrygYLVEFDrtEKIF 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
952-1161 |
2.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEP--VLFSGTVRS 1029
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1030 NL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1102
Cdd:PRK13652 99 DIafGPINlgldeETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387222 1103 MDTETdllIQETIR--EAFADCTMLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSND 1161
Cdd:PRK13652 168 LDPQG---VKELIDflNDLPETYGMTVIFSTHQLdlvpEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
952-1117 |
2.83e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVEL-SGGCIKIDG------IRISDIGLADLRSKLAIIPQE----P 1020
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMpRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1021 VLfsgTVRSNL--DPFN------QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCK 1092
Cdd:PRK11124 96 HL---TVQQNLieAPCRvlglskDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|....*
gi 1720387222 1093 ILILDEATAAMDTETDLLIQETIRE 1117
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
953-1148 |
2.95e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISD-IGLADLRSKLAIIPQEPVlfSGTVRSNL 1031
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhNANEAINHGFALVTEERR--STGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 D-PFN-------QYTEDqiWDALERTHMKE----CIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:PRK10982 342 DiGFNslisnirNYKNK--VGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIG-SLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1100 TAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1148
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
324-516 |
3.33e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.64 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQQAWIL-NATLRDNIL 388
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFrKLTVEDNIL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 389 -------FGKEFDEERYNSVLNscclrpDLailpnsDLTEIGE-RGANLSGGQRQRISLARALYSDRSIYILD------D 454
Cdd:COG1137 101 avlelrkLSKKEREERLEELLE------EF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDepfagvD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 455 PLSALDahvgnhifnsaIRK---RLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 516
Cdd:COG1137 169 PIAVAD-----------IQKiirHLKERgiGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
666-906 |
3.71e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 50.17 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 666 AVMLILKAIRGVVFV-------KGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdVRLPFQAEMFIQ 738
Cdd:cd18543 43 LLLLALGVAEAVLSFlrrylagRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 739 NVILVFFCVGMIAGVFPWF-LVAVGPLLILFsllhIVSRVLIRELKRLDNITQS---PFLSHITSSIQGLATIHAYNKRQ 814
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLaLVALASLPPLV----LVARRFRRRYFPASRRAQDqagDLATVVEESVTGIRVVKAFGRER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 815 EFLHRYQELLDDnqapffLFTCAMRwlAVRLDLISIALITT---TGLMIVL-------MHGQIpSAYAGLA-ISYAVQLT 883
Cdd:cd18543 198 RELDRFEAAARR------LRATRLR--AARLRARFWPLLEAlpeLGLAAVLalggwlvANGSL-TLGTLVAfSAYLTMLV 268
|
250 260
....*....|....*....|...
gi 1720387222 884 GLFQFTVRLASETEARFTSVERI 906
Cdd:cd18543 269 WPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1074-1147 |
4.75e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 4.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1074 SVGERQLLCIARALLRHCKILILDEATAAM-DTETDLLIQeTIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1147
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR-VIRELKSqGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
968-1152 |
5.60e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 968 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISD----IGLADLRSKLAIIPQEPVLFSG-TVRSNL----DPFNQYT 1038
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgICLPPEKRRIGYVFQDARLFPHyKVRGNLrygmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1039 EDQIWDALERTHMkecIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDT--ETDLL--IQET 1114
Cdd:PRK11144 109 FDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprKRELLpyLERL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720387222 1115 IREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1152
Cdd:PRK11144 175 ARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
429-514 |
5.79e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN-SAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 506
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
....*...
gi 1720387222 507 ERGTHEEL 514
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
332-503 |
5.83e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 332 GKLVGICGSVGSGKTSLVSAILGQMT--LLEGSIAVSG------TFAYVA---QQAWILN--ATLRDNILFG------KE 392
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqeTFARISgycEQNDIHSpqVTVRESLIYSaflrlpKE 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 393 FDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNhIFNSAI 472
Cdd:PLN03140 986 VSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA-IVMRTV 1062
|
170 180 190
....*....|....*....|....*....|....
gi 1720387222 473 RKRLKS-KTVLFVTHQ--LQYLVDCDEVIFMKEG 503
Cdd:PLN03140 1063 RNTVDTgRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
955-1166 |
6.27e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 955 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRIsDIGLADLRSKLAIIPQEPVLFSGTVRSNLDPF 1034
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1035 NQYTEDQIWD--ALERTHMKECIAqlplkLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQ 1112
Cdd:TIGR01257 1027 YAQLKGRSWEeaQLEMEAMLEDTG-----LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 1113 ETIREAFADCTMLTIAHRLHT--VLGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFY 1166
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEadLLG-DRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
320-503 |
6.56e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 320 RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQQA-WILNATLR 384
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNILFGkefdeeRYNS----VLNSCCLRPDLAILPNSDL-TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:PRK10982 92 DNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIdIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720387222 460 DAHVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEG 503
Cdd:PRK10982 166 TEKEVNHLFT--IIRKLKERgcGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
310-514 |
6.58e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 310 QIHTGSLRLQRTL-YNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQM----TLLEGSIAVSGTFAYVAQQAWILNATLR 384
Cdd:PRK10418 6 ELRNIALQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKIATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 385 DNilfgkefDEERYNSVLN-------SCCLR---PDLAILPNSdLTEIG----ERGANL-----SGGQRQRISLARALYS 445
Cdd:PRK10418 86 QN-------PRSAFNPLHTmhthareTCLALgkpADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 446 DRSIYILDDPLSALDAHVGNHIFN---SAIRKRlkSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 514
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDlleSIVQKR--ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
325-507 |
6.92e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGtfAYVAQQAW-----ILNATLRDNILF-------GKE 392
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPedyrkLFSAVFTDFHLFdqllgpeGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 393 FDEERYNSVLNSCCLrpdlailpNSDLTEIGERGAN--LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNS 470
Cdd:PRK10522 420 ANPALVEKWLERLKM--------AHKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720387222 471 AIRKRLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 507
Cdd:PRK10522 491 VLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
317-488 |
7.12e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 317 RLQRTLYnidleieEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-----TFAYVAQ------QAWIL--NATL 383
Cdd:TIGR01257 948 RLNITFY-------ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQslgmcpQHNILfhHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNILF-----GKEFDEERYNSVlnscclrpdlAILPNSDLT-EIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 457
Cdd:TIGR01257 1021 AEHILFyaqlkGRSWEEAQLEME----------AMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190
....*....|....*....|....*....|.
gi 1720387222 458 ALDAHVGNHIFNSAIRKRlKSKTVLFVTHQL 488
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHM 1120
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
675-826 |
7.13e-06 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 49.26 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 675 RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILvffCVGMIAgvf 754
Cdd:cd18590 56 RGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK---TLGMLG--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 755 pwFLVAVGPLLILFSLLHIVSRVLI--------RELKR--LDNITQSPFLshITSSIQGLATIHAYNKRQEFLHRYQELL 824
Cdd:cd18590 130 --FMLSLSWQLTLLTLIEMPLTAIAqkvyntyhQKLSQavQDSIAKAGEL--AREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
..
gi 1720387222 825 DD 826
Cdd:cd18590 206 ER 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
319-503 |
7.80e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 319 QRTLYN-IDLEIEEGKLVGICGSVGSGKTSLVSAILG--QMTLLEGSIAVSG---------TFAYVAQQAWIL-NATLRD 385
Cdd:PLN03211 80 ERTILNgVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNrkptkqilkRTGFVTQDDILYpHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILF------GKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720387222 460 DAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLV--DCDEVIFMKEG 503
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEG 283
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
316-514 |
8.10e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 316 LRLQ----RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSaILGQMTLLEGSIAVSGTFAYVAQQAW-------------- 377
Cdd:PRK14247 9 LKVSfgqvEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrrvqmv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 378 ------ILNATLRDNILFGKEFD---------EERYNSVLNSCCLRPDLAilpnsdlTEIGERGANLSGGQRQRISLARA 442
Cdd:PRK14247 88 fqipnpIPNLSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 443 LYSDRSIYILDDPLSALDAHvgnhifNSAIRKRL-----KSKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPE------NTAKIESLflelkKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
956-1152 |
9.37e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 956 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAD-LRSKLAIIPQEP----VLFSGTVRSN 1030
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 -----LDPFNqYTEDQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1105
Cdd:PRK10762 351 msltaLRYFS-RAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1106 ETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1152
Cdd:PRK10762 429 GAKKEIYQLINQFKAEgLSIILVSSEMPEVLGmSDRILVMHEGRISgEFT 478
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
674-785 |
9.94e-06 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 48.85 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 674 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF-FCVGMIag 752
Cdd:cd18784 55 IRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIgVIVFMF-- 132
|
90 100 110
....*....|....*....|....*....|...
gi 1720387222 753 VFPWFLVAVgpLLILFSLLHIVSRVLIRELKRL 785
Cdd:cd18784 133 KLSWQLSLV--TLIGLPLIAIVSKVYGDYYKKL 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
324-506 |
1.14e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT--------------FAYVAQ----QAWILNATLRD 385
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDMSVAE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 386 NILFGkEFDEERYNS--VLNSCCLRpDLA--------ILPNSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILDDP 455
Cdd:COG3845 356 NLILG-RYRRPPFSRggFLDRKAIR-AFAeelieefdVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 456 LSALDahVGNhIfnSAIRKRL-----KSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 506
Cdd:COG3845 430 TRGLD--VGA-I--EFIHQRLlelrdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
430-514 |
1.22e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 430 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI----------FNSAIrkrlksktvLFVTHQLQYLVD-CDEVI 498
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQImtllnelkreFNTAI---------IMITHDLGVVAGiCDKVL 233
|
90
....*....|....*.
gi 1720387222 499 FMKEGCITERGTHEEL 514
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
429-516 |
1.42e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITE 507
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*....
gi 1720387222 508 RGTHEELMN 516
Cdd:PRK14271 243 EGPTEQLFS 251
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
429-516 |
1.46e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGC 504
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL--QLLRELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
90
....*....|..
gi 1720387222 505 ITERGTHEELMN 516
Cdd:PRK15134 235 CVEQNRAATLFS 246
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
952-1107 |
1.59e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV-----ELSGGCIKIDGIRIsdigladlrsklAIIPQEPVL-FSG 1025
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMagvdkEFEGEARPAPGIKV------------GYLPQEPQLdPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 TVRSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFS 1074
Cdd:PRK11819 86 TVRENveegvaevkaaLDRFNEiyaaYAEpDADFDALaaEQGELQEIIDAADAwDLDSQLeiaMDalrcpPWDakvtKLS 165
|
170 180 190
....*....|....*....|....*....|...
gi 1720387222 1075 VGERQLLCIARALLRHCKILILDEATAAMDTET 1107
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
957-1106 |
1.65e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 957 SFTIKPKEKIGIVGRTGSGKSSlgmaLFRLveLSG------GCIKIDGIRISDIGlADLRSKLAIIPQ----EPVLfsgT 1026
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTS----LLRI--LAGlarpdaGEVLWQGEPIRRQR-DEYHQDLLYLGHqpgiKTEL---T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1027 VRSNLDpFNQ-----YTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATA 1101
Cdd:PRK13538 91 ALENLR-FYQrlhgpGDDEALWEALAQVGLAG-FEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
....*
gi 1720387222 1102 AMDTE 1106
Cdd:PRK13538 159 AIDKQ 163
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
654-826 |
1.68e-05 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 48.43 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 654 MQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQA 733
Cdd:cd18558 58 MTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 734 EMFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLLILFSLL--HIVSRVLIRELKRLDNITQSPflshiTSSIQGLA 805
Cdd:cd18558 138 GVIFQNIATFGtgFIIGFIRG---WkltlVILAISPVLGLSAVVwaKILSGFTDKEKKAYAKAGAVA-----EEVLEAFR 209
|
170 180
....*....|....*....|.
gi 1720387222 806 TIHAYNKRQEFLHRYQELLDD 826
Cdd:cd18558 210 TVIAFGGQQKEETRYAQNLEI 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
328-493 |
1.92e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 328 EIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-TFAYVAQQAwilnatlrdnilfgkefdeerynsvlnscc 406
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 407 lrpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLK--SKTVLFV 484
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEegKKTALVV 128
|
170
....*....|..
gi 1720387222 485 THQL---QYLVD 493
Cdd:cd03222 129 EHDLavlDYLSD 140
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
951-1156 |
2.08e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 951 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLR-SKLAIIPQEP-----VLfS 1024
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrglVP-D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1025 GTVRSNLDpFNQYTEDQI-------WDALeRTHMKECIAQLPLK---LESEVmengDNFSVGERQLLCIARALLRHCKIL 1094
Cdd:COG3845 351 MSVAENLI-LGRYRRPPFsrggfldRKAI-RAFAEELIEEFDVRtpgPDTPA----RSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1095 I-------LDEATAAMdtetdllIQETIREAfAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFDTPSV 1156
Cdd:COG3845 425 IaaqptrgLDVGAIEF-------IHQRLLEL-RDagAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEA 489
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
662-863 |
2.20e-05 |
|
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: 47.58 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 662 ALSMAVML--ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFsKDMDEVDVRLPFQAEMFIQN 739
Cdd:cd18566 47 GVVIAILLesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 740 VILVFFCVGMIAgVFPWFLVAV----GPLLILFS-LLHIVSRVLIRELKRLDNITQspflSHITSSIQGLATIHAYNKRQ 814
Cdd:cd18566 126 LPFVLIFLGLIW-YLGGKLVLVplvlLGLFVLVAiLLGPILRRALKERSRADERRQ----NFLIETLTGIHTIKAMAMEP 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 815 EFLHRYQELLDDnqapfflftCAMRWLAVRlDLISIALITTTGLMIVLM 863
Cdd:cd18566 201 QMLRRYERLQAN---------AAYAGFKVA-KINAVAQTLGQLFSQVSM 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
324-517 |
2.54e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 324 NIDLEIEEGKLVGICGSVGSGKTSLVSAILGQ--------MTLLEG--------SIAVSGTFAYVA----QQAWILNATL 383
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnisgTVFKDGkevdvstvSDAIDAGLAYVTedrkGYGLNLIDDI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNI----LFG----------KEFDE-ERYnsvlnscclRPDLAILPNSDLTEIGergaNLSGGQRQRISLARALYSDRS 448
Cdd:NF040905 358 KRNItlanLGKvsrrgvidenEEIKVaEEY---------RKKMNIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 449 IYILDDPLSALDahVGN--HIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEELMNL 517
Cdd:NF040905 425 VLILDEPTRGID--VGAkyEIY--TIINELAAegKGVIVISSELPELLGmCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
322-514 |
2.72e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-TFAYVAQQawILNATLRDNILFGKEFDEERYNS 400
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYDKKS--LLEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 401 VLNSCCLRPDLAILPNSD--------LTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 466
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEvekrvkeaLKAVGMEGfenkppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 467 IFNSAIRKRLKSKTVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
312-462 |
2.89e-05 |
|
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: 46.66 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 312 HTGSLRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVS---------------------GTFA 370
Cdd:COG4778 18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 371 YVAQqawILNATLRDNIL-----------FGKEFDEERYNSVLNSCCLRPDLAILPNsdlteigergANLSGGQRQRISL 439
Cdd:COG4778 97 YVSQ---FLRVIPRVSALdvvaepllergVDREEARARARELLARLNLPERLWDLPP----------ATFSGGEQQRVNI 163
|
170 180
....*....|....*....|...
gi 1720387222 440 ARALYSDRSIYILDDPLSALDAH 462
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAA 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
310-460 |
3.08e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 310 QIHTGSLRLQ--RTLYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSgtFAYVA-----QQAWILNAT 382
Cdd:PRK10938 5 QISQGTFRLSdtKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--FSHITrlsfeQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 383 LRDN---IL------FGKEFDEERYNSVL-NSCCLRpdLA-ILPNSDLteIGERGANLSGGQRQRISLARALYSDRSIYI 451
Cdd:PRK10938 83 WQRNntdMLspgeddTGRTTAEIIQDEVKdPARCEQ--LAqQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
....*....
gi 1720387222 452 LDDPLSALD 460
Cdd:PRK10938 159 LDEPFDGLD 167
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
916-1148 |
3.25e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.98 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 916 EAPARIKNKAPphdwpqegeVTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcik 995
Cdd:PRK11247 2 MNTARLNQGTP---------LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 996 idGIRISDIGLADLRSKLAIIPQEPVLF-------------SGTVRsnldpfnqyteDQIWDALERTHMKECIAQLPLKL 1062
Cdd:PRK11247 68 --ELLAGTAPLAEAREDTRLMFQDARLLpwkkvidnvglglKGQWR-----------DAALQALAAVGLADRANEWPAAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1063 esevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI-----REAFadcTMLTIAHRL-HTVLG 1136
Cdd:PRK11247 135 -----------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVsEAVAM 200
|
250
....*....|..
gi 1720387222 1137 SDRIMVLAQGQV 1148
Cdd:PRK11247 201 ADRVLLIEEGKI 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
322-514 |
4.29e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.72 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG-------------TFAYVAQQA--WILNATLRDN 386
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFGK---EFDEE----RYNSVLNSCCLRPDLAILPNsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:PRK13652 100 IAFGPinlGLDEEtvahRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 460 DAHVGNHI--FNSAIRKRLkSKTVLFVTHQLQYLVDCDEVIF-MKEGCITERGTHEEL 514
Cdd:PRK13652 169 DPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1071-1169 |
4.40e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.02 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1071 DNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE---AFaDCTMLTIAHRLHTVLG-SDRIMVLAQG 1146
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqQF-NITSLYVTHDQSEAFAvSDTVIVMNKG 213
|
90 100
....*....|....*....|...
gi 1720387222 1147 QVVEFDTPSVLLSNDSSRFYAMF 1169
Cdd:PRK11432 214 KIMQIGSPQELYRQPASRFMASF 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
303-493 |
4.70e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 303 PEEEEGKQIH---TGSLRLqrtlYNIDlEIEEGKLVGICGSVGSGKTSLVSAILGQMT---------------------- 357
Cdd:COG1245 72 PEELEEDPVHrygENGFRL----YGLP-VPKKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 358 --------LLEGSIAVSGTFAYVAQQAWILNATLRDnILfgKEFDE----ERYNSVLNscclrpdlailpnsdLTEIGER 425
Cdd:COG1245 147 elqdyfkkLANGEIKVAHKPQYVDLIPKVFKGTVRE-LL--EKVDErgklDELAEKLG---------------LENILDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 426 G-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDahvgnhifnsaIRKRLKS-----------KTVLFVTHQ---LQY 490
Cdd:COG1245 209 DiSELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-----------IYQRLNVarlirelaeegKYVLVVEHDlaiLDY 277
|
...
gi 1720387222 491 LVD 493
Cdd:COG1245 278 LAD 280
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
424-521 |
4.76e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 424 ERGAN-LSGGQRQRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFM 500
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100 110
....*....|....*....|....*....|.
gi 1720387222 501 KE------GCITERGTHEELMN----LNGDY 521
Cdd:TIGR00630 563 GPgagehgGEVVASGTPEEILAnpdsLTGQY 593
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
330-493 |
5.66e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.21 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 330 EEGKLVGICGSVGSGKTSLVSAILGQMT------------------------------LLEGSIAVSGTFAYVAQQAWIL 379
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKpnlgkfddppdwdeildefrgselqnyftkLLEGDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 380 NATLRDNIlfgKEFDEeryNSVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSAL 459
Cdd:cd03236 104 KGKVGELL---KKKDE---RGKLDELVDQLELRHVLDRNIDQ-------LSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720387222 460 DahVGNHIfNSA--IRKRLK-SKTVLFVTHQ---LQYLVD 493
Cdd:cd03236 171 D--IKQRL-NAArlIRELAEdDNYVLVVEHDlavLDYLSD 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
954-1150 |
6.08e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 954 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRIS--------DIGLA---------------DLR 1010
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKGMAyitesrrdngffpnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1011 SKLAIIPQepvLFSGTVRSNLDPFNQYTEDQIWDAlERthmkeciAQLPLKLESeVMENGDNFSVGERQLLCIARALLRH 1090
Cdd:PRK09700 360 QNMAISRS---LKDGGYKGAMGLFHEVDEQRTAEN-QR-------ELLALKCHS-VNQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387222 1091 CKILILDEATAAMDTETDLLIQETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1150
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADdgKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
952-1104 |
8.42e-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: 44.79 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSGGCIKIDG-IRISDIGLADLRSKLAiipqEPVLFSG----- 1025
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTL----LRI--LAGLSPPLAGrVLLNGGPLDFQRDSIA----RGLLYLGhapgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1026 ----TVRSNLDPFNQY-TEDQIWDALERTHMK----ECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILIL 1096
Cdd:cd03231 85 kttlSVLENLRFWHADhSDEQVEEALARVGLNgfedRPVAQL---------------SAGQQRRVALARLLLSGRPLWIL 149
|
....*...
gi 1720387222 1097 DEATAAMD 1104
Cdd:cd03231 150 DEPTTALD 157
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
662-822 |
9.31e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 45.97 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 662 ALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpFQAEMFI 737
Cdd:cd18564 57 AAALVGIALLRGLasyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD---LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 738 QNVILVFFCVGMIAGVF--PWFL----VAVGPLLILFSLLHivSRvLIRELKRldniTQSPFLSHITS----SIQGLATI 807
Cdd:cd18564 134 PLLTNLLTLVGMLGVMFwlDWQLaliaLAVAPLLLLAARRF--SR-RIKEASR----EQRRREGALASvaqeSLSAIRVV 206
|
170
....*....|....*
gi 1720387222 808 HAYNKRQEFLHRYQE 822
Cdd:cd18564 207 QAFGREEHEERRFAR 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
953-1152 |
1.28e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.46 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKI-DGIrisdigladlrsklaIIPQepvlfSGTVRSN- 1030
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT--------------IKMlTGI---------------LVPT-----SGEVRVLg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LDPFNQYTE--DQI-----------WD--ALERTHMKECIAQLP-------LKLESEVMENGD-------NFSVGERQLL 1081
Cdd:COG4586 84 YVPFKRRKEfaRRIgvvfgqrsqlwWDlpAIDSFRLLKAIYRIPdaeykkrLDELVELLDLGElldtpvrQLSLGQRMRC 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387222 1082 CIARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHRLHTV--LgSDRIMVLAQGQVVeFD 1152
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGL----DVVSKEAIREFLKEynrergTTILLTSHDMDDIeaL-CDRVIVIDHGRII-YD 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
952-1107 |
1.41e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.56 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDgirisdigladlrsklaiIPQEPVlfsGTVRSNL 1031
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQF---GREASLI 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 1032 DPFnqYTEDQIWDALERTHM-KECIAQLPLKLESEvmengdnFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1107
Cdd:COG2401 104 DAI--GRKGDFKDAVELLNAvGLSDAVLWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
962-1154 |
1.59e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 962 PKEKIGIVGRTGSGKSSLGMALFR-LVELSGGCIKIDGIRISDIGLADLRSKLaiipqepvlfsgtvrsnldpfnqyted 1040
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1041 qiwdalerthmkeciaqlplkleseVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR---- 1116
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720387222 1117 ---EAFADCTMLTIAHRLHTVLgsDRIMVLAQGQVVEFDTP 1154
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
322-503 |
1.63e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQmtlLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEfdEERYNSV 401
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSE--EDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 402 LN-------SCCLRPDLAIlpnsdlteigeRGanLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSaIR- 473
Cdd:cd03233 98 LTvretldfALRCKGNEFV-----------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-IRt 163
|
170 180 190
....*....|....*....|....*....|...
gi 1720387222 474 --KRLKSKTVLFVTHQLQYLVDC-DEVIFMKEG 503
Cdd:cd03233 164 maDVLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
952-1168 |
1.69e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADLRSKLAIIPQEPVLFSGTVRSNL 1031
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1032 DPFNQYTEDQI---W-----DALERTHMKECIAQLPLklesevmENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1103
Cdd:PRK10253 102 VARGRYPHQPLftrWrkedeEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 1104 DT--ETDL--LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND-SSRFYAM 1168
Cdd:PRK10253 175 DIshQIDLleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAElIERIYGL 243
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
322-514 |
1.75e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.84 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 322 LYNIDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSGT-FAYVAQQawILNatLRDNI-LFGKEFDEERYN 399
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKG--LMK--LRESVgMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 400 -SVLNSCCLRPDLAILPNSDLTEIGERGAN--------------LSGGQRQRISLARALYSDRSIYILDDPLSALDAhVG 464
Cdd:PRK13636 98 aSVYQDVSFGAVNLKLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-MG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 465 nhifNSAIRKRLKSK------TVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 514
Cdd:PRK13636 177 ----VSEIMKLLVEMqkelglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
952-1176 |
1.77e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.07 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLADlrSKLAIIPQEPVLFSG-TVRSN 1030
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1031 LD-----------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEA 1099
Cdd:PRK10851 95 IAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1100 TAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENKV 1176
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRL 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
953-1149 |
2.27e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.10 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 953 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRISDIGLAD---LRSKLAIIPQEP-VLFSGTVR 1028
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLD-PF---NQYTED---QIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1101
Cdd:PRK10908 98 DNVAiPLiiaGASGDDirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720387222 1102 AMDTEtdllIQETIREAFAD-----CTMLTIAHRLHTVLGSD-RIMVLAQGQVV 1149
Cdd:PRK10908 167 NLDDA----LSEGILRLFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
690-888 |
2.27e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 44.45 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 690 LHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNViLVFFCVGMIAGVFPWFLVAVG----PLL 765
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNV-LTLVGVAIILFSINPKLALLTlipiPFL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 766 ILFSLLH-IVSRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYNKRQEFLHRYQELLDDnqapffLFTCAMRw 840
Cdd:cd18778 154 ALGAWLYsKKVRPRYRKVRE--------ALGELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720387222 841 lAVRLDLI---SIALITTTGLMIVLMHGqipsayAGLAISYAVQLTGLFQF 888
Cdd:cd18778 219 -AMKLWAIfhpLMEFLTSLGTVLVLGFG------GRLVLAGELTIGDLVAF 262
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
422-514 |
2.82e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 422 IGERGANLSGGQRQRISLARALY---SDRSIYILDDPLSALDAHVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVDCDE 496
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLE--VLQRLVDKgnTVVVIEHNLDVIKTADY 900
|
90 100
....*....|....*....|....
gi 1720387222 497 VIFM------KEGCITERGTHEEL 514
Cdd:TIGR00630 901 IIDLgpeggdGGGTVVASGTPEEV 924
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
325-513 |
4.40e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 325 IDLEIEEGKLVGICGSVGSGKTSLVSAILGQMTLLEGSIAVSG---TFAYVA---------------QQAWILNATLRDN 386
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpiDIRSPRdairagimlcpedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 387 ILFGKefdeeRYNSVLNSCCLRP------------DLAILPNSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILDD 454
Cdd:PRK11288 352 INISA-----RRHHLRAGCLINNrweaenadrfirSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387222 455 PLSALDahVG------NHIFNSAIRKRlkskTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEE 513
Cdd:PRK11288 423 PTRGID--VGakheiyNVIYELAAQGV----AVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
936-1104 |
4.45e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.58 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 936 VTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGIRIS------DIgl 1006
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1007 ADLRSKLAIIPQ--EPVLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVG 1076
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALvgisESLFEKNPFEL-----------SGG 149
|
170 180
....*....|....*....|....*...
gi 1720387222 1077 ERQLLCIARALLRHCKILILDEATAAMD 1104
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
430-488 |
4.94e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 4.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 430 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQL 488
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDM 524
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
673-826 |
5.10e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 43.39 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 673 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDM----DEVDVRLpfqaEMFIQNVILVFFCVG 748
Cdd:cd18780 60 FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTqvlqNAVTVNL----SMLLRYLVQIIGGLV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 749 MIaGVFPWFLVAVgpLLILFSLLHIVSRVLIRELKRLDNITQSPfLSHITS----SIQGLATIHAYNKRQEFLHRYQELL 824
Cdd:cd18780 136 FM-FTTSWKLTLV--MLSVVPPLSIGAVIYGKYVRKLSKKFQDA-LAAASTvaeeSISNIRTVRSFAKETKEVSRYSEKI 211
|
..
gi 1720387222 825 DD 826
Cdd:cd18780 212 NE 213
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
685-725 |
5.24e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 43.30 E-value: 5.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1720387222 685 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV 725
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEF 112
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
952-1151 |
6.34e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 952 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG--GCIKIDGIRISDiglaDLRSKLAIIPQEPVLFSG-TVR 1028
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1029 SNLDPFNQYTEDQIWDALERTHMKE-CIAQLPL-KLESEVMENG--DNFSVGERQLLCIARALLRHCKILILDEATAAMD 1104
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAEsVISELGLtKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1105 TETDL-LIQetireafadcTMLTIAHRLHTVLGS------------DRIMVLAQGQVVEF 1151
Cdd:PLN03211 239 ATAAYrLVL----------TLGSLAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFF 288
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
945-1161 |
7.02e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.15 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 945 YRENLPLVLK---KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI-----------KIDGIRISDIGLA--- 1007
Cdd:PRK13651 12 FNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKEKVLEKLViqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1008 ----------DLRSKLAIIPQ--EPVLFSGTVRSNL--DPFNQYTEDQiwDALERThmKECIAQLPLKlESEVMENGDNF 1073
Cdd:PRK13651 92 trfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRA--AKYIELVGLD-ESYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1074 SVGERQLLCIARALLRHCKILILDEATAAMD---TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1149
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGK--TIILVTHDLDNVLEwTKRTIFFKDGKII 244
|
250
....*....|...
gi 1720387222 1150 -EFDTPSVLLSND 1161
Cdd:PRK13651 245 kDGDTYDILSDNK 257
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
926-1149 |
1.09e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 926 PPHDwPQEGEVTFE-------NAEMRYRenlpLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALF-----RLVelsGGC 993
Cdd:NF040905 247 PERT-PKIGEVVFEvknwtvyHPLHPER----KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 994 IKIDG--IRISDI------GLA----DlRSKLAIIPQEPVLFSgTVRSNLDPF------NQYTEDQIwdALE-RTHMKec 1054
Cdd:NF040905 319 VFKDGkeVDVSTVsdaidaGLAyvteD-RKGYGLNLIDDIKRN-ITLANLGKVsrrgviDENEEIKV--AEEyRKKMN-- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 1055 iaqlpLKLESeVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHT 1133
Cdd:NF040905 393 -----IKTPS-VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVISSELPE 466
|
250
....*....|....*..
gi 1720387222 1134 VLG-SDRIMVLAQGQVV 1149
Cdd:NF040905 467 LLGmCDRIYVMNEGRIT 483
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
407-498 |
1.92e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 407 LRPDLAILPNSDLTEIG-ERG-ANLSGGQRQRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVL 482
Cdd:PRK00635 453 LKSRLSILIDLGLPYLTpERAlATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVL 532
|
90
....*....|....*.
gi 1720387222 483 FVTHQLQYLVDCDEVI 498
Cdd:PRK00635 533 LVEHDEQMISLADRII 548
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
384-514 |
1.94e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 384 RDNI-LFGKEFDEERYNSVLnscclRPDlAILPNSDLTEI-GERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 461
Cdd:NF000106 104 RENLyMIGR*LDLSRKDARA-----RAD-ELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387222 462 HVGNHIFNSAIRKRLKSKTVLFVThqlQYLVDCD----EVIFMKEGCITERGTHEEL 514
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTT---QYMEEAEqlahELTVIDRGRVIADGKVDEL 231
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
662-829 |
2.50e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 41.32 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 662 ALSMAVMLILKAIRGVVFVKGTLRASSR-LHD---ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemFI 737
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERlLYDlrlRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSE--------LL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 738 QN-----VILVFFCVGMIAGVF----PWFLVA--VGPLLILFSLL-HIVSRVLIRELKrlDNITQSpfLSHITSSIQGLA 805
Cdd:cd18546 114 QTglvqlVVSLLTLVGIAVVLLvldpRLALVAlaALPPLALATRWfRRRSSRAYRRAR--ERIAAV--NADLQETLAGIR 189
|
170 180
....*....|....*....|....
gi 1720387222 806 TIHAYNKRQEFLHRYQELLDDNQA 829
Cdd:cd18546 190 VVQAFRRERRNAERFAELSDDYRD 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
14-210 |
2.89e-03 |
|
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: 41.00 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 14 EKSLGELINICSNDgqrmfeAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLG---SAVFILFYPAMMFVSRltaYFRRK 90
Cdd:cd07346 92 RNRTGDLMSRLTSD------VDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNwklTLVALLLLPLYVLILR---YFRRR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 91 CVAATDDRVQKM-------NEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFS 163
Cdd:cd07346 163 IRKASREVRESLaelsaflQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720387222 164 V--HMTLGFHLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 210
Cdd:cd07346 243 YggYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
429-518 |
3.24e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYS---DRSIYILDDPLSAL---DAHVGNHIFNSAIRkrlKSKTVLFVTHQLQYLVDCDEVIFM-- 500
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTH---QGHTVVIIEHNMHVVKVADYVLELgp 886
|
90 100
....*....|....*....|..
gi 1720387222 501 ----KEGCITERGTHEELMNLN 518
Cdd:PRK00635 887 eggnLGGYLLASCSPEELIHLH 908
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
669-824 |
4.37e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 40.62 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 669 LILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDmDEVDVRLPFQAEMFIQNVILVFFCVG 748
Cdd:cd18568 56 ILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLG 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 749 MIAgVFPWFL--VAVGpLLILFSLLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELL 824
Cdd:cd18568 135 LMF-YYNLQLtlIVLA-FIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKF 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
395-462 |
5.78e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 5.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387222 395 EERYNSVLNSCCLRPDLAIlpnsdlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 462
Cdd:PLN03073 321 EARAASILAGLSFTPEMQV----------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
429-514 |
5.98e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.11 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387222 429 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 506
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElQQKENMALVLITHDLALVAEaAHKIIVMYAGQVV 233
|
....*...
gi 1720387222 507 ERGTHEEL 514
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
966-985 |
9.72e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 39.75 E-value: 9.72e-03
|
| |
