|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-1357 |
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: 813.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 3 SSNVKSKPNPREKANLLSVLFWWWTIDLFKTGYKKVLQIDDLYNPLKNDRSNLLGDRLEKRWNNELENSKRYK------- 75
Cdd:TIGR00957 194 ETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPvsavygk 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 76 -----------------------------RRPSLLRAIFRAFLWEYVVLGLMQILNEFVIRLGtPILLGGLLRYFRKSTD 126
Cdd:TIGR00957 274 kdpskpkgssqldaneevealivksphkpRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIG-PQILSLLIRFVNDPMA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 127 ETYEtALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVYRKALRLSKTALGETAPGKVVNLVANDVNRFDLV 206
Cdd:TIGR00957 353 PDWQ-GYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 207 SIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKM 286
Cdd:TIGR00957 432 ATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 287 YAWEKSFCALIETARKLELRVVKKSSYIRGIyMTFNLFTTrmALFCTLISMLLF-----GNELSADKVFVFSSYFNILAH 361
Cdd:TIGR00957 512 YAWELAFLDKVEGIRQEELKVLKKSAYLHAV-GTFTWVCT--PFLVALITFAVYvtvdeNNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 362 TMTgMFVRGFAEIAECLVAVRRLQHFLMYEEFqentfalnkfaasvngsinnDSKQASNKTSKPDipyideetstyenld 441
Cdd:TIGR00957 589 PLN-ILPMVISSIVQASVSLKRLRIFLSHEEL--------------------EPDSIERRTIKPG--------------- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 442 dsekrkhnglvvvasdllqktanlmeekkrsssirineEPYAVKMTNFTAKWEPGQSEnTLDNLNLEIEKGKIYAVIGMV 521
Cdd:TIGR00957 633 --------------------------------------EGNSITVHNATFTWARDLPP-TLNGITFSIPEGALVAVVGQV 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 522 GAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGSTVRQNILFGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTV 601
Cdd:TIGR00957 674 GCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 602 VGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEECI--QRYLAGKTRILATHQLQYVKNVDAIIL 679
Cdd:TIGR00957 754 IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIV 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 680 IEQGKATVFSHYQDLLSQRPEYAELLAAENETHDDSSLEKS-----------------------VMRRQFSSSSTRSrtp 736
Cdd:TIGR00957 834 MSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSwtalvsgegkeakliengmlvtdVVGKQLQRQLSAS--- 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 737 dASSGGTDDEEEDEDAE------KLNDG----LEGTSRGTVKGPIFIKYFQtGANLCLAVTLLLFFICTQFMASLNDYFV 806
Cdd:TIGR00957 911 -SSDSGDQSRHHGSSAElqkaeaKEETWklmeADKAQTGQVELSVYWDYMK-AIGLFITFLSIFLFVCNHVSALASNYWL 988
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 807 ------PILVSKEETRTYLLqqtalnatnetstenldisSMYNYMYIYTAIVVGLFCIGITRSltfyevCIVCSQKLHDM 880
Cdd:TIGR00957 989 slwtddPMVNGTQNNTSLRL-------------------SVYGALGILQGFAVFGYSMAVSIG------GIQASRVLHQD 1043
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 881 AFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPkavldagQICMMMFGSL--AVS-CIV----NPLFLIPIVFLGT 953
Cdd:TIGR00957 1044 LLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIP-------PVIKMFMGSLfnVIGaLIVillaTPIAAVIIPPLGL 1116
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 954 VFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLD 1033
Cdd:TIGR00957 1117 LYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLE 1196
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1034 ifcFVFTSLVTFSFLLL---EQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYTnippepnlrdrgK 1110
Cdd:TIGR00957 1197 ---CVGNCIVLFAALFAvisRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYS------------E 1261
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1111 FAKKSEKQIALPAnAPKNWPKDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFR-LAKVE 1189
Cdd:TIGR00957 1262 TEKEAPWQIQETA-PPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRiNESAE 1340
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1190 GVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGS 1269
Cdd:TIGR00957 1341 GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1270 NYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEY 1349
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
....*...
gi 383847295 1350 DHPHMLLQ 1357
Cdd:TIGR00957 1501 GAPSNLLQ 1508
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-1393 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 771.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 12 PREKANLLSVLFWWWTIDLFKTGYKKVLQIDDLYNPLKNDRSNLLGDRLEKRWNNELENSKrykrrPSLLRAIFRAFLWE 91
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPK-----PWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 92 YVVLGLMQILNEFVIRLGtPILLGGLLRYFRKstDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSV 171
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVG-PLLLNLLLESMQN--GEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 172 VYRKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQ-- 249
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQtf 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 250 --SYTGKLSsKFRLQtaiKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRgiymTFNLFT-T 326
Cdd:PLN03130 460 iiSKMQKLT-KEGLQ---RTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLS----AFNSFIlN 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 327 RMALFCTLISM---LLFGNELSADKVFVFSSYFNILAHTMTgMFVRGFAEIAECLVAVRRLQHFLMYEEfqentfalnkf 403
Cdd:PLN03130 532 SIPVLVTVVSFgvfTLLGGDLTPARAFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLLAEE----------- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 404 aasvngsinndSKQASNKTSKPDIPYIdeetstyenlddsekrkhnglvvvasdllqktanlmeekkrsssirineepyA 483
Cdd:PLN03130 600 -----------RVLLPNPPLEPGLPAI----------------------------------------------------S 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTakWEPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVE-GHVKVNGSLSYAGQEAWVFGST 562
Cdd:PLN03130 617 IKNGYFS--WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNAT 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTH 642
Cdd:PLN03130 695 VRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 643 VSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELLaaENEthddSSLEKSVM 722
Cdd:PLN03130 775 VGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM--ENA----GKMEEYVE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 723 RRQFSSSSTRSRTPDASSGGTDDEEEDEDAEKLNDGL------EGTSRGTVKGPIFIKYFQTGANLCLAVTLLLFFICTQ 796
Cdd:PLN03130 849 ENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKsvlikqEERETGVVSWKVLERYKNALGGAWVVMILFLCYVLTE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 797 fmaslndyfvpilVSKEETRTYLLqqtalNATNETSTEnlDISSMYnYMYIYTAIVVGLFCIGITRSLTFYEVCIVCSQK 876
Cdd:PLN03130 929 -------------VFRVSSSTWLS-----EWTDQGTPK--THGPLF-YNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKR 987
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 877 LHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDE-LLPKAVLDAGQIcMMMFGSLAVSCIVNPLFLIPIVFLGTVF 955
Cdd:PLN03130 988 LHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRnVAVFVNMFLGQI-FQLLSTFVLIGIVSTISLWAIMPLLVLF 1066
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 956 YWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYcaqdilkKEFDKLQDVHTST----VYMYVVSSSG---F 1028
Cdd:PLN03130 1067 YGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAY-------KAYDRMAEINGRSmdnnIRFTLVNMSSnrwL 1139
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1029 GFSLDIFCFVFTSLvTFSFLLLE-------QSFSGgEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYTNIPP 1101
Cdd:PLN03130 1140 AIRLETLGGLMIWL-TASFAVMQngraenqAAFAS-TMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPS 1217
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1102 EPNLrdrgkfakksekqIALPANAPKNWPKDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISA 1181
Cdd:PLN03130 1218 EAPL-------------VIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNA 1284
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1182 LFRLAKVE-GVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGL 1260
Cdd:PLN03130 1285 LFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGL 1364
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1261 ESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLV 1340
Cdd:PLN03130 1365 DAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILV 1444
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 1341 MDKGRMAEYDHPHMLLQNTYSQFTSLVKETDRAMFDQLVRIAKQSYIAKHGER 1393
Cdd:PLN03130 1445 LDAGRVVEFDTPENLLSNEGSAFSKMVQSTGAANAQYLRSLVFGGDEDRLARE 1497
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-1370 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 729.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 12 PREKANLLSVLFWWWTIDLFKTGYKKVLQIDDLYNPLKNDRSNLLGDRLEKRWnneLENSKRYKrrPSLLRAIFRAFLWE 91
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCW---TEESRRPK--PWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 92 YVVLGLMQI---LNEFVirlgTPILLGGLLRYFRKStDETYeTALWYAAGICIATAINVITLNQAIFGAFHVGARIRVAT 168
Cdd:PLN03232 303 FWLGGIFKIghdLSQFV----GPVILSHLLQSMQEG-DPAW-VGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 169 CSVVYRKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPI 248
Cdd:PLN03232 377 VAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 249 QSYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIrgiyMTFNLFT-TR 327
Cdd:PLN03232 457 QTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLL----SAFNSFIlNS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 328 MALFCTLISM---LLFGNELSADKVFVFSSYFNILAHTMTgMFVRGFAEIAECLVAVRRLQHFLMYEEfqentfalnkfa 404
Cdd:PLN03232 533 IPVVVTLVSFgvfVLLGGDLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE------------ 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 405 asvngsinndSKQASNKTSKPDIPYIdeetstyenlddsekrkhnglvvvasdllqktanlmeekkrsssirineepyAV 484
Cdd:PLN03232 600 ----------RILAQNPPLQPGAPAI----------------------------------------------------SI 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 485 KMTNFTakWEPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVE-GHVKVNGSLSYAGQEAWVFGSTV 563
Cdd:PLN03232 618 KNGYFS--WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATV 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RQNILFGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHV 643
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 644 SKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELLaaENETHDDSSLEKSVMR 723
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM--ENAGKMDATQEVNTND 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 724 RQFSSSSTRSRTpDASSGGTDDEEEDEDAEKLNDGLEGTSRGTVKGPIFIKYFQTGANLCLAVTLLLFFICTQFMASLND 803
Cdd:PLN03232 854 ENILKLGPTVTI-DVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSS 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 804 YFVPILvskeetrtyllqqtalnaTNETSTENLdiSSMYnYMYIYTAIVVGLFCIGITRSLTFYEVCIVCSQKLHDMAFS 883
Cdd:PLN03232 933 TWLSIW------------------TDQSTPKSY--SPGF-YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 884 ALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNPLFLIPIVFLGTVFYWIRKVYL 963
Cdd:PLN03232 992 SILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQ 1071
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 964 KTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLv 1043
Cdd:PLN03232 1072 STSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWL- 1150
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1044 TFSFLLLEQSFSGGEVGLA------ITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYTNIPPEPNLRDRGKfakksek 1117
Cdd:PLN03232 1151 TATFAVLRNGNAENQAGFAstmgllLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENN------- 1223
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1118 qialpaNAPKNWPKDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDD 1196
Cdd:PLN03232 1224 ------RPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDD 1297
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1197 IDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQR 1276
Cdd:PLN03232 1298 CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQR 1377
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLL 1356
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
1370
....*....|....
gi 383847295 1357 QNTYSQFTSLVKET 1370
Cdd:PLN03232 1458 SRDTSAFFRMVHST 1471
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-1373 |
0e+00 |
|
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: 713.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 11 NPREKANLLSVLFWWWTIDLFKTGYKKVLQIDDLYNPLKNDRSNLLGDRLEKRWNNELENSKRykrRPSLLRAIFRAFLW 90
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKK---NPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 91 EYVVLGLMQILNEFViRLGTPILLGGLLRYFRKSTDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCS 170
Cdd:TIGR01271 81 RFVFYGILLYFGEAT-KAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 171 VVYRKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQS 250
Cdd:TIGR01271 160 LIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 251 YTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMAL 330
Cdd:TIGR01271 240 CLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 331 FCTLISMLLFgNELSADKVFVFSSYFNILAHTMTGMFVRGFAEIAECLVAVRRLQHFLMYEEFQentfalnkfaasvngs 410
Cdd:TIGR01271 320 FLSVVPYALI-KGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYK---------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 411 inndskqasnktskpdipyideeTSTYeNLDDSEKRkhngLVVVASDLLQKTANLMEEKKRSSSIR-INEEPYAVKMTNF 489
Cdd:TIGR01271 383 -----------------------TLEY-NLTTTEVE----MVNVTASWDEGIGELFEKIKQNNKARkQPNGDDGLFFSNF 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 490 TAKWEPgqsenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGSTVRQNILF 569
Cdd:TIGR01271 435 SLYVTP-----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIF 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 GQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFE 649
Cdd:TIGR01271 510 GLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 650 ECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELLAAeNETHDDSSLEK--SVMRRQFS 727
Cdd:TIGR01271 590 SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLG-LEAFDNFSAERrnSILTETLR 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 728 SSSTRSRTPDASSGGTDDEEEDEDAEKLND-------------------------------------------------- 757
Cdd:TIGR01271 669 RVSIDGDSTVFSGPETIKQSFKQPPPEFAEkrkqsiilnpiasarkfsfvqmgpqkaqattiedavrepserkfslvped 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 758 --GLEGTSRGTV-----------------------KGP------------------------------------------ 770
Cdd:TIGR01271 749 eqGEESLPRGNQyhhglqhqaqrrqsvlqlmthsnRGEnrreqlqtsfrkkssitqqnelaseldiysrrlskdsvyeis 828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 771 --------------------------IFIKYFQTGANLCLAVTLLLFFICTQFMASLNDYFvpiLVSKEETRTYLLQQTA 824
Cdd:TIGR01271 829 eeineedlkecfaderenvfetttwnTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLW---LITDNPSAPNYVDQQH 905
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 825 LNATNETSTENLDIS--SMYNYMYIYTAIVVGLFCIGITRSLTFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRIL 902
Cdd:TIGR01271 906 ANASSPDVQKPVIITptSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRIL 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 903 NRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNPLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFT 982
Cdd:TIGR01271 986 NRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFS 1065
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 983 HLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLVTFSFLLLEQSfSGGEVGLA 1062
Cdd:TIGR01271 1066 HLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQD-GEGEVGII 1144
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1063 ITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYTNIPPE-PNLRDRGKFAKKSEKQIALPANAPKNWPKDGMIRFRNVY 1141
Cdd:TIGR01271 1145 LTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEePRPSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLT 1224
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1142 MRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLF 1221
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIF 1304
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1222 SGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANV 1301
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1302 DPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLqNTYSQFTSLVKETDRA 1373
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSAADRL 1455
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
76-1367 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 698.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 76 RRPSLLRAIFRAfLWEYVvlgLMQILNEFVIRLGTpILLGGLLRYFRKSTDE---TYETALWYAAGICIATAINVITLNQ 152
Cdd:PTZ00243 230 KRLSLLRTLFAA-LPYYV---WWQIPFKLLSDVCT-LTLPVLLKYFVKFLDAdnaTWGRGLGLVLTLFLTQLIQSVCLHR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 153 AIFGAFHVGARIRVATCSVVYRKALRLSKTALG--ETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTE 230
Cdd:PTZ00243 305 FYYISIRCGLQYRSALNALIFEKCFTISSKSLAqpDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 231 AGYAGLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKK 310
Cdd:PTZ00243 385 VGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRD 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 311 SSYIRGIYMTFNLFTTRMALFCTLISMLLFGNELSADKVFVFSSYFNILAHTMTgMFVRGFAEIAECLVAVRRLQHFLM- 389
Cdd:PTZ00243 465 VQLARVATSFVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFF-MIPWVFTTVLQFLVSIKRISTFLEc 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 390 -------------YEEFQENTFALNKFAASvngsINNDSKQASNKTSKPDIPYIdeETSTYE--------NLDDSEKRKH 448
Cdd:PTZ00243 544 dnatcstvqdmeeYWREQREHSTACQLAAV----LENVDVTAFVPVKLPRAPKV--KTSLLSralrmlccEQCRPTKRHP 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 449 NGLVVV-----------ASDLLQKTANLMEEKKrSSSIRINEEPYAVKMTNFtaKWEPgqsENTLDNLNLEIEKGKIYAV 517
Cdd:PTZ00243 618 SPSVVVedtdygspssaSRHIVEGGTGGGHEAT-PTSERSAKTPKMKTDDFF--ELEP---KVLLRDVSVSVPRGKLTVV 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 518 IGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGSTVRQNILFGQPYDRHRYQKVVKACSLLRDFKQFPQS 597
Cdd:PTZ00243 692 LGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGG 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 598 DQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAI 677
Cdd:PTZ00243 772 LETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYV 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 678 ILIEQGKATVFSHYQDLLsQRPEYAELLA--AENETHDDSSLEKSVMRRQFSSSSTRSRTPDASSGGTDDEEEDEDAEKL 755
Cdd:PTZ00243 852 VALGDGRVEFSGSSADFM-RTSLYATLAAelKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDA 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 756 NDG----LEGTSRGTVKGPIFIKYFQTGANLCLAVTLLLFFICTQFMASLNDYFVPILvskeetrtyllqqtalnatnet 831
Cdd:PTZ00243 931 AAGrlmtREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW---------------------- 988
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 832 STENLDISSMyNYMYIYTAIVV-GLFCIGITRSLTFYEVCIVCSqKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMG 910
Cdd:PTZ00243 989 STRSFKLSAA-TYLYVYLGIVLlGTFSVPLRFFLSYEAMRRGSR-NMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDID 1066
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 911 TIDELLPKAVLDAGQICMMMFGSLAVSCIVNPLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNG 990
Cdd:PTZ00243 1067 ILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQG 1146
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 991 LTTIRAY-CAQDILKKEFDKLQDVHtSTVYMYVVSSSGFGFSLDIFCFVFTSLVTF----SFLLLEQSFSGGEVGLAITQ 1065
Cdd:PTZ00243 1147 SATITAYgKAHLVMQEALRRLDVVY-SCSYLENVANRWLGVRVEFLSNIVVTVIALigviGTMLRATSQEIGLVSLSLTM 1225
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1066 VMAMTGMIQWGMRQNAEAANQMMAVERVLEYT-NIPPE--PNLRDRGKFAKKSEKQIA--------LPANAPKNWP---K 1131
Cdd:PTZ00243 1226 AMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEdmPELDEEVDALERRTGMAAdvtgtvviEPASPTSAAPhpvQ 1305
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1132 DGMIRFRNVYMRYaEEELP-VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRR 1209
Cdd:PTZ00243 1306 AGSLVFEGVQMRY-REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRR 1384
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1210 HISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNN 1289
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1290 K--ILMlDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQNTYSQFTSLV 1367
Cdd:PTZ00243 1465 SgfILM-DEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1133-1352 |
2.61e-126 |
|
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: 389.93 E-value: 2.61e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHI 1211
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKI 1291
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1292 LMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHP 1352
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
781-1097 |
4.41e-107 |
|
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: 341.61 E-value: 4.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 781 NLCLAVTLLLFFICTQFMASLNDYFVPILVSKEETRTYLLQQTALNATNETSTENLDIssmYNYMYIYTAIVVGLFCIGI 860
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDR---DFNLGIYAGLTAATFVFGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 861 TRSLTFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIV 940
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 941 NPLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYM 1020
Cdd:cd18601 158 NPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1021 YVVSSSGFGFSLDIFCFVFTSLVTFSFLLLEQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYT 1097
Cdd:cd18601 238 FLATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
849-1348 |
5.24e-105 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 346.00 E-value: 5.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 849 TAIVVGLFCIGITRSLTFYeVCIVCSQKL-----HDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAV 920
Cdd:COG1132 61 LLLLLLLLGLALLRALLSY-LQRYLLARLaqrvvADLrrdLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 921 LDAGQICMMMFGSLAVSCIVNP----LFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMsrspVFTHLNATLNGLTTIRA 996
Cdd:COG1132 140 PQLVRSVVTLIGALVVLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 997 YCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLVTF--SFLLLEQSFSGGEVGLAITQVMAMTGMIQ 1074
Cdd:COG1132 216 FGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLvgGLLVLSGSLTVGDLVAFILYLLRLFGPLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1075 WGMRQNAEAANQMMAVERVLEYTNIPPEpnlrdrgkfakksekqIALPANAPKNWPKDGMIRFRNVYMRYAEEElPVLKG 1154
Cdd:COG1132 296 QLANVLNQLQRALASAERIFELLDEPPE----------------IPDPPGAVPLPPVRGEIEFENVSFSYPGDR-PVLKD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1155 LNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNL---D 1230
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1231 PfnEFSDAALWEVLEEVELKDavVISG--NGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDAL 1308
Cdd:COG1132 439 P--DATDEEVEEAAKAAQAHE--FIEAlpDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 383847295 1309 IQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:COG1132 515 IQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
484-684 |
6.64e-103 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 325.58 E-value: 6.64e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQSEN--TLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGS 561
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILFGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 642 HVSKHLFEECIQRYLA-GKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:cd03250 161 HVGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
94-384 |
5.46e-99 |
|
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: 318.28 E-value: 5.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 94 VLGLMQILnEFVIRLGTPILLGGLLRYFRKSTDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVY 173
Cdd:cd18579 1 LAGLLKLL-EDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 174 RKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYTG 253
Cdd:cd18579 80 RKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 254 KLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMALFCT 333
Cdd:cd18579 160 KLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLAT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 383847295 334 LISMLLFGNELSADKVFVFSSYFNILaHTMTGMFVRGFAEIAECLVAVRRL 384
Cdd:cd18579 240 FATYVLLGNPLTAAKVFTALSLFNLL-RFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
782-1097 |
7.64e-99 |
|
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: 318.29 E-value: 7.64e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 782 LCLAVTLLLFFICTQFMASLNDYFVpilvskeetrtyllqqtalnatnETSTENLDISSMYNYMYIYTAIVVGLFCIGIT 861
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWS-----------------------SDWSSSPNSSSGYYLGVYAALLVLASVLLVLL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 862 RSLTFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVN 941
Cdd:cd18580 59 RWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 942 PLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMY 1021
Cdd:cd18580 139 PYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLL 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1022 VVSSSGFGFSLDIFCFVFTSLVTFSFLLLEQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYT 1097
Cdd:cd18580 219 LAVQRWLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
94-384 |
5.77e-98 |
|
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: 315.70 E-value: 5.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 94 VLGLMqILNEFVIRLGTPILLGGLLRYFRKSTDE-TYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVV 172
Cdd:cd18593 1 LLGIF-LFLEEAIRVVQPIFLGKLIRYFEGNGSSiSLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 173 YRKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYT 252
Cdd:cd18593 80 YRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 253 GKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMALFC 332
Cdd:cd18593 160 GKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 333 TLISMLLFGNELSADKVFVFSSYFNILAHTMTGMFVRGFAEIAECLVAVRRL 384
Cdd:cd18593 240 TFLAYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1129-1352 |
3.90e-95 |
|
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: 304.34 E-value: 3.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1129 WPKDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDL 1207
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLeevelkdavvisgnglesRVLDRGSNYSVGQRQLVCLARAILR 1287
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1288 NNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHP 1352
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
882-1348 |
1.22e-85 |
|
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: 295.59 E-value: 1.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 882 FSALIRTGMRFFDTNPSGRILNRFSkDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP-LFLIPIVFLG---TVFYW 957
Cdd:COG2274 236 FRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPpLALVVLLLIPlyvLLGLL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 958 IRKVYLKTSKNIKRLEGMSRSpvftHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGfSLDIFCF 1037
Cdd:COG2274 315 FQPRLRRLSREESEASAKRQS----LLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS-TLSGLLQ 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1038 VFTSLVTF---SFLLLEQSFSGGE---VGLAITQVMA-MTGMIQ-WGMRQNAEAAnqmmaVERVLEYTNIPPEPNLrdrg 1109
Cdd:COG2274 390 QLATVALLwlgAYLVIDGQLTLGQliaFNILSGRFLApVAQLIGlLQRFQDAKIA-----LERLDDILDLPPEREE---- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1110 kfakkSEKQIALPanapknwPKDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV- 1188
Cdd:COG2274 461 -----GRSKLSLP-------RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPt 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1189 EGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNL---DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVL 1265
Cdd:COG2274 529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1266 DRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGR 1345
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
...
gi 383847295 1346 MAE 1348
Cdd:COG2274 687 IVE 689
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
94-385 |
2.67e-84 |
|
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: 277.59 E-value: 2.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 94 VLGLMQILNEfVIRLGTPILLGGLLRYFRKSTDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVY 173
Cdd:cd18594 1 LLGILLFLEE-SLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 174 RKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYTG 253
Cdd:cd18594 80 KKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 254 KLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMALFCT 333
Cdd:cd18594 160 KLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFAT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 334 LISMLLFGNELSADKVFVFSSYFNILAHTMTgmfvRGFAE----IAECLVAVRRLQ 385
Cdd:cd18594 240 FVPYVLTGNTLTARKVFTVISLLNALRMTIT----RFFPEsiqtLSESRVSLKRIQ 291
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
875-1358 |
2.12e-71 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 250.06 E-value: 2.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 875 QKLHDMAFSALIRTGMRFFDTNPSGRILNRFskdMGTIDEL-------LPkavldagQICMMMFGSLAVSCIVNPL-FLI 946
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEALdgyfaryLP-------QLFLAALVPLLILVAVFPLdWLS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 947 PIVFLGT-----VFYWIrkVYLKTSK-NIKRLEGMSRspvfthLNA----TLNGLTTIRAYCAQDILKKEFDKL-QDVHT 1015
Cdd:COG4988 161 GLILLVTaplipLFMIL--VGKGAAKaSRRQWRALAR------LSGhfldRLRGLTTLKLFGRAKAEAERIAEAsEDFRK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1016 STvyMYV-----VSSsgfgFSLDIFCFVFTSLVTFSFLLleqSFSGGEVGLAItqvmAMTGMI--------------QWG 1076
Cdd:COG4988 233 RT--MKVlrvafLSS----AVLEFFASLSIALVAVYIGF---RLLGGSLTLFA----ALFVLLlapefflplrdlgsFYH 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1077 MRQNAEAANQmmAVERVLEytnippepnlrdrgkfakkSEKQIALPANAPKNWPKDGMIRFRNVYMRYAEEElPVLKGLN 1156
Cdd:COG4988 300 ARANGIAAAE--KIFALLD-------------------APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR-PALDGLS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1157 LVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLDPFN-E 1234
Cdd:COG4988 358 LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPySGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1235 FSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR 1314
Cdd:COG4988 438 ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALR 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 383847295 1315 RKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQN 1358
Cdd:COG4988 518 RLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1133-1357 |
2.57e-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: 232.50 E-value: 2.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRHI 1211
Cdd:cd03254 1 GEIEFENVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSGTLRRNLDPFNEFSDAALW-EVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQ 1357
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1133-1368 |
3.08e-69 |
|
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: 233.26 E-value: 3.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHI 1211
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKI 1291
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1292 LMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQNTYSQFTSLVK 1368
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
786-1097 |
2.50e-67 |
|
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: 229.28 E-value: 2.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 786 VTLLLFFICTQFMASLNDYFVpilvsKEETRTYllqQTALNATNEtstenlDISSMYnYMYIYTAIVVGLFCIGITRSLT 865
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWL-----GIWASAY---ETSSALPPS------EVSVLY-YLGIYALISLLSVLLGTLRYLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 866 FYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNPLFL 945
Cdd:cd18604 67 FFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 946 IPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSS 1025
Cdd:cd18604 147 LPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1026 SGFGFSLDIFCFVFTSLVTFsFLLLEQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYT 1097
Cdd:cd18604 227 RWLSVRIDLLGALFSFATAA-LLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
782-1097 |
1.79e-66 |
|
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: 227.45 E-value: 1.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 782 LCLAVTLLLFFICTQFMASLNDYFVpilvskeetrTYLLQQTALNATNETSTENLDISSMYN------YMYIYTAIVVGL 855
Cdd:cd18599 2 YVVFLFVLLLFILSVGSTVFSDWWL----------SYWLKQGSGNTTNNVDNSTVDSGNISDnpdlnfYQLVYGGSILVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 856 FCIGITRSLTFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLA 935
Cdd:cd18599 72 LLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 936 VSCIVNPLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHT 1015
Cdd:cd18599 152 IIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1016 STVYMYVVSSSGFGFSLDIFCFVFTSLVTFSFLLLEQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLE 1095
Cdd:cd18599 232 SAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILE 311
|
..
gi 383847295 1096 YT 1097
Cdd:cd18599 312 YI 313
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1135-1345 |
1.12e-65 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 219.56 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSGTLRRNLdpfnefsdaalwevleevelkdavvISGnglesrvldrgsnysvGQRQLVCLARAILRNNKILM 1293
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------LSG----------------GQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1294 LDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGR 1345
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
845-1366 |
1.17e-65 |
|
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: 233.50 E-value: 1.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 845 MYIYTAIV-VGLFciGITRSLTFY-EvcivcsqKL--HDMAFSALIRTGMRFFDT----NP-------SGRILNRFSKDM 909
Cdd:COG4987 52 LNLFVPIVgVRAF--AIGRTVFRYlE-------RLvsHDATLRLLADLRVRLYRRleplAPaglarlrSGDLLNRLVADV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 910 GTIDELLPKAVLDAGQICMMMFGSLAVSCIVNPLF----LIPIVFLGTVFYWI-RKVYLKTSKNIKRLEGMSRspvfTHL 984
Cdd:COG4987 123 DALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALalvlALGLLLAGLLLPLLaARLGRRAGRRLAAARAALR----ARL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 985 NATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMyVVSSSGFGFSLDIFCFVFTSLVTF---SFLLLEQSFSGGEVGL 1061
Cdd:COG4987 199 TDLLQGAAELAAYGALDRALARLDAAEARLAAAQRR-LARLSALAQALLQLAAGLAVVAVLwlaAPLVAAGALSGPLLAL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1062 AITQVMAMTGMIQwGMRQNAEAANQMM-AVERVLEYTNIPPEpnlrdrgkfakksekqIALPAnAPKNWPKDGMIRFRNV 1140
Cdd:COG4987 278 LVLAALALFEALA-PLPAAAQHLGRVRaAARRLNELLDAPPA----------------VTEPA-EPAPAPGGPSLELEDV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1141 YMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISIIPQDPV 1219
Cdd:COG4987 340 SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPqSGSITLGGVDLRDLDEDDLRRRIAVVPQRPH 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1220 LFSGTLRRNL---DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDE 1296
Cdd:COG4987 420 LFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDE 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1297 ATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQN--TYSQFTSL 1366
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQngRYRQLYQR 569
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
843-1097 |
1.93e-64 |
|
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: 220.81 E-value: 1.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 843 NYMYIYTAIVVGLFCIGITRSLTFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLD 922
Cdd:cd18606 36 FYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 923 AGQICMMMFGSLAVSCIVNPLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDI 1002
Cdd:cd18606 116 FLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1003 LKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLVTFSFLLLEQSFSGGEVGLAITQVMAMTGMIQWGMRQNAE 1082
Cdd:cd18606 196 FIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAE 275
|
250
....*....|....*
gi 383847295 1083 AANQMMAVERVLEYT 1097
Cdd:cd18606 276 VENNMNSVERLLHYA 290
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
502-719 |
2.47e-62 |
|
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: 214.34 E-value: 2.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGSTVRQNILFGQPYDRHRYQKV 581
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 582 VKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTR 661
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 662 ILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELLAAeNETHDDSSLEK 719
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMG-YDTFDQFSAER 269
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
93-384 |
2.69e-62 |
|
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: 214.64 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 93 VVLGLMQILNEFVirlgTPILLGGLLRYFRKSTDETyetalW----YAAGICIATAINVITLNQAIFGAFHVGARIRVAT 168
Cdd:cd18595 3 ALLKLLSDILLFA----SPQLLKLLINFVEDPDEPL-----WkgylYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 169 CSVVYRKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPI 248
Cdd:cd18595 74 TSAIYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 249 QSYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRM 328
Cdd:cd18595 154 NAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 329 ALFCTLISMLLFG--NELSADKVFVFSSYFNILAHTMTgMFVRGFAEIAECLVAVRRL 384
Cdd:cd18595 234 VSLATFATYVLSDpdNVLDAEKAFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
850-1360 |
1.13e-60 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 219.20 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 850 AIVVGLFCI-GITRSLTFYEVCIVCSQKLHDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMgtidELLPKAVLDA-- 923
Cdd:TIGR02203 58 LVVIGLAVLrGICSFVSTYLLSWVSNKVVRDIrvrMFEKLLGLPVSFFDRQPTGTLLSRITFDS----EQVASAATDAfi 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 924 ----------GQICMMMFGSLAVSCIVnpLFLIPIvfLGTVFYWIRKVYLKTSKNIKRLEGmsrsPVFTHLNATLNGLTT 993
Cdd:TIGR02203 134 vlvretltviGLFIVLLYYSWQLTLIV--VVMLPV--LSILMRRVSKRLRRISKEIQNSMG----QVTTVAEETLQGYRV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 994 IRAYCAQDILKKEFDKLQDVHTSTVyMYVVSSSGFGFSLDIFCfVFTSLVTFSFLLLEQSFSGG-EVGLAITQVMAMTGM 1072
Cdd:TIGR02203 206 VKLFGGQAYETRRFDAVSNRNRRLA-MKMTSAGSISSPITQLI-ASLALAVVLFIALFQAQAGSlTAGDFTAFITAMIAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1073 IQwGMRQNAEAANQM----MAVERVLEYTNIPPEPnlrDRGKFAKKSEKqialpanapknwpkdGMIRFRNVYMRYAEEE 1148
Cdd:TIGR02203 284 IR-PLKSLTNVNAPMqrglAAAESLFTLLDSPPEK---DTGTRAIERAR---------------GDVEFRNVTFRYPGRD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1149 LPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRR 1227
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIAN 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1228 NL---DPfNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQ 1304
Cdd:TIGR02203 425 NIaygRT-EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1305 TDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEY-DHPHMLLQNTY 1360
Cdd:TIGR02203 504 SERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERgTHNELLARNGL 560
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
785-1097 |
2.80e-60 |
|
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: 209.38 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 785 AVTLLLFFICTQFMASLNDYFVPILVSKEEtrtyllqQTALNATNETSTENLDISSMYnYMYIYTAIVVGLFCIGITRSL 864
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANH-------DVASVVFNITSSSLEDDEVSY-YISVYAGLSLGAVILSLVTNL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 865 TFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNPLF 944
Cdd:cd18602 73 AGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 945 LIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVS 1024
Cdd:cd18602 153 LIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1025 SSGFGFSLDIF--CFVFTSLVTFSFLLLEQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYT 1097
Cdd:cd18602 233 NRWLGIRLDYLgaVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
75-707 |
1.87e-59 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 215.80 E-value: 1.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 75 KRRPSLLRAIFRaFLWEY---VVLGLMQILNEFVIRLGTPILLGGLLRYFRKSTDETY--ETALWYAAGICIATAINVIT 149
Cdd:COG1132 3 KSPRKLLRRLLR-YLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSAllLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 150 LNQAIFGAFHVGARIRVAtcsvVYRKALRLSKTALGETAPGKVVNLVANDVNRF-DLVSIFIHHMWSAPLSALIIAYFLY 228
Cdd:COG1132 82 RYLLARLAQRVVADLRRD----LFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVeQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 229 TEAGYAGLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKS----FCALIETARKLE 304
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 305 LRVVKKSSYIRGIYMTFNLFTtrMALFCTLISMLLFGNELSADKVFVFSSYFNILAHTMTgMFVRGFAEIAECLVAVRRL 384
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLG--LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLR-QLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 385 QHFLmyeefqentfalnkfaasvngsinndskqasnktskpdipyiDEETSTYENLDDSEKRKHNGlvvvasdllqktan 464
Cdd:COG1132 315 FELL------------------------------------------DEPPEIPDPPGAVPLPPVRG-------------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 465 lmeekkrssSIRINeepyavkmtNFTAKWEPGqsENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVK 544
Cdd:COG1132 339 ---------EIEFE---------NVSFSYPGD--RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 545 VNG-------------SLSYAGQEAWVFGSTVRQNILFGQP-YDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLS 610
Cdd:COG1132 399 IDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 611 GGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEEcIQRYLAGKTRILATHQLQYVKNVDAIILIEQGK-ATVFS 689
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRiVEQGT 557
|
650
....*....|....*...
gi 383847295 690 HyQDLLSQRPEYAELLAA 707
Cdd:COG1132 558 H-EELLARGGLYARLYRL 574
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
105-384 |
1.59e-58 |
|
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: 203.84 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 105 VIRLGTPILLGGLLRYFRKSTDETYETALW----YAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVYRKALRLS 180
Cdd:cd18597 11 VLQVLSPLLLKYLINFVEDAYLGGPPPSIGygigYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAIYRKSLRLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 181 KTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYTGKLSSKFR 260
Cdd:cd18597 91 GKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 261 LQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMALFCTLISMLLF 340
Cdd:cd18597 171 KKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASMLSFITYYAT 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 383847295 341 GNELSADKVFVFSSYFNILAHTMTgMFVRGFAEIAECLVAVRRL 384
Cdd:cd18597 251 GHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
818-1097 |
1.62e-58 |
|
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: 203.86 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 818 YLLQQTALNATN----ETSTENLDISSMYN-----YMYIYTAIVVGLFCIGITRSLTFYEVCIVCSQKLHDMAFSALIRT 888
Cdd:cd18603 8 YLLSQAFSVGSNiwlsEWSDDPALNGTQDTeqrdyRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 889 GMRFFDTNPSGRILNRFSKDMGTIDELLPKAVldagQICMMMF----GSLAVSCIVNPLFLIPIVFLGTVFYWIRKVYLK 964
Cdd:cd18603 88 PMSFFDTTPLGRILNRFSKDIDTVDNTLPQNI----RSFLNCLfqviSTLVVISISTPIFLVVIIPLAILYFFIQRFYVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 965 TSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDifcFVFTSLVT 1044
Cdd:cd18603 164 TSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLE---FLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1045 FSFLLL---EQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYT 1097
Cdd:cd18603 241 FAALFAvlsRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1135-1357 |
3.80e-58 |
|
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: 200.53 E-value: 3.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYaEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVsSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSGTLRRNL---DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQ 1357
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1135-1348 |
2.10e-56 |
|
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: 195.53 E-value: 2.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSGTLRRNL---DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1133-1372 |
2.97e-56 |
|
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: 196.61 E-value: 2.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEIDDIDTGSICLEDLRRHIS 1212
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKIL 1292
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1293 MLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLqNTYSQFTSLVKETDR 1372
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHFKQAISPSDR 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
484-683 |
7.34e-55 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 190.62 E-value: 7.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQSenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVN----------------- 546
Cdd:cd03290 1 VQVTNGYFSWGSGLA--TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 547 GSLSYAGQEAWVFGSTVRQNILFGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQ 626
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 627 ADVYLLDDPLSAVDTHVSKHLFEECIQRYLAG--KTRILATHQLQYVKNVDAIILIEQG 683
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1135-1348 |
5.13e-53 |
|
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: 185.82 E-value: 5.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEE-ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHIS 1212
Cdd:cd03249 1 IEFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSGTLRRNLdpfnEFSDAALWEVLEEVELKDAV---VISG--NGLESRVLDRGSNYSVGQRQLVCLARAILR 1287
Cdd:cd03249 81 LVSQEPVLFDGTIAENI----RYGKPDATDEEVEEAAKKANihdFIMSlpDGYDTLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1288 NNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1133-1346 |
5.44e-52 |
|
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: 182.40 E-value: 5.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHI 1211
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSGTLRRNLDPFNEF-SDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRM 1346
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
108-384 |
1.95e-51 |
|
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: 183.15 E-value: 1.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 108 LGTPILLGGLLRYFRKSTDETYETALWyAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVYRKALRLSktALGET 187
Cdd:cd18592 15 IGPTILIRKLLEYLEDSDSSVWYGILL-VLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLR--SLGDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 188 APGKVVNLVANDVNR-FDlVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIK 266
Cdd:cd18592 92 SVGELINIFSNDGQRlFD-AAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 267 TDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMALFCTLISMLLFGNELSA 346
Cdd:cd18592 171 TDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTA 250
|
250 260 270
....*....|....*....|....*....|....*...
gi 383847295 347 DKVFVFSSYFNILAHTMtGMFVRGFAEIAECLVAVRRL 384
Cdd:cd18592 251 AQAFTVIAVFNSMRFSL-RMLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
785-1097 |
9.87e-51 |
|
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: 181.57 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 785 AVTLLLFFICTQFMASLNDYfvpilvskeetrtYLLQQTalNATNETSTENLDISSMYnYMYIYTAIVVGLFCIGITRSL 864
Cdd:cd18605 1 LILILLSLILMQASRNLIDF-------------WLSYWV--SHSNNSFFNFINDSFNF-FLTVYGFLAGLNSLFTLLRAF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 865 TFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVldagQICMMMF----GSLAVSCIV 940
Cdd:cd18605 65 LFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFIL----NILLAQLfgllGYLVVICYQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 941 NPLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYM 1020
Cdd:cd18605 141 LPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1021 YVVSSSGFGFSLDIF-CFVFTSLVTFSFL--LLEQSFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYT 1097
Cdd:cd18605 221 SQAASQWLSIRLQLLgVLIVTFVALTAVVqhFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1118-1358 |
5.72e-50 |
|
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: 188.11 E-value: 5.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1118 QIALPANAPKNWPKDGMIRFRNVYMRYaEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDD 1196
Cdd:COG5265 341 EVADAPDAPPLVVGGGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVtSGRILIDG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1197 IDTGSICLEDLRRHISIIPQDPVLFSGTLRRNL---DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSV 1273
Cdd:COG5265 420 QDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1274 GQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEY-DHP 1352
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERgTHA 577
|
....*.
gi 383847295 1353 HMLLQN 1358
Cdd:COG5265 578 ELLAQG 583
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
772-1096 |
3.50e-49 |
|
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: 178.07 E-value: 3.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 772 FIKYFQTGANLCLAVTLLLFFICTQFMASLNDYFvpiLVSKEETRTyllQQTALNATNETSTENLDISSMYNYMYIYTAI 851
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLW---LLRSQADRV---NTTRPESSSNTYAVIVTFTSSYYVFYIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 852 VVGLFCIGITRSLTFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMF 931
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 932 GSLAVSCIVNPLFLIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQ 1011
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1012 DVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLVTFSFLLLEQsFSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVE 1091
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTG-DGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
....*
gi 383847295 1092 RVLEY 1096
Cdd:cd18600 319 RIFKF 323
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1074-1341 |
1.93e-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: 179.02 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1074 QWGMRQNAEAANQMMAveRVLEYTNIPpepnlrdrgkfakksekqiaLPANAPKNWPKDGMIRFRNVYMRYAEEElPVLK 1153
Cdd:TIGR02857 283 QYHARADGVAAAEALF--AVLDAAPRP--------------------LAGKAPVTAAPASSLEFSGVSVAYPGRR-PALR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1154 GLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNL--- 1229
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPtEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrla 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1230 DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALI 1309
Cdd:TIGR02857 420 RP--DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
250 260 270
....*....|....*....|....*....|..
gi 383847295 1310 QNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVM 1341
Cdd:TIGR02857 498 LEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
876-1348 |
2.81e-47 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 181.84 E-value: 2.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 876 KLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIV 949
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltmvtLINLPLV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 950 FLGTVFY--WIRKVYLKTSKNIKRLEGMSRSpvfthlnaTLNGLTTIRAYCAQDI-LKKEFDKLQDVHTST--------V 1018
Cdd:TIGR00958 315 FLAEKVFgkRYQLLSEELQEAVAKANQVAEE--------ALSGMRTVRSFAAEEGeASRFKEALEETLQLNkrkalayaG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1019 YMYVVSSSGFGFSLDIFCF----VFTSLVT----FSFLLLEQsfsggEVGLAITQVMAMTGmiqwGMRQNAEAAnqmmav 1090
Cdd:TIGR00958 387 YLWTTSVLGMLIQVLVLYYggqlVLTGKVSsgnlVSFLLYQE-----QLGEAVRVLSYVYS----GMMQAVGAS------ 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1091 ERVLEYTNIPPepnlrdrgkfakksekQIALPAN-APKNwpKDGMIRFRNVYMRY-AEEELPVLKGLNLVINPGEKIGIV 1168
Cdd:TIGR00958 452 EKVFEYLDRKP----------------NIPLTGTlAPLN--LEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALV 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1169 GRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLD-PFNEFSDAALWEVLEE 1246
Cdd:TIGR00958 514 GPSGSGKSTVAALLQNLYQpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1247 VELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTirRKFTKCTVLTIA 1326
Cdd:TIGR00958 594 ANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIA 671
|
490 500
....*....|....*....|..
gi 383847295 1327 HRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:TIGR00958 672 HRLSTVERADQILVLKKGSVVE 693
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
58-709 |
4.31e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 181.57 E-value: 4.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 58 DRLEKRWNNEL------ENSKRYKRRPSLLRAIFRAF------LWEYVVLGLM-QILNefvirLGTPILLGGLLryfrks 124
Cdd:COG2274 115 EEFAESWTGVAllleptPEFDKRGEKPFGLRWFLRLLrryrrlLLQVLLASLLiNLLA-----LATPLFTQVVI------ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 125 tDE-----TYETALWYAAGICIATAIN-VITLNQAIFGAfHVGARIRVATCSVVYRKALRLSKTALGETAPGKVVNLVaN 198
Cdd:COG2274 184 -DRvlpnqDLSTLWVLAIGLLLALLFEgLLRLLRSYLLL-RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-R 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 199 DVNR---FdLVSIFIhhmwSAPLSALIIAYFLYTEAGYAGLIGIAAVfVVVPIQSYTGKLSSKFRLQTAIKT----DERV 271
Cdd:COG2274 261 DVESireF-LTGSLL----TALLDLLFVLIFLIVLFFYSPPLALVVL-LLIPLYVLLGLLFQPRLRRLSREEseasAKRQ 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 272 RLMDEIISGVQVIKMYA--------WEKSFCALIetarKLELRVVKKSSYIRGIYMTFNLFTTRMALFctLISMLLFGNE 343
Cdd:COG2274 335 SLLVETLRGIETIKALGaesrfrrrWENLLAKYL----NARFKLRRLSNLLSTLSGLLQQLATVALLW--LGAYLVIDGQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 344 LS-----AdkvfvfssyFNILAHTMTG---MFVRGFAEIAECLVAVRRLQHFLMYEefQENTfalnkfaasvngsinNDS 415
Cdd:COG2274 409 LTlgqliA---------FNILSGRFLApvaQLIGLLQRFQDAKIALERLDDILDLP--PERE---------------EGR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 416 KQASNKTSKPDIpyideetsTYENLddsekrkhnglvvvasdllqktanlmeekkrssSIRineepYavkmtnftakweP 495
Cdd:COG2274 463 SKLSLPRLKGDI--------ELENV---------------------------------SFR-----Y------------P 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 496 GQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGST 562
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGT 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGQPY-DRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:COG2274 565 IRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 642 HvSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELLAAEN 709
Cdd:COG2274 645 E-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
105-384 |
5.21e-46 |
|
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: 168.44 E-value: 5.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 105 VIRLGTPILLGGLLRYFRKSTDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVYRKALRL----- 179
Cdd:cd18596 11 VLSFAPPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 180 --------------SKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVV 245
Cdd:cd18596 91 ssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 246 VPIQSYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFT 325
Cdd:cd18596 171 LPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLI 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 326 TRMALFCTLIS-MLLFGNELSADKVFVFSSYFNILAHTMtGMFVRGFAEIAECLVAVRRL 384
Cdd:cd18596 251 PILVTVVTFATyTLVMGQELTASVAFTSLALFNMLRGPL-NVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1135-1348 |
3.72e-45 |
|
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: 163.43 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEnGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSGTLRRNLDPFNEfsDAALWEVLEEVELKDA---VVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
496-697 |
4.79e-45 |
|
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: 172.64 E-value: 4.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 496 GQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGST 562
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGQP-YDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:COG4988 427 IRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDA 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 642 HVSKHLFEEcIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQ 697
Cdd:COG4988 507 ETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
157-706 |
1.57e-43 |
|
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: 168.02 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 157 AFHVGARIRVAtcsvVYRKALRLSKTALGETAPGKVVNLVANDVNRFDLVSI-FIHHMWSAPLSALIIAYFLY---TEAG 232
Cdd:COG4987 83 TLRLLADLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLrVLLPLLVALLVILAAVAFLAffsPALA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 233 YAGLIGIAAVFVVVPIQSYtgKLSSKF-RLQTAIKTDERVRLMDeIISGVQVIKMY-AWEKSFCALIETARKLeLRVVKK 310
Cdd:COG4987 159 LVLALGLLLAGLLLPLLAA--RLGRRAgRRLAAARAALRARLTD-LLQGAAELAAYgALDRALARLDAAEARL-AAAQRR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 311 SSYIRGIYMTFNLFTtrMALfcTLISMLLFGNELSADK--------VFVFS--SYFNILAhtmtgMFVRGFAEIAECLVA 380
Cdd:COG4987 235 LARLSALAQALLQLA--AGL--AVVAVLWLAAPLVAAGalsgpllaLLVLAalALFEALA-----PLPAAAQHLGRVRAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 381 VRRLQHFLmyeefqentfalnkfaasvngsinndskqasnkTSKPDIPYIDEEtstyenlddsekrkhnglvvvasdllq 460
Cdd:COG4987 306 ARRLNELL---------------------------------DAPPAVTEPAEP--------------------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 461 ktanlmeekkrsssiRINEEPYAVKMTNFTAKWePGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVE 540
Cdd:COG4987 326 ---------------APAPGGPSLELEDVSFRY-PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 541 GHVKVNG-------------SLSYAGQEAWVFGSTVRQNILFGQPY--DrhryQKVVKACSL--LRDF-KQFPQSDQTVV 602
Cdd:COG4987 390 GSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPDatD----EELWAALERvgLGDWlAALPDGLDTWL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 603 GERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEEcIQRYLAGKTRILATHQLQYVKNVDAIILIEQ 682
Cdd:COG4987 466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
570 580
....*....|....*....|....
gi 383847295 683 GKATVFSHYQDLLSQRPEYAELLA 706
Cdd:COG4987 545 GRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1133-1357 |
4.34e-42 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 164.12 E-value: 4.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHI 1211
Cdd:PRK10790 339 GRIDIDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLtEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKI 1291
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1292 LMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQ 1357
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1135-1346 |
7.08e-42 |
|
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: 151.60 E-value: 7.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSGTLRRNldpfnefsdaalwevleevelkdavVISGnglesrvldrgsnysvGQRQLVCLARAILRNNKILM 1293
Cdd:cd03246 81 LPQDDELFSGSIAEN-------------------------ILSG----------------GQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1294 LDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMDSDKVLVMDKGRM 1346
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1089-1363 |
1.57e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 162.30 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1089 AVERVLEYTNIPPEPnlrdrgKFAKKSEKQIALPAnapknwpkdgmIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIV 1168
Cdd:PRK11160 310 SARRINEITEQKPEV------TFPTTSTAAADQVS-----------LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1169 GRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNL---DPfnEFSDAALWEVL 1244
Cdd:PRK11160 373 GRTGCGKSTLLQLLTRAWDPQqGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1245 EEVELkDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLT 1324
Cdd:PRK11160 451 QQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLM 529
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 383847295 1325 IAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLL--QNTYSQF 1363
Cdd:PRK11160 530 ITHRLTGLEQFDRICVMDNGQIIEQGTHQELLaqQGRYYQL 570
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
851-1366 |
2.25e-40 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 159.03 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 851 IVVGLFCI-GITRSLTFYEVCIVCSQKLHDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDA--- 923
Cdd:PRK11176 70 VVIGLMILrGITSFISSYCISWVSGKVVMTMrrrLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVvre 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 924 -----GQICMMMFGSLAVSCIvnpLFLI-PIVFLGtvfywIR---KVYLKTSKNIKRLEGMsrspVFTHLNATLNGLTTI 994
Cdd:PRK11176 150 gasiiGLFIMMFYYSWQLSLI---LIVIaPIVSIA-----IRvvsKRFRNISKNMQNTMGQ----VTTSAEQMLKGHKEV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 995 RAYCAQDILKKEFDKLQDvHTSTVYMYVVSSSG-------FGFSLDIFCFVFTSlvtfSFLLLEQSFSGGevglAITQVM 1067
Cdd:PRK11176 218 LIFGGQEVETKRFDKVSN-RMRQQGMKMVSASSisdpiiqLIASLALAFVLYAA----SFPSVMDTLTAG----TITVVF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1068 -AMTGMiqwgMRQ-------NAEAANQMMAVERVLEYTNIPPEpnlRDRGKFAKKSEKqialpanapknwpkdGMIRFRN 1139
Cdd:PRK11176 289 sSMIAL----MRPlksltnvNAQFQRGMAACQTLFAILDLEQE---KDEGKRVIERAK---------------GDIEFRN 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1140 VYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISIIPQDP 1218
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIdEGEILLDGHDLRDYTLASLRNQVALVSQNV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1219 VLFSGTLRRNL--DPFNEFSDAalwEVLEEVELKDAV-VISG--NGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILM 1293
Cdd:PRK11176 427 HLFNDTIANNIayARTEQYSRE---QIEEAARMAYAMdFINKmdNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1294 LDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEY-DHPHMLLQN-TYSQFTSL 1366
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERgTHAELLAQNgVYAQLHKM 578
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1150-1348 |
1.86e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 156.16 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNL 1229
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1230 ---DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTD 1306
Cdd:PRK11174 444 llgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 383847295 1307 ALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:PRK11174 522 QLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1133-1348 |
2.20e-39 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 155.89 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEIDDIDTGSICLEDLRRHI 1211
Cdd:PRK13657 333 GAVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVfDPQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSGTLRRNLDPFNE-FSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
94-359 |
2.30e-39 |
|
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: 148.47 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 94 VLGLMQILNeFVIRLGTPILLGGLLRYFrKSTDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVY 173
Cdd:cd18598 1 PLGLLKLLA-DVLGFAGPLLLNKLVEFL-EDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 174 RKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQ---- 249
Cdd:cd18598 79 RKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINkwia 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 250 SYTGKLSSKFRLQTaiktDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIyMTFNLFTTRMA 329
Cdd:cd18598 159 KRIGALSEKMMKHK----DARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATTPVL 233
|
250 260 270
....*....|....*....|....*....|.
gi 383847295 330 L-FCTLISMLLFGNELSADKVFVFSSYFNIL 359
Cdd:cd18598 234 IsILTFATYVLMGNTLTAAKVFTSLALFNML 264
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
495-704 |
6.44e-39 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 145.45 E-value: 6.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGS 561
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILFGQP-YDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:cd03251 91 TVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 641 ThVSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAEL 704
Cdd:cd03251 171 T-ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
138-360 |
1.53e-38 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 146.61 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 138 GICIATAINVITLNQAIF--GAFHV----GARIRVATCSVVYRKALRLSKTAL--GETAPGKVVNLVANDVNRFDLVSIF 209
Cdd:cd18591 55 GYVLAVILFLALLLQATFsqASYHIvireGIRLKTALQAMIYEKALRLSSWNLssGSMTIGQITNHMSEDANNIMFFFWL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 210 IHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAW 289
Cdd:cd18591 135 IHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAW 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 290 EKSFCALIETARKLELRVVKKSSYIRGIyMTFnlFTTRMALFCTLISMLLF----GNELSADKVFVFSSYFNILA 360
Cdd:cd18591 215 ENIFLDKIQEARRKELKLLLKDAVYWSL-MTF--LTQASPILVTLVTFGLYpyleGEPLTAAKAFSSLALFNQLT 286
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
845-1329 |
4.44e-38 |
|
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: 150.97 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 845 MYIYTAIV-VGLFciGITRSLTFYEVCIVcsqkLHDMAFSALIRTGMRFFD----TNPSGR-------ILNRFSKDMGTI 912
Cdd:TIGR02868 50 LYLSVAAVaVRAF--GIGRAVFRYLERLV----GHDAALRSLGALRVRVYErlarQALAGRrrlrrgdLLGRLGADVDAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 913 DELLPKAVLDAGQICMMMFGSLAVSCIVNPLF-LIPIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGL 991
Cdd:TIGR02868 124 QDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAaLILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 992 TTIRAYCAQDILKKEFDKlQDVHTSTVYMYVVSSSGFGFSLDIfcfVFTSLVTFSFLLL--EQSFSGGEVGLAITQVM-- 1067
Cdd:TIGR02868 204 AELVASGALPAALAQVEE-ADRELTRAERRAAAATALGAALTL---LAAGLAVLGALWAggPAVADGRLAPVTLAVLVll 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1068 ---------AMTGMIQwGMRQNAEAAnqmmavERVLEYTNIPPEpnlrdrgkfakKSEKQIALPANAPknwPKDGMIRFR 1138
Cdd:TIGR02868 280 plaafeafaALPAAAQ-QLTRVRAAA------ERIVEVLDAAGP-----------VAEGSAPAAGAVG---LGKPTLELR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1139 NVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFR-LAKVEGVIEIDDIDTGSICLEDLRRHISIIPQD 1217
Cdd:TIGR02868 339 DLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQD 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1218 PVLFSGTLRRNL---DPfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILML 1294
Cdd:TIGR02868 418 AHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
490 500 510
....*....|....*....|....*....|....*
gi 383847295 1295 DEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRL 1329
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
495-684 |
8.44e-38 |
|
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: 139.83 E-value: 8.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGS 561
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILfgqpydrhryqkvvkacsllrdfkqfpqsdqtvvgergsslSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:cd03228 91 TIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 383847295 642 HvSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:cd03228 130 E-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1116-1349 |
6.48e-37 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 147.97 E-value: 6.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1116 EKQIALPAnapknwPKdGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEI 1194
Cdd:COG4618 319 PERMPLPR------PK-GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPpTAGSVRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1195 DDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVG 1274
Cdd:COG4618 392 DGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1275 QRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEY 1349
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
502-704 |
7.56e-37 |
|
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: 139.60 E-value: 7.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-------------LSYAGQEAWVFGSTVRQNIL 568
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPyDRHRYQkVVKACSL--LRDF-KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSK 645
Cdd:cd03249 99 YGKP-DATDEE-VEEAAKKanIHDFiMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE-SE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 646 HLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAEL 704
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1108-1349 |
8.17e-37 |
|
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: 147.49 E-value: 8.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1108 RGKFAKKSEKQIALPANAPK-NWPK-DGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL 1185
Cdd:TIGR01842 288 RQAYKRLNELLANYPSRDPAmPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1186 AK-VEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLDPFNEFSDAAlwEVLEEVELKDA--VVIS-GNGLE 1261
Cdd:TIGR01842 368 WPpTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPE--KIIEAAKLAGVheLILRlPDGYD 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1262 SRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTD-ALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLV 1340
Cdd:TIGR01842 446 TVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEqALANAIKALKARGITVVVITHRPSLLGCVDKILV 525
|
....*....
gi 383847295 1341 MDKGRMAEY 1349
Cdd:TIGR01842 526 LQDGRIARF 534
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
495-684 |
1.27e-36 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 138.11 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGS 561
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILFGQPYdrHRYQKVVKACSL--LRDF-KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSA 638
Cdd:cd03245 93 TLRDNITLGAPL--ADDERILRAAELagVTDFvNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 383847295 639 VDTHVSKHLFEEcIQRYLAGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:cd03245 171 MDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1135-1353 |
3.72e-36 |
|
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: 137.08 E-value: 3.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKpTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPV--LFSGTLR-------RNL--DPfnEFSDAALWEVLEEVELKDavvisgnglesrVLDRGSNY-SVGQRQLVCL 1281
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENLglPR--EEIRERVEEALELVGLEH------------LADRPPHElSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1282 ARAILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPH 1353
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPR 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1152-1299 |
9.64e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.16 E-value: 9.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSG-TLRRNL 1229
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1230 -------DPFNEFSDAALWEVLEEVELKDAvvisgngLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATA 1299
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
502-680 |
3.13e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 142.43 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNIL 568
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPY-DRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHL 647
Cdd:TIGR02857 418 LARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE-TEAE 496
|
170 180 190
....*....|....*....|....*....|...
gi 383847295 648 FEECIQRYLAGKTRILATHQLQYVKNVDAIILI 680
Cdd:TIGR02857 497 VLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
885-1348 |
4.54e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 143.94 E-value: 4.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 885 LIRTGMRFFDTNPSGRILNRFSKdMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVN-PLFLIPIVFL---GTVFYWIRk 960
Cdd:TIGR03797 219 LLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSwKLALVAVALAlvaIAVTLVLG- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 961 vYLKTSKNIKRLEGMSRspVFTHLNATLNGLTTIRA--------------YCAQDILKKEFDKLQDVHTSTVYMYVVsss 1026
Cdd:TIGR03797 297 -LLQVRKERRLLELSGK--ISGLTVQLINGISKLRVagaenrafarwaklFSRQRKLELSAQRIENLLTVFNAVLPV--- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1027 gfgfsldifcfvFTSLVTFSFLlleqSFSGGEVGLAITQVMAMT---GMIQWGMRQNAEAANQMMAV----ERVLEYTNI 1099
Cdd:TIGR03797 371 ------------LTSAALFAAA----ISLLGGAGLSLGSFLAFNtafGSFSGAVTQLSNTLISILAViplwERAKPILEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1100 PPEPNLR--DRGKFAkksekqialpanapknwpkdGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSS 1177
Cdd:TIGR03797 435 LPEVDEAktDPGKLS--------------------GAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1178 LisalFRL-----AKVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDA 1252
Cdd:TIGR03797 495 L----LRLllgfeTPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAED 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1253 VVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRkfTKCTVLTIAHRLNTI 1332
Cdd:TIGR03797 571 IRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTI 648
|
490
....*....|....*.
gi 383847295 1333 MDSDKVLVMDKGRMAE 1348
Cdd:TIGR03797 649 RNADRIYVLDAGRVVQ 664
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1132-1346 |
1.29e-34 |
|
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: 132.59 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1132 DGMIRFRNVYMRYAEE-ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEG--VIeiddIDTGSICLED-- 1206
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGgqVL----LDGKPISQYEhk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 -LRRHISIIPQDPVLFSGTLRRNLD------PFNEFSDAAlwevlEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLV 1279
Cdd:cd03248 85 yLHSKVSLVGQEPVLFARSLQDNIAyglqscSFECVKEAA-----QKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1280 CLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRM 1346
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1136-1345 |
3.96e-34 |
|
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: 130.66 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1136 RFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAL-FRLAKVEGVIEIDDIDTGSICLEDLRRHISII 1214
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1215 PQDP--VLFSGTLR-------RNLDPFNEFSDAALWEVLEEVELKDavvisgngLESRVLdrgSNYSVGQRQLVCLARAI 1285
Cdd:cd03225 81 FQNPddQFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLEG--------LRDRSP---FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1286 LRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1136-1345 |
4.79e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 128.52 E-value: 4.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1136 RFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISII 1214
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1215 PQdpvlfsgtlrrnldpfnefsdaalwevleevelkdavvisgnglesrvldrgsnYSVGQRQLVCLARAILRNNKILML 1294
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 1295 DEATANVDPQTDALIQNTIRRKF-TKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1135-1348 |
7.07e-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: 128.58 E-value: 7.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFR-LAKVEGVIEIDDIDTGSicLEDLRRH-IS 1212
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSD--LEKALSSlIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSGTLRRNLdpfnefsdaalwevleevelkdavvisgnglesrvldrGSNYSVGQRQLVCLARAILRNNKIL 1292
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1293 MLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1134-1358 |
8.80e-34 |
|
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: 137.73 E-value: 8.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL----AKVEGVIEIDDIDTGSICLEDLRR 1209
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphgGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1210 HISIIPQDP------------VLFsgTLRRNLDPFNEFSDAALwEVLEEVelkdavvisgnGLESRVLDRGSNYSVGQRQ 1277
Cdd:COG1123 84 RIGMVFQDPmtqlnpvtvgdqIAE--ALENLGLSRAEARARVL-ELLEAV-----------GLERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHM 1354
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....
gi 383847295 1355 LLQN 1358
Cdd:COG1123 230 ILAA 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1134-1359 |
1.04e-33 |
|
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: 130.75 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEdLRRHIS 1212
Cdd:COG4555 1 MIEVENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIDGEDVRKEPRE-ARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSG-TLRRNLDPFNEFSDaalwEVLEEVELKDAVVISGNGLEsRVLDRG-SNYSVGQRQLVCLARAILRNNK 1290
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAELYG----LFDEELKKRIEELIELLGLE-EFLDRRvGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTiAHrlntIMD-----SDKVLVMDKGRMAEYDHPHMLLQNT 1359
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRalKKEGKTVLFS-SH----IMQevealCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1134-1362 |
1.65e-33 |
|
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: 130.31 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRY--AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRH 1210
Cdd:COG1124 1 MLEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPvlFS-----GTLRRNLD-PFNEF----SDAALWEVLEEVelkdavvisgnGLESRVLDRgsnY----SVGQR 1276
Cdd:COG1124 81 VQMVFQDP--YAslhprHTVDRILAePLRIHglpdREERIAELLEQV-----------GLPPSFLDR---YphqlSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTI--MdSDKVLVMDKGRMAEY--- 1349
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEEltv 223
|
250
....*....|...
gi 383847295 1350 DHPHMLLQNTYSQ 1362
Cdd:COG1124 224 ADLLAGPKHPYTR 236
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
502-710 |
1.68e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 138.05 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVvEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNIL 568
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQP-YDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHL 647
Cdd:PRK11174 445 LGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH-SEQL 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 648 FEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELLAAENE 710
Cdd:PRK11174 524 VMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1134-1349 |
2.41e-33 |
|
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: 129.16 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELPV--LKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSI---CLEDL 1207
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtSGSIIFDGKDLLKLsrrLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPV-----------LFSGTLRRNLDPFNEfsdaalwEVLEEVELKDAVVIsgnGLESRVLDRgsnY----S 1272
Cdd:cd03257 81 RKEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKK-------EARKEAVLLLLVGV---GLPEEVLNR---YphelS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1273 VGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTI-MDSDKVLVMDKGRMAEY 1349
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
501-698 |
6.50e-33 |
|
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: 127.73 E-value: 6.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNI 567
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFGQPYDRHryQKVVKACSLLR--DF-KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVS 644
Cdd:cd03254 98 RLGRPNATD--EEVIEAAKEAGahDFiMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 645 KhLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQR 698
Cdd:cd03254 176 K-LIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1135-1345 |
7.65e-33 |
|
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: 126.82 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEEL---PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIddidtgsicledlRRH 1210
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1291 ILMLDEATANVDPQT-DALIQNTIRRKFTKC-TVLTIAHRLNTIMDSDKVLVMDKGR 1345
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
117-388 |
1.96e-32 |
|
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: 128.49 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 117 LLRYFRKSTDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVVYRKALRLSKTALGETAPGKVVNLV 196
Cdd:cd18559 22 LLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 197 ANDVNRFDLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIKTDERVRLMDE 276
Cdd:cd18559 102 SKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 277 IISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMALFCTLISMLLFG--NELSADKVFVFSS 354
Cdd:cd18559 182 TLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslAGLVALKVFYSLA 261
|
250 260 270
....*....|....*....|....*....|....
gi 383847295 355 YFNILAhtmtgMFVRGFAEIAECLVAVRRLQHFL 388
Cdd:cd18559 262 LTTYLN-----WPLNMSPEVITNIVAAEVSLERS 290
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
504-1342 |
6.39e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.31 E-value: 6.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 504 NLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS--------------LSYAGQEAWVFGSTVRQNILF 569
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskIGVVSQDPLLFSNSIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 G-------------------QPYD-------------------------------RHRYQKV-------VKACSLLRDF- 591
Cdd:PTZ00265 483 SlyslkdlealsnyynedgnDSQEnknkrnscrakcagdlndmsnttdsneliemRKNYQTIkdsevvdVSKKVLIHDFv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 592 KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHLFEECIQRYLAGKTRI--LATHQLQ 669
Cdd:PTZ00265 563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNENRItiIIAHRLS 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 670 YVKNVDAIILI---EQG-KATVFSHYQDLLSQRPEYAE----------------------LLAAENETHD---------- 713
Cdd:PTZ00265 642 TIRYANTIFVLsnrERGsTVDVDIIGEDPTKDNKENNNknnkddnnnnnnnnnnkinnagSYIIEQGTHDalmknkngiy 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 714 ----------------DSSLEKSVMRRQFSSSSTRSRTPDASSGGTDDEEEDEDAEKLNDGLEGTSRGTVKG---PIFIK 774
Cdd:PTZ00265 722 ytminnqkvsskkssnNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASENNAGgklPFLRN 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 775 YFQ---TGANLCLAVTLLLFfictQFMASLNDYFVPILVSKEetrtyLLQQTALNATNETST----ENLDISSMYNYMYI 847
Cdd:PTZ00265 802 LFKrkpKAPNNLRIVYREIF----SYKKDVTIIALSILVAGG-----LYPVFALLYAKYVSTlfdfANLEANSNKYSLYI 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 848 YTaIVVGLFcigITRSLTFYEVCIVCSQKLHDMA---FSALIRTGMRFFD--TNPSGRILNRFSKDMGTIDELLPKAVLD 922
Cdd:PTZ00265 873 LV-IAIAMF---ISETLKNYYNNVIGEKVEKTMKrrlFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVI 948
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 923 AGQICMMMFGSLAVSCIVNPLflIPIVFLGTVFYWIR----KVYLKTSKNIKRLEGMSRSPVFTH-------------LN 985
Cdd:PTZ00265 949 FTHFIVLFLVSMVMSFYFCPI--VAAVLTGTYFIFMRvfaiRARLTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQ 1026
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 986 ATLNGLTTIRAYCAQDILKKEFDKLQDV-HTSTVYMYVVSSSGFGFS------LDIFCFVFTSLVT-------------- 1044
Cdd:PTZ00265 1027 EAFYNMNTVIIYGLEDYFCNLIEKAIDYsNKGQKRKTLVNSMLWGFSqsaqlfINSFAYWFGSFLIrrgtilvddfmksl 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1045 FSFLlleqsFSGGEVGlaitQVMAMTGmiqwgmrqnaEAANQMMAVER----VLEYTNIppepNLRDRGKFAKKSEKQIa 1120
Cdd:PTZ00265 1107 FTFL-----FTGSYAG----KLMSLKG----------DSENAKLSFEKyyplIIRKSNI----DVRDNGGIRIKNKNDI- 1162
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1121 lpanapknwpkDGMIRFRNVYMRY-AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFR--------------- 1184
Cdd:PTZ00265 1163 -----------KGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkne 1231
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1185 ----------------------------------------LAKVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGT 1224
Cdd:PTZ00265 1232 htndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMS 1311
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1225 LRRNLDPFNEfsDAALWEVLEEVELK--DAVVIS-GNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANV 1301
Cdd:PTZ00265 1312 IYENIKFGKE--DATREDVKRACKFAaiDEFIESlPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 383847295 1302 DPQTDALIQNT---IRRKFTKcTVLTIAHRLNTIMDSDKVLVMD 1342
Cdd:PTZ00265 1390 DSNSEKLIEKTivdIKDKADK-TIITIAHRIASIKRSDKIVVFN 1432
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
502-704 |
7.06e-32 |
|
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: 125.04 E-value: 7.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNIL 568
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQP--YDRHRYqKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKH 646
Cdd:cd03253 97 YGRPdaTDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTERE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 647 LFeECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAEL 704
Cdd:cd03253 176 IQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
502-704 |
1.31e-31 |
|
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: 124.52 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNIL 568
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQP-YDRHRyqkVVKACSLL--RDF-KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvS 644
Cdd:cd03252 98 LADPgMSMER---VIEAAKLAgaHDFiSELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-S 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 645 KHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAEL 704
Cdd:cd03252 174 EHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1135-1349 |
7.12e-31 |
|
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: 121.90 E-value: 7.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL------AKVEGVIEID--DIDTGSICLED 1206
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgAPDEGEVLLDgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDPVLFSGTLRRNLD--------PFNEFSDAALWEVLEEVELKDavvisgnglesRVLDR--GSNYSVGQR 1276
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWD-----------EVKDRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAH------RLntimdSDKVLVMDKGRMAEY 1349
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEF 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1150-1360 |
3.01e-30 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 129.09 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRN 1228
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1229 LDPFNE--FSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTD 1306
Cdd:TIGR01193 568 LLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1307 ALIQNTIrRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEY-DHPHMLLQNTY 1360
Cdd:TIGR01193 648 KKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQgSHDELLDRNGF 701
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1135-1345 |
3.14e-30 |
|
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: 120.30 E-value: 3.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEID--DIDTGS-ICLEDLRRH 1210
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLlRPDSGEVLIDgeDISGLSeAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLFSG-TLRRNLD-PFNEFSDAALWEVLEEVELKDAVVisgnGLESRVLDRGSNYSVGQRQLVCLARAILRN 1288
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTRLSEEEIREIVLEKLEAV----GLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1289 NKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGK 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1134-1364 |
4.83e-30 |
|
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: 126.56 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAE---EELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSIC---LED 1206
Cdd:COG1123 260 LLEVRNLSKRYPVrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDPV--LF-----SGTLRRNLDPFNEFSDAALW----EVLEEVelkdavvisgnGLESRVLDRgsnY---- 1271
Cdd:COG1123 340 LRRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGLLSRAERRervaELLERV-----------GLPPDLADR---Yphel 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1272 SVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAE 1348
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|....*.
gi 383847295 1349 YDHPHMLLQNTYSQFT 1364
Cdd:COG1123 486 DGPTEEVFANPQHPYT 501
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1134-1353 |
7.35e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 119.76 E-value: 7.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHIS 1212
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPsSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVL-FSGTLR------RN--LDPFNEFSD---AALWEVLEEVELKDavvisgngLESRVLDR--GsnysvGQRQL 1278
Cdd:COG1120 79 YVPQEPPApFGLTVRelvalgRYphLGLFGRPSAedrEAVEEALERTGLEH--------LADRPVDElsG-----GERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1279 VCLARAILRNNKILMLDEATANVDP--QTDALiqNTIRR--KFTKCTVLTIAHRLN-TIMDSDKVLVMDKGRMAEYDHPH 1353
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLahQLEVL--ELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPE 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1135-1372 |
7.61e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.01 E-value: 7.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSiCLEDLRRHISI 1213
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSG-TLRRNLDPF-------NEFSDAALWEVLEEVELKDAvvisgngLESRVldrgSNYSVGQRQLVCLARAI 1285
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFarlyglpRKEARERIDELLELFGLTDA-------ADRKV----GTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1286 LRNNKILMLDEATANVDPQTDALIQNTIRRKFTK-CTVLtiahrLNT-IMD-----SDKVLVMDKGRMAEYDHPHMLLQN 1358
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVL-----LSThYLEeaerlCDRVAIIDKGRIVADGTPDELKAR 221
|
250
....*....|....*
gi 383847295 1359 TYSQ-FTSLVKETDR 1372
Cdd:COG1131 222 LLEDvFLELTGEEAR 236
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
789-1071 |
9.17e-30 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 120.06 E-value: 9.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 789 LLFFICTQFMASLNDYFVPILVSKeetrtyllqqtaLNATNETSTENLDIssmynYMYIYTAIVVGLFCIGITRSLTFYE 868
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDV------------LLPDGDPETQALNV-----YSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 869 VCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNPLFLIPI 948
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 949 VFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGF 1028
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 383847295 1029 GFSLDIFCFVFTSLVTF--SFLLLEQSFSGGEVGLAITQVMAMTG 1071
Cdd:pfam00664 228 FGITQFIGYLSYALALWfgAYLVISGELSVGDLVAFLSLFAQLFG 272
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1134-1348 |
3.31e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDtgsicLEDLRRHIS 1212
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGKP-----PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQ----DP--------VLFSGTLRRN--LDPFNEFSDAALWEVLEEVELKDavvisgngLESRVLdrgSNYSVGQRQL 1278
Cdd:COG1121 79 YVPQraevDWdfpitvrdVVLMGRYGRRglFRRPSRADREAVDEALERVGLED--------LADRPI---GELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1279 VCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAE 1348
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
495-704 |
7.19e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 123.67 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVN-------------GSLSYAGQEAWVFGS 561
Cdd:PRK10789 324 PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILFGQP-YDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:PRK10789 404 TVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 641 THVSKHLFEEcIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAEL 704
Cdd:PRK10789 484 GRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1134-1349 |
9.19e-29 |
|
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: 116.14 E-value: 9.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAE--EELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSIC---LEDL 1207
Cdd:cd03258 1 MIELKNVSKVFGDtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLVDGTDLTLLSgkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPVLFSG-TLRRNLD-PFnEFSDAALWEVLEEV-ELKDAVvisgnGLESRVLDRGSNYSVGQRQLVCLARA 1284
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPL-EIAGVPKAEIEERVlELLELV-----GLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1285 ILRNNKILMLDEATANVDPQTD----ALIQNtIRRKFtKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEY 1349
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTqsilALLRD-INREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1134-1351 |
1.12e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.53 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSIC---LEDLRR 1209
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1210 HISIIPQD---------------PVLFSGTLRRNLdpfnefsDAALWEVLEEVELkdavvisgnglesrvLDRGSNY--- 1271
Cdd:COG2884 80 RIGVVFQDfrllpdrtvyenvalPLRVTGKSRKEI-------RRRVREVLDLVGL---------------SDKAKALphe 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1272 -SVGQRQLVCLARAILRNNKILMLDEATANVDPQT-----DALIQntIRRKFTkcTVLtIA-HRLNtIMDS--DKVLVMD 1342
Cdd:COG2884 138 lSGGEQQRVAIARALVNRPELLLADEPTGNLDPETsweimELLEE--INRRGT--TVL-IAtHDLE-LVDRmpKRVLELE 211
|
....*....
gi 383847295 1343 KGRMAEYDH 1351
Cdd:COG2884 212 DGRLVRDEA 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1143-1357 |
1.28e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 122.90 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1143 RYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRRHISIIPQDPVLF 1221
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVsEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1222 SGTLRRNL---DPfnefsdAALWEVLEEV----ELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILML 1294
Cdd:PRK10789 402 SDTVANNIalgRP------DATQQEIEHVarlaSVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1295 DEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEY-DHPHMLLQ 1357
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRgNHDQLAQQ 539
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1135-1346 |
1.58e-28 |
|
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: 113.26 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSIClEDLRRHISI 1213
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSG-TLRRNLDpfnefsdaalwevleevelkdavvisgnglesrvldrgsnYSVGQRQLVCLARAILRNNKIL 1292
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1293 MLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRM 1346
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
502-637 |
3.91e-28 |
|
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: 111.20 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVF-GSTVRQNI 567
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 568 LFGQpyDRHRYQKVVKACSLLRDFKQFPQSDQ--TVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLS 637
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1131-1346 |
7.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.70 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1131 KDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSS---LISALFRLAKveGVIEIDDIDTGSICLEDL 1207
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQS--GEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDP------------VLFsGTLRRNLDPfNEFSDAALwEVLEEVELKDAvvisgnglesrvLDRGS-NYSVG 1274
Cdd:PRK13632 82 RKKIGIIFQNPdnqfigatveddIAF-GLENKKVPP-KKMKDIID-DLAKKVGMEDY------------LDKEPqNLSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1275 QRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRM 1346
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
502-684 |
3.36e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.68 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNIL 568
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FgqPYD-RHRYQKVVKACSLLRDFkQFPQS--DQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSK 645
Cdd:COG4619 96 F--PFQlRERKFDRERALELLERL-GLPPDilDKPV-----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-NT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 383847295 646 HLFEECIQRYLA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:COG4619 167 RRVEELLREYLAeeGRAVLWVSHDPEQIERVaDRVLTLEAGR 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1134-1359 |
6.37e-27 |
|
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: 110.84 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEID--DIDTGSIC-LEDLRR 1209
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPdSGEILVDgqDITGLSEKeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1210 HISIIPQDPVLFSG-T--------LRRNLD-PFNEFSDAALwEVLEEVELKDAVV-----ISGnglesrvldrgsnysvG 1274
Cdd:COG1127 83 RIGMLFQGGALFDSlTvfenvafpLREHTDlSEAEIRELVL-EKLELVGLPGAADkmpseLSG----------------G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1275 QRQLVCLARAILRNNKILMLDEATANVDPQT----DALIQnTIRRKFtKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEY 1349
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITsaviDELIR-ELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
250
....*....|
gi 383847295 1350 DHPHMLLQNT 1359
Cdd:COG1127 224 GTPEELLASD 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1138-1346 |
8.74e-27 |
|
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: 108.29 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1138 RNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRHISIIPQ 1216
Cdd:cd03214 3 ENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1217 dpvlfsgtlrrnldpfnefsdaalweVLEEVELKDavvisgngLESRVLDRGSNysvGQRQLVCLARAILRNNKILMLDE 1296
Cdd:cd03214 81 --------------------------ALELLGLAH--------LADRPFNELSG---GERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 1297 ATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLN-TIMDSDKVLVMDKGRM 1346
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
484-684 |
1.07e-26 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 109.51 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGqSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLS 550
Cdd:cd03244 3 IEFKNVSLRYRPN-LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 551 YAGQEAWVFGSTVRQNI-LFGQpYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADV 629
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 630 YLLDDPLSAVDTHvSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:cd03244 161 LVLDEATASVDPE-TDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGR 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1135-1345 |
1.42e-26 |
|
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: 109.12 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAE--EELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDL---- 1207
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQD---------------PVLFSGTLRRnldpfnEFSDAALwEVLEEVelkdavvisgnGLESRVLDRGSNYS 1272
Cdd:cd03255 81 RRHIGFVFQSfnllpdltalenvelPLLLAGVPKK------ERRERAE-ELLERV-----------GLGDRLNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1273 VGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMDSDKVLVMDKGR 1345
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
502-684 |
5.41e-26 |
|
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: 105.40 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGslsyagqeawvfgstvrqnilfgQPYDRHRYQKV 581
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-----------------------KDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 582 VKACSLLrdfkqfPQsdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHLFEECIQRYLA-GKT 660
Cdd:cd00267 72 RRRIGYV------PQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLRELAEeGRT 132
|
170 180
....*....|....*....|....*
gi 383847295 661 RILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd00267 133 VIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1135-1345 |
7.85e-26 |
|
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: 105.73 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEID--DIDTGSICLEDLRRHI 1211
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSgtlrrNLDpfnefsdaalweVLEEVELkdavvisgnGLesrvldrgsnySVGQRQLVCLARAILRNNKI 1291
Cdd:cd03229 79 GMVFQDFALFP-----HLT------------VLENIAL---------GL-----------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1292 LMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
502-683 |
1.43e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.10 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG--------SLSYAGQEA---WVFGSTVRQNILFG 570
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAevdWDFPITVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 --------QPYDRHRYQKVVKACSL--LRDFKQFPqsdqtvVGErgssLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEALERvgLEDLADRP------IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 641 tHVSKHLFEECIQRYLA-GKTRILATHQLQYV-KNVDAIILIEQG 683
Cdd:COG1121 172 -AATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLLNRG 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1134-1348 |
1.60e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 109.40 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRY--AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSIC---LEDL 1207
Cdd:COG1135 1 MIELENLSKTFptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLVDGVDLTALSereLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPVLFSgtlRRNldpfnefsdaalweVLEEVEL------KDAVVIsgnglESRVL---------DRGSNY- 1271
Cdd:COG1135 81 RRKIGMIFQHFNLLS---SRT--------------VAENVALpleiagVPKAEI-----RKRVAellelvglsDKADAYp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1272 ---SVGQRQLVCLARAiLRNN-KILMLDEATANVDPQTD----ALIQNtIRRKFtKCTVLTIAHRLNTIMD-SDKVLVMD 1342
Cdd:COG1135 139 sqlSGGQKQRVGIARA-LANNpKVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVLE 215
|
....*.
gi 383847295 1343 KGRMAE 1348
Cdd:COG1135 216 NGRIVE 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
502-705 |
2.02e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 113.66 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNIL 568
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FG-QPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHL 647
Cdd:TIGR00958 577 YGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 648 FEEciqRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELL 705
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
502-684 |
3.01e-25 |
|
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: 106.10 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLSYAGQEAWVF-GSTVRQNI- 567
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYdRLTVRENIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDThVSKHL 647
Cdd:COG4555 97 YFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARRL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 383847295 648 FEECIQRYLA-GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:COG4555 171 LREILRALKKeGKTVLFSSHIMQEVEALcDRVVILHKGK 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
484-684 |
3.17e-25 |
|
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: 105.63 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-------------LS 550
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 551 YAGQEAWVFGSTVRQNILFGQPydRHRYQKVVKACSLLR--DF-KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQA 627
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQKAHahSFiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 628 DVYLLDDPLSAVDTHvSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:cd03248 170 QVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
490-668 |
3.69e-25 |
|
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: 111.68 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 490 TAKWEPGQSenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-------------LSYAGQEA 556
Cdd:TIGR02868 341 SAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 557 WVFGSTVRQNILFGQP-YDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDP 635
Cdd:TIGR02868 419 HLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 383847295 636 LSAVDTHVSKHLFEECIQRyLAGKTRILATHQL 668
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1134-1348 |
4.52e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.13 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYA--EEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSIC---LEDL 1207
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSereLARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RR-HISIIPQD---------------PVLFSGTLRRNldpfnefSDAALWEVLEEVelkdavvisgnGLESRVLDRGSNY 1271
Cdd:COG1136 84 RRrHIGFVFQFfnllpeltalenvalPLLLAGVSRKE-------RRERARELLERV-----------GLGDRLDHRPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1272 SVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1135-1350 |
6.51e-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: 104.14 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAkvEGVIEIDDIDTGSICLEdlRRHI 1211
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLlrlIAGLERPD--SGEILIDGRDVTGVPPE--RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLF----------SGtLRRNLDPFNEFSDAALwEVLEEVELkdavvisgngleSRVLDRgsnY----SVGQRQ 1277
Cdd:cd03259 75 GMVFQDYALFphltvaeniaFG-LKLRGVPKAEIRARVR-ELLELVGL------------EGLLNR---YphelSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYD 1350
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
495-684 |
7.85e-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: 103.70 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYAGQEAW--------------VF 559
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkDLTKLSLKELrrkvglvfqnpddqFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 560 GSTVRQNILFG---QPYDRH-RYQKVVKACSL--LRDF-KQFPQsdqtvvgergsSLSGGQKARINLARSLYRQADVYLL 632
Cdd:cd03225 90 GPTVEEEVAFGlenLGLPEEeIEERVEEALELvgLEGLrDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 633 DDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1134-1315 |
1.45e-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: 102.94 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTgSICLEDLRRHIS 1212
Cdd:COG4133 2 MLEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpSAGEVLWNGEPI-RDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSG-TLRRNLDpF------NEFSDAALWEVLEEVelkdavvisgnGLESRVLDRGSNYSVGQRQLVCLARAI 1285
Cdd:COG4133 79 YLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190
....*....|....*....|....*....|
gi 383847295 1286 LRNNKILMLDEATANVDPQTDALIQNTIRR 1315
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
495-704 |
1.85e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.11 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG---------SL----SYAGQEAWVFGS 561
Cdd:PRK11176 352 PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaSLrnqvALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILF--GQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAV 639
Cdd:PRK11176 432 TIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 640 DTHVskhlfEECIQRYLA----GKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAEL 704
Cdd:PRK11176 512 DTES-----ERAIQAALDelqkNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1150-1344 |
1.91e-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: 103.00 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDtgsicLEDLRRHISIIPQ------------ 1216
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKP-----LEKERKRIGYVPQrrsidrdfpisv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1217 -DPVLFSGTLRRNLDPFNEFSD-AALWEVLEEVELKDavvisgngLESRVLdrgSNYSVGQRQLVCLARAILRNNKILML 1294
Cdd:cd03235 88 rDVVLMGLYGHKGLFRRLSKADkAKVDEALERVGLSE--------LADRQI---GELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1295 DEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMDS-DKVLVMDKG 1344
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
502-684 |
4.10e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 102.45 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLSYAGQEAWVFGS-TVRQNI- 567
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 ----LFGQPYD--RHRYQKVVKACSLlRDFKqfpqsdqtvvGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:COG1131 96 ffarLYGLPRKeaRERIDELLELFGL-TDAA----------DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 642 hVSKHLFEECIQRYLA-GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:COG1131 165 -EARRELWELLRELAAeGKTVLLSTHYLEEAERLcDRVAIIDKGR 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1132-1328 |
5.02e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1132 DGMIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALfrlAkvegviEIDDIDTGSICLEDLRRhI 1211
Cdd:COG4178 360 DGALALEDLTLRTPDGR-PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI---A------GLWPYGSGRIARPAGAR-V 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSGTLRRNL---DPFNEFSDAALWEVLEEVELKDavvisgngLESRvLDRGSNY----SVGQRQLVCLARA 1284
Cdd:COG4178 429 LFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH--------LAER-LDEEADWdqvlSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 1285 ILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHR 1328
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1135-1352 |
7.15e-24 |
|
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: 101.88 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSI---CLEDLRRH 1210
Cdd:cd03256 1 IEVENLSKTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTDINKLkgkALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDP-----------VLfSGTL-RRNLDP--FNEFSDAalwEVLEEVELKDAVvisgnGLESRVLDRGSNYSVGQR 1276
Cdd:cd03256 80 IGMIFQQFnlierlsvlenVL-SGRLgRRSTWRslFGLFPKE---EKQRALAALERV-----GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTK--CTVLTIAHRLNTIMD-SDKVLVMDKGRMAeYDHP 1352
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREyADRIVGLKDGRIV-FDGP 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
495-688 |
8.46e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 107.53 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGS 561
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNI-LFGQPYDrhryQKVVKACSL-------LRdfkqFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLD 633
Cdd:COG4618 421 TIAENIaRFGDADP----EKVVAAAKLagvhemiLR----LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 634 DPLSAVDTHVSKHLFeECIQRyL--AGKTRILATHQLQYVKNVDAIILIEQGKATVF 688
Cdd:COG4618 493 EPNSNLDDEGEAALA-AAIRA-LkaRGATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
93-359 |
1.83e-23 |
|
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: 101.95 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 93 VVLGLMQILNEFvIRLGTPILLGGLLRYFRKSTDETYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVV 172
Cdd:pfam00664 2 ILAILLAILSGA-ISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 173 YRKALRLSKTALGETAPGKVVNLVANDVNRFDLVSIFIHHMWSAPLS---ALIIAYFLYTeaGYAGLIGIAAVFVVVPIQ 249
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLAtivGGIIVMFYYG--WKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 250 SYTGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFN-LFTTRM 328
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITqFIGYLS 238
|
250 260 270
....*....|....*....|....*....|..
gi 383847295 329 ALFCTLISMLL-FGNELSADKVFVFSSYFNIL 359
Cdd:pfam00664 239 YALALWFGAYLvISGELSVGDLVAFLSLFAQL 270
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
497-683 |
2.65e-23 |
|
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: 99.53 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 497 QSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG--------SLSYAGQEA---WVFGSTVRQ 565
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRsidRDFPISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 566 NIL--------FGQPYDRHRYQKVVKACSL--LRDFKQfpqsdqtvvgERGSSLSGGQKARINLARSLYRQADVYLLDDP 635
Cdd:cd03235 90 VVLmglyghkgLFRRLSKADKAKVDEALERvgLSELAD----------RQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 383847295 636 LSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYV-KNVDAIILIEQG 683
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
495-704 |
2.90e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.06 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGS 561
Cdd:PRK11160 349 PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILFGQPY-DRHRYQKVVKACSLlRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:PRK11160 429 TLRDNLLLAAPNaSDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 641 THVSKH----LFEECiqrylAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAEL 704
Cdd:PRK11160 508 AETERQilelLAEHA-----QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
502-684 |
3.90e-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: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLSYAGQEAWVFGS-TVRQNIl 568
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 fgqpydrhryqkvvkacsllrdfkqfpqsdqtvvgergsSLSGGQKARINLARSLYRQADVYLLDDPLSAVDThVSKHLF 648
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREF 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 383847295 649 EECIQRYLA-GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03230 135 WELLRELKKeGKTILLSSHILEEAERLcDRVAILNNGR 172
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1130-1348 |
5.85e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.78 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1130 PKDGMIRFRNVYMRYAEE--ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDtgsicLED 1206
Cdd:COG1116 3 AAAPALELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtSGEVLVDGKP-----VTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDPVLFs-gTLRRN----LD----PFNEFSDAALwEVLEEVELKDAV-----VISGnglesrvldrgsnys 1272
Cdd:COG1116 78 PGPDRGVVFQEPALLpwlTVLDNvalgLElrgvPKAERRERAR-ELLELVGLAGFEdayphQLSG--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1273 vGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAH------RLntimdSDKVLVMDK- 1343
Cdd:COG1116 142 -GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
....*.
gi 383847295 1344 -GRMAE 1348
Cdd:COG1116 216 pGRIVE 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
495-686 |
8.63e-23 |
|
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: 97.00 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS------------LSYAGQEAWVFGST 562
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNIlfgqpydrhryqkvvkacsllrdfkqfpqsdqtvvgerGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTH 642
Cdd:cd03247 91 LRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 643 VSKHLFEECIQrYLAGKTRILATHQLQYVKNVDAIILIEQGKAT 686
Cdd:cd03247 133 TERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
988-1341 |
9.92e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 106.27 E-value: 9.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 988 LNGLTTIRAYCAQDILKKEFDK--------------LQDVHTSTVYMYVVSSSGFGFSldifcfvFTSLVTFSFLLLEQS 1053
Cdd:PTZ00265 243 LVGIRTVVSYCGEKTILKKFNLseklyskyilkanfMESLHIGMINGFILASYAFGFW-------YGTRIIISDLSNQQP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1054 ---FSGGEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVERVLEYTNIPPEPNLRDRGKFAKKSEKqialpanapknwp 1130
Cdd:PTZ00265 316 nndFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKK------------- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1131 kdgmIRFRNVYMRY-AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDI-DTGSICLEDL 1207
Cdd:PTZ00265 383 ----IQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIINDShNLKDINLKWW 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPVLFSGTLRRNL--------------DPFNE--------------------------------------- 1234
Cdd:PTZ00265 459 RSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemr 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1235 -----FSDAALWEVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALI 1309
Cdd:PTZ00265 539 knyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
410 420 430
....*....|....*....|....*....|....*
gi 383847295 1310 QNTI---RRKFTKCTVLtIAHRLNTIMDSDKVLVM 1341
Cdd:PTZ00265 619 QKTInnlKGNENRITII-IAHRLSTIRYANTIFVL 652
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
495-685 |
1.12e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.52 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-------------LSYAGQEAWVFGS 561
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILfgqpydrhryqkvvkacsllrdfkqfpqsdqtvvgergsslSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:cd03246 91 SIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 642 HVSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKA 685
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1135-1358 |
1.24e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.96 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL------AKVEGVIEIDDID--TGSICLED 1206
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgARVEGEILLDGEDiyDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDPVLFSGTLRRN---------------LDPFNEFS--DAALWEvleEVE--LKDavviSGNGLesrvldr 1267
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNvayglrlhgikskseLDEIVEESlrKAALWD---EVKdrLKK----SALGL------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1268 gsnySVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRlntiMD-----SDKVLVMD 1342
Cdd:COG1117 156 ----SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFY 227
|
250
....*....|....*.
gi 383847295 1343 KGRMAEYDHPHMLLQN 1358
Cdd:COG1117 228 LGELVEFGPTEQIFTN 243
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1135-1347 |
2.70e-22 |
|
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: 94.80 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFrlakveGVIEIDDidtGSIcledlrrhisii 1214
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS------GLYKPDS---GEI------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1215 pqdpvLFSGTLRRNLDPfnefSDAAlwevleevELKDAVVisgnglesrvldrgSNYSVGQRQLVCLARAILRNNKILML 1294
Cdd:cd03216 58 -----LVDGKEVSFASP----RDAR--------RAGIAMV--------------YQLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1295 DEATANVDPQ-TDALIqNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMA 1347
Cdd:cd03216 107 DEPTAALTPAeVERLF-KVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
502-667 |
3.11e-22 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 96.39 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLSYAGQEAWVFGS-TVRQNIL 568
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 F-----GQPYDRHRYQKVVKACSL--LRDfkqfpqsdqtvvgERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLagLAD-------------LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|....*..
gi 383847295 642 HvSKHLFEECIQRYLA-GKTRILATHQ 667
Cdd:COG4133 165 A-GVALLAELIAAHLArGGAVLLTTHQ 190
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1134-1391 |
3.40e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.14 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAKveGVIEIDDIDTGSIC-LEDLRR 1209
Cdd:PRK13644 1 MIRLENVSYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQK--GKVLVSGIDTGDFSkLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1210 HISIIPQDP-VLFSGtlrRNLDPFNEFSDAALweVLEEVELKDAV--VISGNGLESRVLDRGSNYSVGQRQLVCLARAIL 1286
Cdd:PRK13644 78 LVGIVFQNPeTQFVG---RTVEEDLAFGPENL--CLPPIEIRKRVdrALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1287 RNNKILMLDEATANVDPQTDALIQNTIRRKFTKC-TVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQNTYSQFTS 1365
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
250 260
....*....|....*....|....*.
gi 383847295 1366 LVKETdramfdqLVRIAKQsyIAKHG 1391
Cdd:PRK13644 233 LTPPS-------LIELAEN--LKMHG 249
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1134-1349 |
3.94e-22 |
|
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: 98.97 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYA--EEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL----AKVEGVIEIDDIDTGSICLEDL 1207
Cdd:COG0444 1 LLEVRNLKVYFPtrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 R----RHISIIPQD------PVL-----FSGTLRRNLDpfneFSDAALW----EVLEEVELKDAvvisgngleSRVLDRg 1268
Cdd:COG0444 81 RkirgREIQMIFQDpmtslnPVMtvgdqIAEPLRIHGG----LSKAEAReraiELLERVGLPDP---------ERRLDR- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1269 snY----SVGQRQLVCLARAILRNNKILMLDEATANVdpqtDALIQ-------NTIRRKFtKCTVLTIAHRLNTI--MdS 1335
Cdd:COG0444 147 --YphelSGGMRQRVMIARALALEPKLLIADEPTTAL----DVTIQaqilnllKDLQREL-GLAILFITHDLGVVaeI-A 218
|
250
....*....|....
gi 383847295 1336 DKVLVMDKGRMAEY 1349
Cdd:COG0444 219 DRVAVMYAGRIVEE 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
484-690 |
4.81e-22 |
|
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: 95.56 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPgQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLS 550
Cdd:cd03369 7 IEVENLSVRYAP-DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 551 YAGQEAWVFGSTVRQNIlfgQPYDRHRYQKVVKACSllrdfkqfpqsdqtvVGERGSSLSGGQKARINLARSLYRQADVY 630
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 631 LLDDPLSAVDTHvSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSH 690
Cdd:cd03369 148 VLDEATASIDYA-TDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1135-1357 |
5.34e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.78 E-value: 5.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDP-VLFSGTLRRNLDPFN-EFSDAALWEVLEEVElkDAV--VisgnGLESRVLDRGSNYSVGQRQLVCLARAILRNN 1289
Cdd:PRK13635 86 VFQNPdNQFVGATVQDDVAFGlENIGVPREEMVERVD--QALrqV----GMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1290 KILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMDSDKVLVMDKGR-MAE------YDHPHMLLQ 1357
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEiLEEgtpeeiFKSGHMLQE 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1135-1346 |
5.95e-22 |
|
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: 95.65 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIDDIDTGSiCLEDLRRHISI 1213
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSG-TLRRNLDPFNEFSDAALWEVLEEVELkdavVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKIL 1292
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYARLKGLPKSEIKEEVEL----LLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1293 MLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRlntiMD-----SDKVLVMDKGRM 1346
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHS----MDeaealCDRIAIMSDGKL 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1148-1358 |
1.45e-21 |
|
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: 94.81 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1148 ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDID-TGSICLEDLRRHISIIPQDPVLFSG-T 1224
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1225 LRRNLD-----PFNEFSDAALWEVLEEVELkdavvisgngLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATA 1299
Cdd:cd03224 92 VEENLLlgayaRRRAKRKARLERVYELFPR----------LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1300 NVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQN 1358
Cdd:cd03224 162 GLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1135-1346 |
1.81e-21 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 94.40 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSI---CLEDLRRH 1210
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLfsgtlrrnLDPFNEFSDAAL-WEVLE----EVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAI 1285
Cdd:cd03292 80 IGVVFQDFRL--------LPDRNVYENVAFaLEVTGvpprEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 1286 LRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMD--SDKVLVMDKGRM 1346
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
502-684 |
3.03e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 92.50 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKvngslsyagqeawvfgstvrqniLFGQPYDRHRYQKV 581
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----------------------LDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 582 VKACSLLrdfkqfPQS-DQTVVG---ERG-SSLSGGQKARINLARSLYRQADVYLLDDPLSAVD----THVSKHLFEECI 652
Cdd:cd03214 72 ARKIAYV------PQAlELLGLAhlaDRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLAR 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 383847295 653 QRylaGKTRILATHQL----QYvknVDAIILIEQGK 684
Cdd:cd03214 146 ER---GKTVVMVLHDLnlaaRY---ADRVILLKDGR 175
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1135-1346 |
5.58e-21 |
|
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: 92.67 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSicLEDLRRHISI 1213
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQK--NIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSG-TLRRNLDPFNE---FSDAALWEVLEEVELKDAvvisgnglESRvldRGSNYSVGQRQLVCLARAILRNN 1289
Cdd:cd03268 77 LIEAPGFYPNlTARENLRLLARllgIRKKRIDEVLDVVGLKDS--------AKK---KVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1290 KILMLDEATANVDPQTDALIQNTIRRKFTK-CTVLTIAHRLNTIMD-SDKVLVMDKGRM 1346
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKL 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
502-666 |
6.18e-21 |
|
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: 92.58 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-----------SLSYAGQEAWVFGS-TVRQNILF 569
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDYALFPHlTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 G-------QPYDRHRYQKVVKACSLLRDFKQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTH 642
Cdd:cd03259 96 GlklrgvpKAEIRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180
....*....|....*....|....*.
gi 383847295 643 VSKHLFEEcIQRYLA--GKTRILATH 666
Cdd:cd03259 165 LREELREE-LKELQRelGITTIYVTH 189
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1134-1348 |
6.39e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.02 E-value: 6.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRY--AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDL--- 1207
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERpTSGRVLVDGQDLTALSEKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPVLFSgtlRRNLdpfneFSDAAL------W---EVLEEV-ELKDAVvisgnGLESRVLDRGSNYSVGQRQ 1277
Cdd:PRK11153 81 RRQIGMIFQHFNLLS---SRTV-----FDNVALplelagTpkaEIKARVtELLELV-----GLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTD----ALIQNtIRRKFtKCTVLTIAHRlntiMD-----SDKVLVMDKGRMAE 1348
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTrsilELLKD-INREL-GLTIVLITHE----MDvvkriCDRVAVIDAGRLVE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1135-1345 |
9.80e-21 |
|
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: 92.21 E-value: 9.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDD--IDTGSICLEDLRRHI 1211
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIDGlkLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSgtlrrNLDpfnefsdaalweVLEEVEL---------KDAVVISGNGLESRV--LDRGSNY----SVGQR 1276
Cdd:cd03262 79 GMVFQQFNLFP-----HLT------------VLENITLapikvkgmsKAEAEERALELLEKVglADKADAYpaqlSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGR 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1134-1345 |
2.84e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAE---EELPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAkvEGVIEIDDID-TGsicLED 1206
Cdd:COG1101 1 MLELKNLSKTFNPgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLlnaIAGSLPPD--SGSILIDGKDvTK---LPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRR--HISIIPQDPV------------------------LFSGTLRRNLDPFNEfsdaalwevleevELKDAvvisGNGL 1260
Cdd:COG1101 76 YKRakYIGRVFQDPMmgtapsmtieenlalayrrgkrrgLRRGLTKKRRELFRE-------------LLATL----GLGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1261 ESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALI----QNTIRRKftKCTVLTIAHRLNTIMD-S 1335
Cdd:COG1101 139 ENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTHNMEQALDyG 216
|
250
....*....|
gi 383847295 1336 DKVLVMDKGR 1345
Cdd:COG1101 217 NRLIMMHEGR 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1135-1348 |
3.68e-20 |
|
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: 90.61 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRY--AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDtgsicLEDLRRHI 1211
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFS----------GtLRRNLDPFNEFSDAALwEVLEEVELKDAvvisgnglESRvldrgsnY----SVGQRQ 1277
Cdd:cd03293 76 GYVFQQDALLPwltvldnvalG-LELQGVPKAEARERAE-ELLELVGLSGF--------ENA-------YphqlSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTDALIQN---TIRRKfTKCTVLTIAHRLN-TIMDSDKVLVMDK--GRMAE 1348
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEellDIWRE-TGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
502-684 |
4.04e-20 |
|
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: 89.17 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVkvngslsyagqeaWVFGSTVRQNILFGQPYDRH-RYqk 580
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-------------LIDGEDLTDLEDELPPLRRRiGM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 581 vvkacsLLRDFKQFPQsdQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHlfeecIQRYLA--- 657
Cdd:cd03229 81 ------VFQDFALFPH--LTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE-----VRALLKslq 147
|
170 180 190
....*....|....*....|....*....|.
gi 383847295 658 ---GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03229 148 aqlGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
502-684 |
4.24e-20 |
|
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: 90.24 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSaILGEIDVV-EGHVKVNG-SLSYAGQEAW----------VFGS-------T 562
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtDISKLSEKELaafrrrhigfVFQSfnllpdlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGQPYDRHRY-QKVVKACSLLRDF------KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDP 635
Cdd:cd03255 99 ALENVELPLLLAGVPKkERRERAEELLERVglgdrlNHYP-----------SELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 636 LSAVDTHVSK---HLFEEcIQRyLAGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:cd03255 168 TGNLDSETGKevmELLRE-LNK-EAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
502-684 |
4.90e-20 |
|
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: 91.26 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWV-FGSTVRQNI 567
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFGqpydRHRYQKVvkacsllrdFKQFPQSDQTVVGE------------RG-SSLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:COG1120 97 ALG----RYPHLGL---------FGRPSAEDREAVEEalertglehladRPvDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 635 PLSAVDTHvskHLFE--ECIQRyLA---GKTRILATHQL----QYvknVDAIILIEQGK 684
Cdd:COG1120 164 PTSHLDLA---HQLEvlELLRR-LArerGRTVVMVLHDLnlaaRY---ADRLVLLKDGR 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1134-1345 |
5.95e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.20 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELpvlkGLNLVINPGEKIGIVGRTGAGKSSLISAL--FrlakvegvieiDDIDTGSICL--EDL-- 1207
Cdd:COG3840 1 MLRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIagF-----------LPPDSGRILWngQDLta 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 ----RRHISIIPQDPVLFSG-TLRRN----LDP---FNEFSDAALWEVLEEVELkdavvisgNGLESRvldRGSNYSVGQ 1275
Cdd:COG3840 66 lppaERPVSMLFQENNLFPHlTVAQNiglgLRPglkLTAEQRAQVEQALERVGL--------AGLLDR---LPGQLSGGQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1276 RQLVCLARAILRNNKILMLDEATANVDPqtdALIQ------NTIRRKfTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDP---ALRQemldlvDELCRE-RGLTVLMVTHDPEDAARiADRVLLVADGR 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
502-694 |
8.68e-20 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 89.70 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------SLSYAGQ---------EAWVFGSTVRQN 566
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRkvglvfqnpDDQLFAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 567 ILFG-----QPYD--RHRYQKVVKACSL--LRDfkQFPQSdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLS 637
Cdd:COG1122 97 VAFGpenlgLPREeiRERVEEALELVGLehLAD--RPPHE-----------LSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 638 AVDtHVSKHLFEECIQRY-LAGKTRILATHQLQYV-KNVDAIILIEQGK-------ATVFSHYQDL 694
Cdd:COG1122 164 GLD-PRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRivadgtpREVFSDYELL 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1134-1345 |
1.12e-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: 90.14 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFR-LAKVEG-VIEIDDIDTGSICLEDLRRHI 1211
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SII---------PQDPVL------FSGTLRRnldpFNEFSDAAL---WEVLEEVELKDavvisgngLESRVLDRgsnYSV 1273
Cdd:COG1119 81 GLVspalqlrfpRDETVLdvvlsgFFDSIGL----YREPTDEQReraRELLELLGLAH--------LADRPFGT---LSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1274 GQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMDS-DKVLVMDKGR 1345
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
502-668 |
1.15e-19 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 89.07 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG--------SLSYAGQEAWVFG-STVRQNILFG-- 570
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDALLPwLTVLDNVALGle 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 --QPYDRHRYQKVVKACSL--LRDF-KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSK 645
Cdd:cd03293 100 lqGVPKAEARERAEELLELvgLSGFeNAYP-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTRE 168
|
170 180
....*....|....*....|....*....
gi 383847295 646 HLfeeciQRYL------AGKTRILATHQL 668
Cdd:cd03293 169 QL-----QEELldiwreTGKTVLLVTHDI 192
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
846-1096 |
1.23e-19 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 91.12 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 846 YIYTAIVVGLFCI-GITRSLTFYEVCIV---CSQKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELlpkavl 921
Cdd:cd18559 38 QVYLSVLGALAILqGITVFQYSMAVSIGgifASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSM------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 922 dAGQICMMMFGSLAVS---CI----VNPLFLIpIVFLGTVFYWIRKVYLKTSKNIKRLEGMSRSPVFTHLNATLNGLTTI 994
Cdd:cd18559 112 -APQVIKMWMGPLQNViglYLlillAGPMAAV-GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 995 RAYCAQDILKKEFDKLQDvHTSTVYMYVVSSSGFGFSLDIFCFVFTSLVTFSFLLLEQSFSgGEVGLAITQVMAMTGMIQ 1074
Cdd:cd18559 190 KAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLA-GLVALKVFYSLALTTYLN 267
|
250 260
....*....|....*....|..
gi 383847295 1075 WGMRQNAEAANQMMAVERVLEY 1096
Cdd:cd18559 268 WPLNMSPEVITNIVAAEVSLER 289
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
502-679 |
1.48e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.15 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYAGQE-AWVFGS-------TVRQNILFGQP 572
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkPVTGPGPDrGVVFQEpallpwlTVLDNVALGLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 573 YDRH----RYQKVVKACSL--LRDF-KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDThVSK 645
Cdd:COG1116 107 LRGVpkaeRRERARELLELvgLAGFeDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDA-LTR 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 383847295 646 HLFEECIQRYLA--GKTRILATHqlqyvkNVD-AIIL 679
Cdd:COG1116 175 ERLQDELLRLWQetGKTVLFVTH------DVDeAVFL 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1133-1352 |
1.77e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAkvEGVIEIDDID-TGsicLEDLR 1208
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmIAGLEDPT--SGEILIGGRDvTD---LPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1209 RHISIIPQDPVLF-SGTLRRNLdpfnEFS-----------DAALWEVLEEVELKDavvisgnglesrVLDR-GSNYSVGQ 1275
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENI----AFPlklrkvpkaeiDRRVREAAELLGLED------------LLDRkPKQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1276 RQLVCLARAILRNNKILMLDEATANVDPQtdalIQNTIRRKFTKctvltIAHRLNTIM-----D-------SDKVLVMDK 1343
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAK----LRVEMRAEIKR-----LHRRLGTTTiyvthDqveamtlADRIAVMND 209
|
....*....
gi 383847295 1344 GRMAEYDHP 1352
Cdd:COG3839 210 GRIQQVGTP 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1140-1345 |
2.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1140 VYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDID-TG-SICLEDLRRHISIIPQ 1216
Cdd:PRK13637 11 IYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVDiTDkKVKLSDIRKKVGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1217 DP--VLFSGTLRRNLdpfnEFSDAALWevLEEVELKDAVVISGN--GLESRVLDRGSNY--SVGQRQLVCLARAILRNNK 1290
Cdd:PRK13637 91 YPeyQLFEETIEKDI----AFGPINLG--LSEEEIENRVKRAMNivGLDYEDYKDKSPFelSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKlADRIIVMNKGK 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1131-1353 |
2.71e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1131 KDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDLRR 1209
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1210 HISIIPQDP------------VLFSgtLRRNLDPFNEFSDAaLWEVLEEVELKDavvisgnglesRVLDRGSNYSVGQRQ 1277
Cdd:PRK13648 84 HIGIVFQNPdnqfvgsivkydVAFG--LENHAVPYDEMHRR-VSEALKQVDMLE-----------RADYEPNALSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTK-CTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPH 1353
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKvKSEHnITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1151-1347 |
3.06e-19 |
|
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: 87.63 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGeKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEdLRRHISIIPQDPVLFSG-TLRRN 1228
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPpSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1229 LDPF-------NEFSDAALWEVLEEVelkdavvisgnGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANV 1301
Cdd:cd03264 93 LDYIawlkgipSKEVKARVDEVLELV-----------NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 383847295 1302 DPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMDS-DKVLVMDKGRMA 1347
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLV 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1135-1363 |
4.27e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.13 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEIDDIDTGSICLEDLRRHISI 1213
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSG-TLRRN--LDP-----FNEFSDAALWEVLEEVELKDAvvisgnglesRVLDR-GSNYSVGQRQLVCLARA 1284
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkllkwPKEKIRERADELLALVGLDPA----------EFADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1285 ILRNNKILMLDEATANVDPQTDALIQN---TIRRKFTKcTVLTIAHRLN-TIMDSDKVLVMDKGRMAEYDHPHMLLQNTY 1360
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEefkRLQQELGK-TIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
...
gi 383847295 1361 SQF 1363
Cdd:cd03295 229 NDF 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
502-704 |
4.36e-19 |
|
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: 92.96 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG---------SLSYA-G---QEAWVFGSTVRQNIL 568
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaSLRAAiGivpQDTVLFNDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQP-YDRHRYQKVVKACSLlRDF-KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVskh 646
Cdd:COG5265 454 YGRPdASEEEVEAAARAAQI-HDFiESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT--- 529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 647 lfEECIQRYL----AGKTRILATHQLQYVKNVDAII------LIEQGkatvfSHyQDLLSQRPEYAEL 704
Cdd:COG5265 530 --ERAIQAALrevaRGRTTLVIAHRLSTIVDADEILvleagrIVERG-----TH-AELLAQGGLYAQM 589
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1149-1347 |
5.91e-19 |
|
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: 86.45 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1149 LPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAL---FRLAKVEGVIEIDDIDTGsicLEDLRRHISIIPQDPVLFSG-T 1224
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPTlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1225 LRRNLDpfneFSdaalwevleeVELKdavVISGnglesrvldrgsnysvGQRQLVCLARAILRNNKILMLDEATANVDPQ 1304
Cdd:cd03213 99 VRETLM----FA----------AKLR---GLSG----------------GERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 383847295 1305 TDALIQNTIRR-KFTKCTVLTIAHRLNTIMDS--DKVLVMDKGRMA 1347
Cdd:cd03213 146 SALQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
502-684 |
7.20e-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: 87.24 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGhVKVNGSLSYAGQEAW---------------VFGS----- 561
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG-APDEGEVLLDGKDIYdldvdvlelrrrvgmVFQKpnpfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 -TVRQNILFGQPY----DRHRYQKVVKAC----SLLRDFKqfpqsDQTvvgeRGSSLSGGQKARINLARSLYRQADVYLL 632
Cdd:cd03260 95 gSIYDNVAYGLRLhgikLKEELDERVEEAlrkaALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 633 DDPLSAVDThVSKHLFEECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03260 166 DEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGR 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1149-1344 |
1.32e-18 |
|
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: 86.23 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1149 LPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIDDIDTGSICLEDL----RRHISIIPQDPVLFSG 1223
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1224 TLRRNL---DPFNEFSDAAlweVLEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATAN 1300
Cdd:cd03290 94 TVEENItfgSPFNKQRYKA---VTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 383847295 1301 VDPQ-TDALIQNTIRR--KFTKCTVLTIAHRLNTIMDSDKVLVMDKG 1344
Cdd:cd03290 171 LDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1134-1347 |
1.79e-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: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELPV--LKGLNLVINPGEKIGIVGRTGAGKSS---LISALFRLAKveGVIEIDDIDTGSICLEdLR 1208
Cdd:cd03266 1 MITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTtlrMLAGLLEPDA--GFATVDGFDVVKEPAE-AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1209 RHISIIPQDPVLFSG-TLRRNLDPFnefsdAALWEvLEEVELKDAV--VISGNGLESRVLDRGSNYSVGQRQLVCLARAI 1285
Cdd:cd03266 78 RRLGFVSDSTGLYDRlTARENLEYF-----AGLYG-LKGDELTARLeeLADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1286 LRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMA 1347
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
501-707 |
2.26e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.96 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDNL-----------NLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSlSYAG------------QEAW 557
Cdd:COG3840 3 RLDDLtyrygdfplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-DLTAlppaerpvsmlfQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 558 VFGS-TVRQNILFG-QP---YDRHRYQKVVKACSL--LRDFKQ-FPqsdqtvvgergSSLSGGQKARINLARSLYRQADV 629
Cdd:COG3840 82 LFPHlTVAQNIGLGlRPglkLTAEQRAQVEQALERvgLAGLLDrLP-----------GQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 630 YLLDDPLSAVDTHVSK---HLFEECIQRYlaGKTRILATHQLQYVKNV-DAIILIEQGKATVFSHYQDLLSQRPeyAELL 705
Cdd:COG3840 151 LLLDEPFSALDPALRQemlDLVDELCRER--GLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGEP--PPAL 226
|
..
gi 383847295 706 AA 707
Cdd:COG3840 227 AA 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
502-710 |
3.17e-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: 85.82 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGS-TVRQNI 567
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 -----LFGqpYDRHRYQKVVKacSLLRDFKQFPQSdqtvVGERGSS-LSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:cd03295 97 alvpkLLK--WPKEKIRERAD--ELLALVGLDPAE----FADRYPHeLSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 642 HVSKHLFEEC--IQRYLaGKTRILATHQLQ-YVKNVDAIILIEQGKATVFSHYQDLL-SQRPEYAELLAAENE 710
Cdd:cd03295 169 ITRDQLQEEFkrLQQEL-GKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILrSPANDFVAEFVGADR 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
502-684 |
3.38e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 84.89 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAI--LGEIDvvEGHVKVNGSLSYAGQEAW---------VFGS-------TV 563
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNInelrqkvgmVFQQfnlfphlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RQNILFGQPYDRHRYQK--VVKACSLLRDFKQFPQSDQtvvgeRGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:cd03262 94 LENITLAPIKVKGMSKAeaEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 383847295 642 HVSKHLFEecIQRYLA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03262 169 ELVGEVLD--VMKDLAeeGMTMVVVTHEMGFAREVaDRVIFMDDGR 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
502-715 |
5.11e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.64 E-value: 5.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG---------QEAWVFGSTVRQNIL 568
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRASlrrniavvfQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQP--YDRHRYQKVVKACSLlrDF--KQfPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVS 644
Cdd:PRK13657 431 VGRPdaTDEEMRAAAERAQAH--DFieRK-PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 645 KHLfEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEYAELLAAENETHDDS 715
Cdd:PRK13657 508 AKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDE 577
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
496-684 |
6.92e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 84.54 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 496 GQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYA------GQEAWVFGS---- 561
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKalrqlrRQIGMIFQQfnli 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 ---TVRQNILFG------------QPYDRHRYQKvvkACSLLRDFKQFPQSDQtvvgeRGSSLSGGQKARINLARSLYRQ 626
Cdd:cd03256 91 erlSVLENVLSGrlgrrstwrslfGLFPKEEKQR---ALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 627 ADVYLLDDPLSAVDTHVSK---HLFEE-CIQRylaGKTRILATHQLQYVK-NVDAIILIEQGK 684
Cdd:cd03256 163 PKLILADEPVASLDPASSRqvmDLLKRiNREE---GITVIVSLHQVDLAReYADRIVGLKDGR 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
502-684 |
6.97e-18 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 84.48 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG------------QEAWVFGS-TVR 564
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisGLSEAElyrlrrrmgmlfQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILFgqpydrhryqkvvkacsLLRDFKQFPQSDQT--------VVGERG------SSLSGGQKARINLARSLYRQADVY 630
Cdd:cd03261 96 ENVAF-----------------PLREHTRLSEEEIReivlekleAVGLRGaedlypAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 631 LLDDPLSAVDThVSKHLFEECIQRYLA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03261 159 LYDEPTAGLDP-IASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIaDRIAVLYDGK 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1134-1380 |
9.57e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFrlakveGVIEIDdidTGSICLE-------- 1205
Cdd:COG1129 4 LLEMRGISKSFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILS------GVYQPD---SGEILLDgepvrfrs 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1206 --DLRRH-ISIIPQDPVL----------FSGTLRRN---LDPFNEFSDAAlwEVLEEVELKdavvISgngLESRVldrgS 1269
Cdd:COG1129 73 prDAQAAgIAIIHQELNLvpnlsvaeniFLGREPRRgglIDWRAMRRRAR--ELLARLGLD----ID---PDTPV----G 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1270 NYSVGQRQLVCLARAILRNNKILMLDEATANVDPQ-TDALIqNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRM 1346
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLF-RIIRRlKAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
250 260 270
....*....|....*....|....*....|....
gi 383847295 1347 AEydhphmllqntysqfTSLVKETDRamfDQLVR 1380
Cdd:COG1129 219 VG---------------TGPVAELTE---DELVR 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
502-684 |
1.34e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.97 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILG--EIDvvEGHVKVNGSLSYAG---QE---AWVFGS-------TVRQN 566
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGleTPD--SGRIVLNGRDLFTNlppRErrvGFVFQHyalfphmTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 567 ILFG---QPYDRHRYQKVVKacSLLRDF------KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLS 637
Cdd:COG1118 96 IAFGlrvRPPSKAEIRARVE--ELLELVqleglaDRYP-----------SQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 383847295 638 AVDTHVSKHLfEECIQRYLA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:COG1118 163 ALDAKVRKEL-RRWLRRLHDelGGTTVFVTHDQEEALELaDRVVVMNQGR 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1147-1362 |
2.00e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.43 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1147 EELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEID--DIDTGS-ICLEDLRRHISIIPQDPvlFS- 1222
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDgqDLDGLSrRALRPLRRRMQVVFQDP--FGs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1223 ---------------GTLRRNLDPfnEFSDAALWEVLEEVelkdavvisgnGLESRVLDRgsnY----SVGQRQLVCLAR 1283
Cdd:COG4172 375 lsprmtvgqiiaeglRVHGPGLSA--AERRARVAEALEEV-----------GLDPAARHR---YphefSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1284 AILRNNKILMLDEATAnvdpqtdAL---IQNTI---------RRKFtkcTVLTIAHRLNTI--MdSDKVLVMDKGRMAE- 1348
Cdd:COG4172 439 ALILEPKLLVLDEPTS-------ALdvsVQAQIldllrdlqrEHGL---AYLFISHDLAVVraL-AHRVMVMKDGKVVEq 507
|
250 260
....*....|....*....|
gi 383847295 1349 ------YDHPhmllQNTYSQ 1362
Cdd:COG4172 508 gpteqvFDAP----QHPYTR 523
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1124-1348 |
2.14e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.33 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1124 NAPKNWPKdgmIRFRNVYMRYAEEELPVlKGLNLVINPGEKIGIVGRTGAGKSS---LISALFRlaKVEGVIEIDDIDTG 1200
Cdd:PRK10522 315 QAFPDWQT---LELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTlamLLTGLYQ--PQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1201 SICLEDLRRHISIIPQDPVLFSgtlrRNLDPFNEFSDAALWEV-LEEVELKDAVVISGNglesRVLDrgSNYSVGQRQLV 1279
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDFHLFD----QLLGPEGKPANPALVEKwLERLKMAHKLELEDG----RISN--LKLSKGQKKRL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1280 CLARAILRNNKILMLDEATANVDPQtdaliqntIRRKFTKC----------TVLTIAHRLNTIMDSDKVLVMDKGRMAE 1348
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPH--------FRREFYQVllpllqemgkTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1151-1363 |
2.71e-17 |
|
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: 82.77 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLIsalfrlakvEGVIEIDDIDTGSICL--EDL------RRHISIIPQDPVLFS 1222
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLL---------ETIAGFIKPDSGKILLngKDItnlppeKRDISYVPQNYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1223 gtlrrNLDPFNEFSDAALWEVLEEVELKDAVV-ISGNGLESRVLDRG-SNYSVGQRQLVCLARAILRNNKILMLDEATAN 1300
Cdd:cd03299 85 -----HMTVYKNIAYGLKKRKVDKKEIERKVLeIAEMLGIDHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1301 VDPQTDALIQN---TIRRKFtKCTVLTIAHRLNTI-MDSDKVLVMDKGRMAEYDHPHMLLQNTYSQF 1363
Cdd:cd03299 160 LDVRTKEKLREelkKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1134-1347 |
4.26e-17 |
|
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: 81.95 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDL-RRHI 1211
Cdd:COG0410 3 MLEVENLHAGYGG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIRFDGEDITGLPPHRIaRLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSG-TLRRNLD--PFNEFSDAALWEVLEEV-----ELKDavvisgnglesRVLDRGSNYSVGQRQLVCLAR 1283
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgAYARRDRAEVRADLERVyelfpRLKE-----------RRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1284 AILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMA 1347
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1134-1352 |
5.73e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIDDIDTGSICLEDLRRHIS 1212
Cdd:PRK13548 2 MLEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVL-FSGTLRR----NLDPFNEFS---DAALWEVLEEVELKdavvisgnGLESRvldrgsNY---SVGQRQLVCL 1281
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEvvamGRAPHGLSRaedDALVAAALAQVDLA--------HLAGR------DYpqlSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1282 ARAILR------NNKILMLDEATANVDP--QtdaliQNTIR--RKFTK---CTVLTIAHRLN-TIMDSDKVLVMDKGRMA 1347
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLahQ-----HHVLRlaRQLAHergLAVIVVLHDLNlAARYADRIVLLHQGRLV 220
|
....*
gi 383847295 1348 EYDHP 1352
Cdd:PRK13548 221 ADGTP 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
502-684 |
6.12e-17 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 81.47 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG------------QEAWVFGS-TVR 564
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltLLSGKElrkarrrigmifQHFNLLSSrTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILF-----GQPyDRHRYQKVVKACSL--LRDFKQF-PqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPL 636
Cdd:cd03258 101 ENVALpleiaGVP-KAEIEERVLELLELvgLEDKADAyP-----------AQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 637 SAVD---THVSKHLFEEcIQRYLaGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03258 169 SALDpetTQSILALLRD-INREL-GLTIVLITHEMEVVKRIcDRVAVMEKGE 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
486-698 |
7.71e-17 |
|
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: 82.21 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 486 MTNFTAKWEPGqSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVvEGHVKVNG-------------SLSYA 552
Cdd:cd03289 5 VKDLTAKYTEG-GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGvswnsvplqkwrkAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 553 GQEAWVFGSTVRQNIlfgQPYDRHRYQ---KVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADV 629
Cdd:cd03289 83 PQKVFIFSGTFRKNL---DPYGKWSDEeiwKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 630 YLLDDPLSAVDThVSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQR 698
Cdd:cd03289 160 LLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
502-684 |
9.56e-17 |
|
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: 79.01 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGslsyagqeawvfgstvrQNILFGQPYDRHR---- 577
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFASPRDARRagia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 578 --YQkvvkacsllrdfkqfpqsdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEecIQRY 655
Cdd:cd03216 79 mvYQ-----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRR 127
|
170 180 190
....*....|....*....|....*....|..
gi 383847295 656 LA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03216 128 LRaqGVAVIFISHRLDEVFEIaDRVTVLRDGR 159
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1138-1348 |
1.06e-16 |
|
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: 80.94 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1138 RNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVegvieiddiDTGSICLEDlrRHISIIP-- 1215
Cdd:cd03219 4 RGLTKRFGG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP---------TSGSVLFDG--EDITGLPph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1216 -----------QDPVLFSG-TLRRNL-------------DPFNEFSDAALWE----VLEEVELkdavvisgngleSRVLD 1266
Cdd:cd03219 71 eiarlgigrtfQIPRLFPElTVLENVmvaaqartgsgllLARARREEREAREraeeLLERVGL------------ADLAD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1267 R-GSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQ-TDALIqNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMD 1342
Cdd:cd03219 139 RpAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLD 217
|
....*..
gi 383847295 1343 KGRM-AE 1348
Cdd:cd03219 218 QGRViAE 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
484-684 |
1.45e-16 |
|
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: 79.99 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEpgqSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSL-SYAGQE----AWV 558
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvTDLPPKdrdiAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 559 FGS-------TVRQNILFG-----QPYDRHRyQKVVKACSLLRDfkqfpqsdQTVVGERGSSLSGGQKARINLARSLYRQ 626
Cdd:cd03301 78 FQNyalyphmTVYDNIAFGlklrkVPKDEID-ERVREVAELLQI--------EHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 627 ADVYLLDDPLSAVDTHVSKHLFEEC--IQRYLaGKTRILATH-QLQYVKNVDAIILIEQGK 684
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELkrLQQRL-GTTTIYVTHdQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
484-684 |
1.53e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 80.24 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQSENT-LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAGQE--- 555
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 556 ---AWVF----GS-----TVRQNILfgQPYDRHRYQKVVKACS--LLRDFKQFPQSDQtVVGERGSSLSGGQKARINLAR 621
Cdd:cd03257 82 keiQMVFqdpmSSlnprmTIGEQIA--EPLRIHGKLSKKEARKeaVLLLLVGVGLPEE-VLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 622 SLYRQADVYLLDDPLSAVDTHVSK---HLFEECIQRYlaGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAqilDLLKKLQEEL--GLTLLFITHDLGVVAKIaDRVAVMYAGK 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
502-688 |
1.73e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 80.27 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSyagqeaWVFG--------STVRQNILFG--- 570
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLGlgggfnpeLTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 ----QPYDRHRYQKVVkACSLLRDFKQFPqsdqtvVGErgssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvskh 646
Cdd:cd03220 112 lglsRKEIDEKIDEII-EFSELGDFIDLP------VKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAA---- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 383847295 647 lF-EECIQRYLA----GKTRILATHQLQYVKNV-DAIILIEQGKATVF 688
Cdd:cd03220 177 -FqEKCQRRLREllkqGKTVILVSHDPSSIKRLcDRALVLEKGKIRFD 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
500-684 |
1.92e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 79.61 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 500 NTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----------SLSYAGQEA--WVFGSTVRQNI 567
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVdyQLFTDSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFGQPyDRHRYQKVVKAcsLLRDFK------QFPQSdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:cd03226 94 LLGLK-ELDAGNEQAET--VLKDLDlyalkeRHPLS-----------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 383847295 642 H----VSKhLFEECiqrYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03226 160 KnmerVGE-LIREL---AAQGKAVIVITHDYEFLAKVcDRVLLLANGA 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1137-1350 |
2.60e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1137 FRNVYMRYAEEELpvLKGLNLVINPGEKIGIVGRTGAGKSSLisalFRLakVEGVIEIDDidtGSICLE-DLRrhISIIP 1215
Cdd:COG0488 1 LENLSKSFGGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTL----LKI--LAGELEPDS---GEVSIPkGLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1216 QDPVLFSGT---------------LRRNLD------PFNEFSDAALWEVLEEVELKDA--------VVISGNGLESRVLD 1266
Cdd:COG0488 68 QEPPLDDDLtvldtvldgdaelraLEAELEeleaklAEPDEDLERLAELQEEFEALGGweaearaeEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1267 RG-SNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRkfTKCTVLTIAH-R--LNTImdSDKVLVMD 1342
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRV--ATRILELD 223
|
....*...
gi 383847295 1343 KGRMAEYD 1350
Cdd:COG0488 224 RGKLTLYP 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1134-1345 |
2.86e-16 |
|
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: 80.08 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDID-TG----SICLEDL 1207
Cdd:COG0411 4 LLEVRGLTKRFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPtSGRILFDGRDiTGlpphRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RR---HISIIPQDPVL---------------FSGTLR--RNLDPFNEFSDAAlWEVLEEVelkdavvisgnGLESRVLDR 1267
Cdd:COG0411 82 ARtfqNPRLFPELTVLenvlvaaharlgrglLAALLRlpRARREEREARERA-EELLERV-----------GLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1268 GSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQ-TDALIQnTIR--RKFTKCTVLTIAHRLNTIMD-SDKVLVMDK 1343
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRrlRDERGITILLIEHDMDLVMGlADRIVVLDF 228
|
..
gi 383847295 1344 GR 1345
Cdd:COG0411 229 GR 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1120-1353 |
3.21e-16 |
|
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: 83.69 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1120 ALPANAPKNWPKD-GMIRFRNVYMRYAEEELP---VLKGLNLVINPGEKIGIVGRTGAGKSS---LISALFRlaKVEGVI 1192
Cdd:COG4615 312 AAADAAAPPAPADfQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTlakLLTGLYR--PESGEI 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1193 EIDDIDTGSICLEDLRRHISIIPQDPVLFsgtlRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRvldrgsNYS 1272
Cdd:COG4615 390 LLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLELDHKVSVEDGRFSTT------DLS 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1273 VGQRQLVCLARAILRNNKILMLDEATANVDPQtdaliqntIRRKFT-----------KcTVLTIAHrlntimD------S 1335
Cdd:COG4615 460 QGQRKRLALLVALLEDRPILVFDEWAADQDPE--------FRRVFYtellpelkargK-TVIAISH------DdryfdlA 524
|
250
....*....|....*...
gi 383847295 1336 DKVLVMDKGRMAEYDHPH 1353
Cdd:COG4615 525 DRVLKMDYGKLVELTGPA 542
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
484-684 |
3.37e-16 |
|
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: 76.72 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQsenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVngslsyagqeawvfGSTV 563
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------GSTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RqnilfgqpydrhryqkvvkacsllrdFKQFPQsdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHv 643
Cdd:cd03221 64 K--------------------------IGYFEQ------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE- 104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 383847295 644 SKHLFEECIQRYlaGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03221 105 SIEALEEALKEY--PGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1134-1352 |
3.38e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAkvEGVIEIDDIDtgsicLEDL--- 1207
Cdd:COG3842 5 ALELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLlrmIAGFETPD--SGRILLDGRD-----VTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPVLFS----------GtLR-RNLDPfnEFSDAALWEVLEEVELKdavvisgnGLESRvldRGSNYSVGQR 1276
Cdd:COG3842 76 KRNVGMVFQDYALFPhltvaenvafG-LRmRGVPK--AEIRARVAELLELVGLE--------GLADR---YPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHrlntimD-------SDKVLVMDKGRMA 1347
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTH------DqeealalADRIAVMNDGRIE 215
|
250
....*....|..
gi 383847295 1348 E-------YDHP 1352
Cdd:COG3842 216 QvgtpeeiYERP 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1130-1348 |
3.70e-16 |
|
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: 79.40 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1130 PKDGMIRFRNVYMRY--AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLakvegvieiDDIDTGSICL--E 1205
Cdd:COG4181 4 SSAPIIELRGLTKTVgtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL---------DRPTSGTVRLagQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1206 DL------------RRHISIIPQD-PVLFSGT----------LRRNLDPFNEfsdAAlwEVLEEVelkdavvisgnGLES 1262
Cdd:COG4181 75 DLfaldedararlrARHVGFVFQSfQLLPTLTalenvmlpleLAGRRDARAR---AR--ALLERV-----------GLGH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1263 RVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTI----RRKFTkcTVLTIAHRLNTIMDSDKV 1338
Cdd:COG4181 139 RLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGT--TLVLVTHDPALAARCDRV 216
|
250
....*....|
gi 383847295 1339 LVMDKGRMAE 1348
Cdd:COG4181 217 LRLRAGRLVE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
502-684 |
4.48e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.94 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAGQEAW------VF-------GSTVR 564
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLKRREIPYLrrrigvVFqdfrllpDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILFG---QPYDRHRYQKVVKAcsLLRDF------KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDP 635
Cdd:COG2884 98 ENVALPlrvTGKSRKEIRRRVRE--VLDLVglsdkaKALP-----------HELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 636 LSAVDTHVSK---HLFEEcIQRylAGKTRILATHQLQYVKNVDA-IILIEQGK 684
Cdd:COG2884 165 TGNLDPETSWeimELLEE-INR--RGTTVLIATHDLELVDRMPKrVLELEDGR 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
502-680 |
4.49e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG--SLSYAGQ---EAWVFGSTVRQNILFG------ 570
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQrseVPDSLPLTVRDLVAMGrwarrg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 --QPYDRHRYQKVVKACSL--LRDFKqfpqsdqtvvGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKH 646
Cdd:NF040873 88 lwRRLTRDDRAAVDDALERvgLADLA----------GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE-SRE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 383847295 647 LFEECIQRYLA-GKTRILATHQLQYVKNVDAIILI 680
Cdd:NF040873 157 RIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1150-1328 |
6.19e-16 |
|
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: 76.81 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDidtgsicledlRRHISIIPQDPVLFSGTLRRN 1228
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRIGMPE-----------GEDLLFLPQRPYLPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1229 LdpfnefsdAALWevleevelkdavvisgngleSRVLdrgsnySVGQRQLVCLARAILRNNKILMLDEATANVDPQTDAL 1308
Cdd:cd03223 84 L--------IYPW--------------------DDVL------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|
gi 383847295 1309 IQNTIRRKFTkcTVLTIAHR 1328
Cdd:cd03223 130 LYQLLKELGI--TVISVGHR 147
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
502-699 |
6.27e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.98 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAI--LGEID----VVEGhVKVNG---SLSYAGQEA-WVFGS-------TVR 564
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdlIVDG-LKVNDpkvDERLIRQEAgMVFQQfylfphlTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILFGqPYdRHRYQKVVKACSLLRDFkqfpqsdQTVVG--ERG----SSLSGGQKARINLARSLYRQADVYLLDDPLSA 638
Cdd:PRK09493 96 ENVMFG-PL-RVRGASKEEAEKQAREL-------LAKVGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 639 VDTH-------VSKHLFEEciqrylaGKTRILATHQLQYVKNVDA-IILIEQGKATVFSHYQDLLSQRP 699
Cdd:PRK09493 167 LDPElrhevlkVMQDLAEE-------GMTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIKNPP 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1130-1359 |
6.41e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1130 PKDGMIRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSS---LISALFRL-AKVEGVIEIDDIDTGSICLE 1205
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPdDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1206 DLRRHISIIPQDPvlfsgtlrrnlDpfNEFSDAALwevleevelKDAVVIsgnGLESRVLDRG----------------- 1268
Cdd:PRK13640 81 DIREKVGIVFQNP-----------D--NQFVGATV---------GDDVAF---GLENRAVPRPemikivrdvladvgmld 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1269 ------SNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMDSDKVLV 1340
Cdd:PRK13640 136 yidsepANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLV 215
|
250
....*....|....*....
gi 383847295 1341 MDKGRMAEYDHPHMLLQNT 1359
Cdd:PRK13640 216 LDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
499-684 |
7.49e-16 |
|
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: 78.11 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 499 ENTLDNLNLEIE---KGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSL-----------------SYAGQEAWV 558
Cdd:cd03297 7 EKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 559 FGS-TVRQNILFGQPY-----DRHRYQKVVKACSLlrdfkqfpqsdQTVVGERGSSLSGGQKARINLARSLYRQADVYLL 632
Cdd:cd03297 87 FPHlNVRENLAFGLKRkrnreDRISVDELLDLLGL-----------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 633 DDPLSAVDTHVSKHLFEEcIQRYLA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03297 156 DEPFSALDRALRLQLLPE-LKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGR 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1134-1355 |
8.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEE-ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLIsalfRLakVEGVIEIDdidTGSICLE------- 1205
Cdd:PRK13650 4 IIEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTV----RL--IDGLLEAE---SGQIIIDgdlltee 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1206 ---DLRRHISIIPQDP-VLFSGTLRRNLDPFN-EFSDAALWEVLEEVELKDAVVisgnGLESRVLDRGSNYSVGQRQLVC 1280
Cdd:PRK13650 75 nvwDIRHKIGMVFQNPdNQFVGATVEDDVAFGlENKGIPHEEMKERVNEALELV----GMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1281 LARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHML 1355
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
502-684 |
9.03e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 78.48 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG------------QEAWVFGS-TVR 564
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditGLSEKElyelrrrigmlfQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILFgqPYDRHRY------QKVVKACsL----LRDF-KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLD 633
Cdd:COG1127 101 ENVAF--PLREHTDlseaeiRELVLEK-LelvgLPGAaDKMP-----------SELSGGMRKRVALARALALDPEILLYD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 634 DPLSAVDThVSKHLFEECIQ--RYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:COG1127 167 EPTAGLDP-ITSAVIDELIRelRDELGLTSVVVTHDLDSAFAIaDRVAVLADGK 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
502-681 |
9.48e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.52 E-value: 9.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEID---VVEGHVKVNGSLSYAG-----------QEAWVFGS-TVRQN 566
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALpaeqrrigilfQDDLLFPHlSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 567 ILFGQPYDRHRYQKVVKACSLLRD------FKQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:COG4136 97 LAFALPPTIGRAQRRARVEQALEEaglagfADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 641 TH----VSKHLFEECIQRYLAGktrILATHQLQYVKNVDAIILIE 681
Cdd:COG4136 166 AAlraqFREFVFEQIRQRGIPA---LLVTHDEEDAPAAGRVLDLG 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
495-717 |
9.52e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 81.87 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEID---VVEGHVKVNG-------------SLSYAGQEAWV 558
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGrdllelsealrgrRIGMVFQDPMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 559 --FGSTVRQNILFG-------QPYDRHRYQKVVKACSLLRDFKQFPQsdqtvvgergsSLSGGQKARINLARSLYRQADV 629
Cdd:COG1123 95 qlNPVTVGDQIAEAlenlglsRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 630 YLLDDPLSAVDTHVSKH---LFEECIQRYlaGKTRILATHQLQYVKNV-DAIILIEQGK-------ATVFSHYQDLLSQR 698
Cdd:COG1123 164 LIADEPTTALDVTTQAEildLLRELQRER--GTTVLLITHDLGVVAEIaDRVVVMDDGRivedgppEEILAAPQALAAVP 241
|
250
....*....|....*....
gi 383847295 699 PEYAELLAAENETHDDSSL 717
Cdd:COG1123 242 RLGAARGRAAPAAAAAEPL 260
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1135-1348 |
1.04e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.42 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL------AKVEGVIEIDDIDTGSICLEDLR 1208
Cdd:PRK14247 4 IEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1209 RHISIIPQDP-----------VLFSGTLRRNLDPFNEFSDAALWeVLEEVELKDAVvisgnglESRVLDRGSNYSVGQRQ 1277
Cdd:PRK14247 82 RRVQMVFQIPnpipnlsifenVALGLKLNRLVKSKKELQERVRW-ALEKAQLWDEV-------KDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAH------RLntimdSDKVLVMDKGRMAE 1348
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1152-1355 |
1.07e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.80 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV---EGVIEIDDIDTGSIcleDLRRHISIIPQDPVLFSG-TLRR 1227
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtsgRATVAGHDVVREPR---EVRRRIGIVFQDLSVDDElTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1228 NLDPF-------NEFSDAALWEVLEEVELKDAVvisgnglesrvlDR-GSNYSVGQRQLVCLARAILRNNKILMLDEATA 1299
Cdd:cd03265 93 NLYIHarlygvpGAERRERIDELLDFVGLLEAA------------DRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1300 NVDPQTDALIQNTIR---RKFTkCTVLTIAHrlntIMD-----SDKVLVMDKGRMAEYDHPHML 1355
Cdd:cd03265 161 GLDPQTRAHVWEYIEklkEEFG-MTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
505-684 |
1.15e-15 |
|
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: 77.53 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 505 LNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-----------SLSYAGQEAWVFGS-TVRQNILFG-- 570
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFAHlTVEQNVGLGls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 -----QPYDRHRYQKVVKACSLLRDFKQFPQSdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSK 645
Cdd:cd03298 97 pglklTAEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 646 HLF----EECIQRylaGKTRILATHQLQYVKNVDA-IILIEQGK 684
Cdd:cd03298 166 EMLdlvlDLHAET---KMTVLMVTHQPEDAKRLAQrVVFLDNGR 206
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1155-1349 |
1.45e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.77 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1155 LNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVI---------EIDDIDTGSicLEDLR-RHISIIPQDPVlfsgt 1224
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsatfngrEILNLPEKE--LNKLRaEQISMIFQDPM----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1225 lrRNLDPFNEFSDaALWEVL-------------EEVELKDAVVISgnglESRvlDRGSNY----SVGQRQLVCLARAILR 1287
Cdd:PRK09473 108 --TSLNPYMRVGE-QLMEVLmlhkgmskaeafeESVRMLDAVKMP----EAR--KRMKMYphefSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1288 NNKILMLDEATANVDPQTDALIQ---NTIRRKFTKcTVLTIAHRLNTIMDS-DKVLVMDKGRMAEY 1349
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMtllNELKREFNT-AIIMITHDLGVVAGIcDKVLVMYAGRTMEY 243
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
502-685 |
1.49e-15 |
|
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: 76.94 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-LSYAGQEAwvFG------------STVRQNIL 568
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpLDIAARNR--IGylpeerglypkmKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDThVSKHLF 648
Cdd:cd03269 94 LAQLKGLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 383847295 649 EECIQRYL-AGKTRILATHQLQYVKNV-DAIILIEQGKA 685
Cdd:cd03269 168 KDVIRELArAGKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1134-1359 |
1.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEE-ELPVLKGLNLVINPGEKIGIVGRTGAGKSS---LISALFRlaKVEGVIEIDDIDTGSICLEDLRR 1209
Cdd:PRK13642 4 ILEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1210 HISIIPQDP-VLFSGTLRRNLDPFNEFSDAALWEvlEEVELKDAVVISGNGLESRVLDRgSNYSVGQRQLVCLARAILRN 1288
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQGIPRE--EMIKRVDEALLAVNMLDFKTREP-ARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 1289 NKILMLDEATANVDPQTDALIQNTIRRKFTK--CTVLTIAHRLNTIMDSDKVLVMDKGRMAEYDHPHMLLQNT 1359
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
494-695 |
1.69e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 77.31 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 494 EPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEID---VVEGHVKVNG----------SLSYAGQ-EAWVF 559
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGqprkpdqfqkCVAYVRQdDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 560 GSTVRQNILF-----GQPYDRHRYQKVVKACSLLRDFkqfpqSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:cd03234 95 GLTVRETLTYtailrLPRKSSDAIRKKRVEDVLLRDL-----ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 635 PLSAVDTHVSKHLFEecIQRYLAGKTRIlathqlqyvknvdAIILIEQGKATVFSHYQDLL 695
Cdd:cd03234 170 PTSGLDSFTALNLVS--TLSQLARRNRI-------------VILTIHQPRSDLFRLFDRIL 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
502-666 |
2.17e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 79.37 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSlSYAGQEAW------VFGS-------TVRQNIL 568
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-DVTGLPPEkrnvgmVFQDyalfphlTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FG---QPYDRH-RYQKVVKACSL--LRDF-KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:COG3842 100 FGlrmRGVPKAeIRARVAELLELvgLEGLaDRYP-----------HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDA 168
|
170 180
....*....|....*....|....*..
gi 383847295 642 HVSKHLFEEcIQRYLA--GKTRILATH 666
Cdd:COG3842 169 KLREEMREE-LRRLQRelGITFIYVTH 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1135-1347 |
2.44e-15 |
|
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: 76.38 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPvlkgLNLVINPGEKIGIVGRTGAGKSSLIS--ALFRLAKvEGVIEIDDIDTGSicLEDLRRHIS 1212
Cdd:cd03298 1 VRLDKIRFSYGEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNliAGFETPQ-SGRVLINGVDVTA--APPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSG-TLRRNLD----P---FNEFSDAALWEVLEEVELkdavvisgNGLESRvldRGSNYSVGQRQLVCLARA 1284
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGlglsPglkLTAEDRQAIEVALARVGL--------AGLEKR---LPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1285 ILRNNKILMLDEATANVDP----QTDALIqNTIRRKfTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMA 1347
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPalraEMLDLV-LDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1125-1368 |
2.50e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1125 APKNWPKDGMIRFRNVYMRYAE---EELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTG 1200
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEkqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKyGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1201 SICLED----------------LRRHISIIPQDP--VLFSGTLRRNLdpfnEFSDAALWEVLEEVELKDAVVISGNGLES 1262
Cdd:PRK13631 92 DKKNNHelitnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDI----MFGPVALGVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1263 RVLDRGS-NYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR-RKFTKCTVLTIAHRLNTIMD-SDKVL 1339
Cdd:PRK13631 168 SYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILdAKANNKTVFVITHTMEHVLEvADEVI 247
|
250 260 270
....*....|....*....|....*....|
gi 383847295 1340 VMDKGRMAEYDHPHMLLQN-TYSQFTSLVK 1368
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDqHIINSTSIQV 277
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
502-701 |
2.69e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG---------QEAWVFGSTVRQNIL 568
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsSLSHSVlrqgvamvqQDPVVLADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVskhlf 648
Cdd:PRK10790 437 LGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT----- 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 649 EECIQRYLAG----KTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQRPEY 701
Cdd:PRK10790 512 EQAIQQALAAvrehTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1134-1358 |
4.04e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.16 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYaeEELPVLkgLNLVINPGEKIGIVGRTGAGKSSLIS--ALFrLAKVEGVIEIDDIDTGSIclEDLRRHI 1211
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMR--FDLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQDHTTT--PPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSG-TLRRN----LDP---FNEFSDAALWEVLEEVELKDavvisgnglesrVLDR-GSNYSVGQRQLVCLA 1282
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIED------------LLARlPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1283 RAILRNNKILMLDEATANVDPqtdALIQNTIRRKFTKC-----TVLTIAHRLNTIMD-SDKVLVMDKGRMAeYDHPHMLL 1356
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDP---ALRQEMLTLVSQVCqerqlTLLMVSHSLEDAARiAPRSLVVADGRIA-WDGPTDEL 217
|
..
gi 383847295 1357 QN 1358
Cdd:PRK10771 218 LS 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-688 |
4.07e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKV--NGSLSYAGQEAWVF--GSTVRQNILFGQPYDRHR 577
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDQHQEELdpDKTVLDELRDGAPGGTEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 578 YqkvvkACSLLRDFkQFPQSDQ-TVVGergsSLSGGQKARINLARSLYRQADVYLLDDPlsavdT-H---VSKHLFEECI 652
Cdd:COG0488 411 E-----VRGYLGRF-LFSGDDAfKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP-----TnHldiETLEALEEAL 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 383847295 653 QRYlAGkTRILATHQLQYVKNV-DAIILIEQGKATVF 688
Cdd:COG0488 476 DDF-PG-TVLLVSHDRYFLDRVaTRILEFEDGGVREY 510
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
502-707 |
4.96e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 79.56 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYAGQEAW---------VF----GS-----T 562
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkDLTKLSRRSLrelrrrvqmVFqdpySSlnprmT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNI-----LFGQPYDRHRYQKVV---KACSLLRDFKQ-FPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLD 633
Cdd:COG1123 361 VGDIIaeplrLHGLLSRAERRERVAellERVGLPPDLADrYP-----------HELSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 634 DPLSAVDTHVSKH---LFEEcIQRYLaGKTRILATHQLQYVKNV-DAIILIEQGK-------ATVFSHYQDLLSQRpeya 702
Cdd:COG1123 430 EPTSALDVSVQAQilnLLRD-LQREL-GLTYLFISHDLAVVRYIaDRVAVMYDGRivedgptEEVFANPQHPYTRA---- 503
|
....*
gi 383847295 703 eLLAA 707
Cdd:COG1123 504 -LLAA 507
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1134-1357 |
5.06e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.28 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEIDDIDTGSICLEDLRRHIS 1212
Cdd:COG4604 1 MIEIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLlPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLfsgTLR---RNLDPFNEF---------SD-AALWEVLEEVELKDavvisgngLESRVLDrgsNYSVGQRQLV 1279
Cdd:COG4604 79 ILRQENHI---NSRltvRELVAFGRFpyskgrltaEDrEIIDEAIAYLDLED--------LADRYLD---ELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1280 CLARAILRNNKILMLDEATANVDPQTDALIQNTIRR---KFTKCTVLTIaHRLN-TIMDSDKVLVMDKGRMAEYDHPHML 1355
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRladELGKTVVIVL-HDINfASCYADHIVAMKDGRVVAQGTPEEI 223
|
..
gi 383847295 1356 LQ 1357
Cdd:COG4604 224 IT 225
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
851-1093 |
5.64e-15 |
|
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: 77.21 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 851 IVVGLFCIGITRSLTFY---EVCIVCSQK-LHDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDA 923
Cdd:cd07346 41 IALLLLLLALLRALLSYlrrYLAARLGQRvVFDLrrdLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 924 GQICMMMFGSLAVSCIVNP------LFLIPIVFLgtVFYWIRKVYLKTSKNIKRlegmSRSPVFTHLNATLNGLTTIRAY 997
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWkltlvaLLLLPLYVL--ILRYFRRRIRKASREVRE----SLAELSAFLQESLSGIRVVKAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 998 CAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLVTF--SFLLLEQSFSGGEvglaITQVMAMTGMIQW 1075
Cdd:cd07346 195 AAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLygGYLVLQGSLTIGE----LVAFLAYLGMLFG 270
|
250 260
....*....|....*....|..
gi 383847295 1076 GMRQNAEAANQ----MMAVERV 1093
Cdd:cd07346 271 PIQRLANLYNQlqqaLASLERI 292
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
488-688 |
5.83e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.89 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 488 NFTAKWEPGQSENT-LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDV--VEGHVKVNG----------SLSYAGQ 554
Cdd:cd03213 10 TVTVKSSPSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGrpldkrsfrkIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 555 EAWVFGS-TVRQNILFGqpydrhryqkvvkacSLLRdfkqfpqsdqtvvgergsSLSGGQKARINLARSLYRQADVYLLD 633
Cdd:cd03213 90 DDILHPTlTVRETLMFA---------------AKLR------------------GLSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 634 DPLSAVDTHvSKHLFEECIQRyLA--GKTRILATHQLQY--VKNVDAIILIEQGKaTVF 688
Cdd:cd03213 137 EPTSGLDSS-SALQVMSLLRR-LAdtGRTIICSIHQPSSeiFELFDKLLLLSQGR-VIY 192
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1134-1346 |
9.33e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRY----AeeelpvLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDD-----------I 1197
Cdd:COG3845 5 ALELRGITKRFggvvA------NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIDGkpvrirsprdaI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1198 DTGsicledlrrhISIIPQDPVLFsgtlrrnlDPFNefsdaalweVLEEV----ELKDAVVISGNGLESRVLDRGSNY-- 1271
Cdd:COG3845 79 ALG----------IGMVHQHFMLV--------PNLT---------VAENIvlglEPTKGGRLDRKAARARIRELSERYgl 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1272 -----------SVGQRQLVCLARAILRNNKILMLDEATANVDPQ-TDALIQnTIRRkFTK--CTVLTIAHRLNTIMD-SD 1336
Cdd:COG3845 132 dvdpdakvedlSVGEQQRVEILKALYRGARILILDEPTAVLTPQeADELFE-ILRR-LAAegKSIIFITHKLREVMAiAD 209
|
250
....*....|
gi 383847295 1337 KVLVMDKGRM 1346
Cdd:COG3845 210 RVTVLRRGKV 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1135-1349 |
9.71e-15 |
|
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: 74.62 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDdidtGSICLEDLRRHISI 1213
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILpDSGEVLFD----GKPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IP-----------QDPVLFSGTLrRNLDPfnefSDAALW--EVLEEVELKDavvisgngLESRVLDRgsnYSVGQRQLVC 1280
Cdd:cd03269 75 LPeerglypkmkvIDQLVYLAQL-KGLKK----EEARRRidEWLERLELSE--------YANKRVEE---LSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 1281 LARAILRNNKILMLDEATANVDPQTDALIQNTI---RRKFTkcTVLTIAHRLNTIMD-SDKVLVMDKGRMAEY 1349
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIrelARAGK--TVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1135-1388 |
1.03e-14 |
|
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: 78.69 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAL--------------FRLAKVEGV--------- 1191
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiYHVALCEKCgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1192 -------------IEIDDIDTGSICLEDLRRHISIIPQDPVLFSG---TLRRNLDPFNEFSDAALWEVLEEVELKDAVvi 1255
Cdd:TIGR03269 79 gepcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddtVLDNVLEALEEIGYEGKEAVGRAVDLIEMV-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1256 sgnGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIM 1333
Cdd:TIGR03269 157 ---QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1334 D-SDKVLVMDKGRMAEYDHPHMLLQNTYSQFTSLVKETDRAMFDQLVRI--AKQSYIA 1388
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVrnVSKRYIS 291
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
502-698 |
1.19e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSyagqeaWVFG--------STVRQNILF---- 569
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLElgagfhpeLTGRENIYLngrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 -GqpYDRHRYQKVVKAC---SLLRDFKqfpqsDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHV-- 643
Cdd:COG1134 116 lG--LSRKEIDEKFDEIvefAELGDFI-----DQPV-----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFqk 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 644 -SKHLFEECIQRylaGKTRILATHQLQYVKNV-DAIILIEQGK-------ATVFSHYQDLLSQR 698
Cdd:COG1134 184 kCLARIRELRES---GRTVIFVSHSMGAVRRLcDRAIWLEKGRlvmdgdpEEVIAAYEALLAGR 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1135-1327 |
1.29e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL------AKVEGVIEI--DDIDTGSICLED 1206
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneeARVEGEVRLfgRNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDP---------------VLFSGTLR--RNLDPFNEFS--DAALWEvleevELKDavvisgnglesRVLDR 1267
Cdd:PRK14267 83 VRREVGMVFQYPnpfphltiydnvaigVKLNGLVKskKELDERVEWAlkKAALWD-----EVKD-----------RLNDY 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1268 GSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAH 1327
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1136-1348 |
1.33e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.49 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1136 RFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLED---LRRHI 1211
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAQrkaFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDP---VLFSGTLRRNLD-PFNEFSD-------AALWEVLEEVELKDAVvisgnglesrvLDR-GSNYSVGQRQLV 1279
Cdd:PRK10419 92 QMVFQDSisaVNPRKTVREIIRePLRHLLSldkaerlARASEMLRAVDLDDSV-----------LDKrPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1280 CLARAILRNNKILMLDEATANVDP--QTDALIQ-NTIRRKF-TKCtvLTIAHRLNTIMD-SDKVLVMDKGRMAE 1348
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlQAGVIRLlKKLQQQFgTAC--LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1135-1315 |
1.50e-14 |
|
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: 74.50 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDID-TGSICLEDLRRHIS 1212
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQDiTKLPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSG-TLRRNLDPFNEFSDAALWEVLEEVELkdavVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKI 1291
Cdd:cd03218 79 YLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEE----LLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180
....*....|....*....|....
gi 383847295 1292 LMLDEATANVDPQTDALIQNTIRR 1315
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1135-1332 |
1.50e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEID--------DIDTGSICLED 1206
Cdd:PRK14258 8 IKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffnqNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDPVLFSGTLRRN---------------LDPFNE--FSDAALWEVLEEVELKDAVVISGnglesrvldrgs 1269
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNvaygvkivgwrpkleIDDIVEsaLKDADLWDEIKHKIHKSALDLSG------------ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1270 nysvGQRQLVCLARAILRNNKILMLDEATANVDP----QTDALIQNTIRRkfTKCTVLTIAHRLNTI 1332
Cdd:PRK14258 154 ----GQQQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
502-640 |
1.93e-14 |
|
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: 74.12 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG--------------SLSYAGQEAWVFGS-TVRQN 566
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 567 I---LFGQPYDRHRYQKvvKACSLLRDFKQFPQSDQtvvgeRGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:cd03218 96 IlavLEIRGLSKKEREE--KLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1134-1362 |
2.10e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.36 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDT--GSICLEDLRRH 1210
Cdd:PRK09493 1 MIEFKNVSKHFGP--TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDGLKVndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLFS----------GTLRRNLDPFNEFSDAALwEVLEEVelkdavvisgnGLESRVLDRGSNYSVGQRQLVC 1280
Cdd:PRK09493 79 AGMVFQQFYLFPhltalenvmfGPLRVRGASKEEAEKQAR-ELLAKV-----------GLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1281 LARAILRNNKILMLDEATANVDPQtdaliqntIRRKFTKC---------TVLTIAHRLNTIMD-SDKVLVMDKGRMAEYD 1350
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPE--------LRHEVLKVmqdlaeegmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDG 218
|
250
....*....|..
gi 383847295 1351 HPHMLLQNTYSQ 1362
Cdd:PRK09493 219 DPQVLIKNPPSQ 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
506-705 |
2.24e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 506 NLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-----------LSYAGQEAWVFGS-TVRQNILFG--- 570
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 ----QPYDRHRYQKVVKACSLLRDFKQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKH 646
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 647 ---LFEE-CIQRYLagkTRILATHQLQyvknvDAI------ILIEQGKATVFSHYQDLLSQRPEYAELL 705
Cdd:PRK10771 168 mltLVSQvCQERQL---TLLMVSHSLE-----DAAriaprsLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1143-1344 |
2.31e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1143 RYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK---VEGVIEIDDIDtgsicledlrrhisiIPQDpv 1219
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtpVAGCVDVPDNQ---------------FGRE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1220 lfsGTLRRNLDPFNEFSDAAlwEVLEEVELKDAVVIsgnglesrvLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATA 1299
Cdd:COG2401 100 ---ASLIDAIGRKGDFKDAV--ELLNAVGLSDAVLW---------LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 383847295 1300 NVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD--SDKVLVMDKG 1344
Cdd:COG2401 166 HLDRQTAKRVARNLQKlaRRAGITLVVATHHYDVIDDlqPDLLIFVGYG 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1135-1365 |
2.35e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.25 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGL---NLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDD----IDTGSICLED 1206
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLdniSFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDP--VLFSGTLRRNLD--PFN-EFSDaalwevlEEVELKDAVVISGNGLESRVLDRGS-NYSVGQRQLVC 1280
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPKNfGFSE-------DEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1281 LARAILRNNKILMLDEATANVDPQT-DALIQNTIRRKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHP------ 1352
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPkeifsd 235
|
250
....*....|....*....
gi 383847295 1353 ------HMLLQNTYSQFTS 1365
Cdd:PRK13641 236 kewlkkHYLDEPATSRFAS 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
502-678 |
3.47e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-------------LSYAGQEAWVFGSTVRQNIL 568
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FgqPYDRHRYQKVVKAcsLLRDFKQFpQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHLF 648
Cdd:PRK10247 103 F--PWQIRNQQPDPAI--FLDDLERF-ALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHNV 176
|
170 180 190
....*....|....*....|....*....|..
gi 383847295 649 EECIQRYLAGK--TRILATHQLQYVKNVDAII 678
Cdd:PRK10247 177 NEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1152-1365 |
3.80e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEIddidTGSICLE------------DLRRHISIIPQDPV 1219
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTI----TGSIVYNghniysprtdtvDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1220 LFSGTLRRN---------------LDPFNEFS--DAALWEvleevELKDAVVISGNGLesrvldrgsnySVGQRQLVCLA 1282
Cdd:PRK14239 97 PFPMSIYENvvyglrlkgikdkqvLDEAVEKSlkGASIWD-----EVKDRLHDSALGL-----------SGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1283 RAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQNTYS 1361
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
....
gi 383847295 1362 QFTS 1365
Cdd:PRK14239 241 KETE 244
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1154-1352 |
4.13e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.15 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1154 GLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEID--DIDTGS-ICLEDLRRHISIIPQDPvlFSgtlrrNL 1229
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPtSGEILFDgqDITGLSgRELRPLRRRMQMVFQDP--YA-----SL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1230 DP-------------FNEFSDAAlwEVLEEV-ELKDAVvisgnGLESRVLDRgsnY----SVGQRQLVCLARAILRNNKI 1291
Cdd:COG4608 109 NPrmtvgdiiaeplrIHGLASKA--ERRERVaELLELV-----GLRPEHADR---YphefSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1292 LMLDEATAnvdpqtdAL---IQ-------NTIRRKFtKCTVLTIAHRLNT---ImdSDKVLVMDKGRMAE-------YDH 1351
Cdd:COG4608 179 IVCDEPVS-------ALdvsIQaqvlnllEDLQDEL-GLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEiaprdelYAR 248
|
.
gi 383847295 1352 P 1352
Cdd:COG4608 249 P 249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
502-669 |
4.39e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 72.92 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLSYAGQEAWVFGS-TVRQNIL 568
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 F-----GQPydRHRYQKVVKAcsLLRDFKQFPQSDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDtHV 643
Cdd:cd03263 98 FyarlkGLP--KSEIKEEVEL--LLRVLGLTDKANKRA-----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PA 167
|
170 180
....*....|....*....|....*.
gi 383847295 644 SKHLFEECIQRYLAGKTRILATHQLQ 669
Cdd:cd03263 168 SRRAIWDLILEVRKGRSIILTTHSMD 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1152-1350 |
5.35e-14 |
|
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: 72.71 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVIN---PGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDI---DTG-SICLEDLRRHISIIPQDPVLFSG 1223
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDgGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1224 -TLRRNLdpfnEFSdaalWEVLEEVELKDAV--VISGNGLESrVLDRG-SNYSVGQRQLVCLARAILRNNKILMLDEATA 1299
Cdd:cd03297 90 lNVRENL----AFG----LKRKRNREDRISVdeLLDLLGLDH-LLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1300 NVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTI-MDSDKVLVMDKGRMAEYD 1350
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1134-1357 |
6.44e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHIS 1212
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTpQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDPVLFSGTLRRNLDPFNEFSDAALWEVL-EEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKI 1291
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRSPWLSLWGRLsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1292 LMLDEATANVDPQTDALIQNTIRRKFTKC-TVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQ 1357
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1151-1348 |
6.45e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDD--IDTG-SI-----CLEDLRRHISIIPQDpvlf 1221
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEaGTIRVGDitIDTArSLsqqkgLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1222 sgtlrrnldpFNEFSD-AALWEVLE-----EVELKDAVVISGNGLESRVLDRG--SNY----SVGQRQLVCLARAILRNN 1289
Cdd:PRK11264 94 ----------FNLFPHrTVLENIIEgpvivKGEPKEEATARARELLAKVGLAGkeTSYprrlSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1290 KILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAE 1348
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
877-1378 |
7.57e-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: 76.87 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 877 LHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKA--VLDAGQICMMMFG----SLAVSCIVNPLFLIpivF 950
Cdd:TIGR01271 157 LFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAhfVWIAPLQVILLMGliweLLEVNGFCGLGFLI---L 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 951 LGTVFYWIRKVYLKTSKniKRLEGMSRSPVFThlNATLNGLTTIRAYCAQDILKKEFDKLQDVHTS----TVYMYVVSSS 1026
Cdd:TIGR01271 234 LALFQACLGQKMMPYRD--KRAGKISERLAIT--SEIIENIQSVKAYCWEEAMEKIIKNIRQDELKltrkIAYLRYFYSS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1027 GFGFSldIFCFVFTSLVTFSF---LLLEQSFSggEVGLAITQVMAMTGMIQWGMRQNAEAANQMMAVE--------RVLE 1095
Cdd:TIGR01271 310 AFFFS--GFFVVFLSVVPYALikgIILRRIFT--TISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQdflckeeyKTLE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1096 YTNIPPEPNLR------DRGkFAKKSEKqIALPANAPKNWPKDGMIRFRNVYMRYAeeelPVLKGLNLVINPGEKIGIVG 1169
Cdd:TIGR01271 386 YNLTTTEVEMVnvtaswDEG-IGELFEK-IKQNNKARKQPNGDDGLFFSNFSLYVT----PVLKNISFKLEKGQLLAVAG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1170 RTGAGKSSLISALF-RLAKVEGVIeiddidtgsicledlrRH---ISIIPQDPVLFSGTLRRNLDPFNEFSDAALWEVLE 1245
Cdd:TIGR01271 460 STGSGKSSLLMMIMgELEPSEGKI----------------KHsgrISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1246 EVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALI-QNTIRRKFTKCTVLT 1324
Cdd:TIGR01271 524 ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRIL 603
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1325 IAHRLNTIMDSDKVLVMDKGRMAEYDhPHMLLQNTYSQFTSLVKETDRamFDQL 1378
Cdd:TIGR01271 604 VTSKLEHLKKADKILLLHEGVCYFYG-TFSELQAKRPDFSSLLLGLEA--FDNF 654
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
502-666 |
8.45e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.34 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-----------SLSYagqeawVFGS-------TV 563
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlppkdrNIAM------VFQSyalyphmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RQNILFG-----QPYDRHRyQKVVKACSLLR--DF-KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDP 635
Cdd:COG3839 93 YENIAFPlklrkVPKAEID-RRVREAAELLGleDLlDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 383847295 636 LSAVDTHVSKHLFEEcIQRYLA--GKTRILATH 666
Cdd:COG3839 161 LSNLDAKLRVEMRAE-IKRLHRrlGTTTIYVTH 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
502-686 |
8.79e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG---------QEAWV-FGSTVRQNI 567
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddveALSARAasrrvasvpQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFGQPYDRHRY-------QKVVKACSLLRDFKQFpqSDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:PRK09536 99 EMGRTPHRSRFdtwtetdRAAVERAMERTGVAQF--ADRPV-----TSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 383847295 641 THVSKHLFEecIQRYLA--GKTRILATHQLQY-VKNVDAIILIEQGKAT 686
Cdd:PRK09536 172 INHQVRTLE--LVRRLVddGKTAVAAIHDLDLaARYCDELVLLADGRVR 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
483-684 |
1.20e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 483 AVKMTNFTAKWEPGQSENT--LDNLNLEIEKGKIYAVIGMVGAGKSSFL---SAIL----GEIDVVEGHVKVNG------ 547
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITIAGYHITPETgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 548 ------SLSYAGQEAWVFGSTVRQNILFGqPYDRHRYQKVVKACSLlRDFKQFPQSDQtVVGERGSSLSGGQKARINLAR 621
Cdd:PRK13641 82 klrkkvSLVFQFPEAQLFENTVLKDVEFG-PKNFGFSEDEAKEKAL-KWLKKVGLSED-LISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 622 SLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYV-KNVDAIILIEQGK 684
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGK 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-710 |
1.40e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG--SLSYAGQEAWVF-GSTVRQNILFG-------- 570
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTVLDGdaelrale 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 QPYDR------------HRYQKV-------------VKACSLLRDFKqFPQSDQTvvgERGSSLSGGQKARINLARSLYR 625
Cdd:COG0488 94 AELEEleaklaepdedlERLAELqeefealggweaeARAEEILSGLG-FPEEDLD---RPVSELSGGWRRRVALARALLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 626 QADVYLLDDPlsavdTHvskHL-------FEECIQRYlaGKTRILATHQ---LQYVknVDAIILIEQGKATVFS-HYQDL 694
Cdd:COG0488 170 EPDLLLLDEP-----TN---HLdlesiewLEEFLKNY--PGTVLVVSHDryfLDRV--ATRILELDRGKLTLYPgNYSAY 237
|
250
....*....|....*.
gi 383847295 695 LSQRPEYAELLAAENE 710
Cdd:COG0488 238 LEQRAERLEQEAAAYA 253
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1135-1345 |
1.41e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.40 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIDDIDTgsicledlrrhISI 1213
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWGSTVK-----------IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQdpvlFSGtlrrnldpfnefsdaalwevleevelkdavvisgnglesrvldrgsnysvGQRQLVCLARAILRNNKILM 1293
Cdd:cd03221 68 FEQ----LSG--------------------------------------------------GEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1294 LDEATANVDPQTDALIQNTIRRKftKCTVLTIAH-R--LNTImdSDKVLVMDKGR 1345
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
502-684 |
1.79e-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: 71.07 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGkIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGslsyagQEAWVFGSTVRQNI-----LFGqPYDRH 576
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG------QDVLKQPQKLRRRIgylpqEFG-VYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 577 RYQKVVKACSLLRDFKQfPQSDQTVVG------------ERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDThVS 644
Cdd:cd03264 88 TVREFLDYIAWLKGIPS-KEVKARVDEvlelvnlgdrakKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 383847295 645 KHLFEECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGK 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1167-1348 |
1.85e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1167 IVGRTGAGKSSLISALFRLA-KVEGVIEIDDIDTGSICL------EDLRRHISIIPQDPVLF---------SGTLRRNLD 1230
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNdKVSGYRYSGDVLLGGRSIfnyrdvLEFRRRVGMLFQRPNPFpmsimdnvlAGVRAHKLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1231 PFNEFSDAALWEvLEEVELKDAVvisgnglESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQ 1310
Cdd:PRK14271 132 PRKEFRGVAQAR-LTEVGLWDAV-------KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 383847295 1311 NTIRRKFTKCTVLTIAHRL-NTIMDSDKVLVMDKGRMAE 1348
Cdd:PRK14271 204 EFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
484-709 |
1.98e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 71.60 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWepgqSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-----------LSYA 552
Cdd:cd03299 1 LKVENLSKDW----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 553 GQEAWVFGS-TVRQNILFGQpydRHRYQKVVKACSLLRDFKQFPQSDQtVVGERGSSLSGGQKARINLARSLYRQADVYL 631
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGL---KKRKVDKKEIERKVLEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 632 LDDPLSAVDTHVSKHLFEECIQ-RYLAGKTRILATHQLQYVKNV-DAIILIEQGKATVFSHYQDLLSqRP---EYAELLA 706
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKiRKEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFK-KPkneFVAEFLG 231
|
...
gi 383847295 707 AEN 709
Cdd:cd03299 232 FNN 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1131-1346 |
2.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1131 KDGMIRFRNVYMRYAEEE----LPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALfrLAKVEGVIEIDDIDTGSI- 1202
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNAL--LIPSEGKVYVDGLDTSDEe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1203 CLEDLRRHISIIPQDP------------VLFSGtlrRNLDPFNEFSDAALWEVLEEV---ELKDAV--VISGnglesrvl 1265
Cdd:PRK13633 79 NLWDIRNKAGMVFQNPdnqivativeedVAFGP---ENLGIPPEEIRERVDESLKKVgmyEYRRHAphLLSG-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1266 drgsnysvGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMDSDKVLVMDK 1343
Cdd:PRK13633 148 --------GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDS 219
|
...
gi 383847295 1344 GRM 1346
Cdd:PRK13633 220 GKV 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
502-690 |
2.62e-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: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAI--LGEIDvvEGHVKVNG----SLSyaGQEAW--------VFGS------ 561
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInlLERPT--SGSVLVDGvdltALS--ERELRaarrkigmIFQHfnllss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 -TVRQNILFgqP-----YDRHRYQKVVKacSLLrDF-------KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQAD 628
Cdd:COG1135 97 rTVAENVAL--PleiagVPKAEIRKRVA--ELL-ELvglsdkaDAYP-----------SQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 629 VYLLDDPLSAVDTHVSK---HLFEEcIQRYLaGKTRILATHQLQYVKNV-DAIILIEQGK-------ATVFSH 690
Cdd:COG1135 161 VLLCDEATSALDPETTRsilDLLKD-INREL-GLTIVLITHEMDVVRRIcDRVAVLENGRiveqgpvLDVFAN 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1135-1357 |
2.66e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKvegvieiDDIDTGSICLEDL------- 1207
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTH-------PDAGSISLCGEPVpsrarha 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQ----DPVLfsgTLRRNLDPFNEFSDAALWEVLEEVelkdAVVISGNGLESRVLDRGSNYSVGQRQLVCLAR 1283
Cdd:PRK13537 79 RQRVGVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALV----PPLLEFAKLENKADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1284 AILRNNKILMLDEATANVDPQTDALIQNTIRRKFT--KCTVLTI-----AHRLntimdSDKVLVMDKGRMAEYDHPHMLL 1356
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArgKTILLTThfmeeAERL-----CDRLCVIEEGRKIAEGAPHALI 226
|
.
gi 383847295 1357 Q 1357
Cdd:PRK13537 227 E 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1144-1314 |
2.67e-13 |
|
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: 70.08 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1144 YAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEdLRRHISIIPQDPVLfS 1222
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRpDSGEVRWNGTPLAEQRDE-PHENILYLGHLPGL-K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1223 GTL--RRNLDPFNEFSDAA---LWEVLEEVELkdavvisgNGLEsrvlDRGSNY-SVGQRQLVCLARAILRNNKILMLDE 1296
Cdd:TIGR01189 86 PELsaLENLHFWAAIHGGAqrtIEDALAAVGL--------TGFE----DLPAAQlSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*...
gi 383847295 1297 ATANVDPQTDALIQNTIR 1314
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR 171
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
502-684 |
2.68e-13 |
|
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: 71.22 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG--SLSYAGQE---AWVFGS-------TVRQNILF 569
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQErnvGFVFQHyalfrhmTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 GQPYdRHRYQKVVKAC--SLLRDFKQFPQSDQtvVGER-GSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKH 646
Cdd:cd03296 98 GLRV-KPRSERPPEAEirAKVHELLKLVQLDW--LADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 647 LfeeciQRYLA------GKTRILATH-QLQYVKNVDAIILIEQGK 684
Cdd:cd03296 175 L-----RRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGR 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1134-1352 |
2.83e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAKVEGVIEIDDIDTGSICLEDLRRH 1210
Cdd:PRK13638 1 MLATSDLWFRYQDE--PVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDP---VLFSgtlrrNLDPFNEFSDAALWEVLEEV--ELKDAV-VISGNGLESRVLDRGSNysvGQRQLVCLARA 1284
Cdd:PRK13638 79 VATVFQDPeqqIFYT-----DIDSDIAFSLRNLGVPEAEItrRVDEALtLVDAQHFRHQPIQCLSH---GQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1285 ILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTI-AHRLNTIMD-SDKVLVMDKGRMAEYDHP 1352
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
502-698 |
3.50e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.53 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG------QEAWVF-------GSTVR 564
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltALSEKElrkarrQIGMIFqhfnllsSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILF-----GQPyDRHRYQKVVKACSL--LRDFK-QFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPL 636
Cdd:PRK11153 101 DNVALplelaGTP-KAEIKARVTELLELvgLSDKAdRYP-----------AQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 637 SAVD---THVSKHLFEEcIQRYLaGKTRILATHQLQYVKNV-D--AII----LIEQGK-ATVFSHYQDLLSQR 698
Cdd:PRK11153 169 SALDpatTRSILELLKD-INREL-GLTIVLITHEMDVVKRIcDrvAVIdagrLVEQGTvSEVFSHPKHPLTRE 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
502-684 |
3.86e-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: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-----LSYAGQEAWVFGS-------TVRQNILF 569
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlPPHKRPVNTVFQNyalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 GQPYDR----HRYQKVVKACSL--LRDF-KQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTH 642
Cdd:cd03300 96 GLRLKKlpkaEIKERVAEALDLvqLEGYaNRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 643 VSKHLFEEC--IQRYLaGKTRILATH-QLQYVKNVDAIILIEQGK 684
Cdd:cd03300 165 LRKDMQLELkrLQKEL-GITFVFVTHdQEEALTMSDRIAVMNKGK 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1138-1345 |
4.18e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1138 RNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGvieiDDIDTGSICLEDLRRHISIIPQD 1217
Cdd:PRK11247 16 NAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA----GELLAGTAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1218 PVLF-------------SGTLRrnldpfnefsDAALwEVLEEVelkdavvisgnGLESRVLDRGSNYSVGQRQLVCLARA 1284
Cdd:PRK11247 90 ARLLpwkkvidnvglglKGQWR----------DAAL-QALAAV-----------GLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1285 ILRNNKILMLDEATANVDPQTDALIQNTIRRKFTK--CTVLTIAHRLN-TIMDSDKVLVMDKGR 1345
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSeAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1132-1345 |
4.62e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.42 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1132 DGMIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDD--IDTGSICLEDLR 1208
Cdd:PRK13636 3 DYILKVEELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGkpIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1209 RHISIIPQDP--VLFSGTLrrnldpFNEFSDAALWEVLEEVELKDAV--VISGNGLESRVLDRGSNYSVGQRQLVCLARA 1284
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASV------YQDVSFGAVNLKLPEDEVRKRVdnALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1285 ILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTI-MDSDKVLVMDKGR 1345
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGR 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
502-667 |
5.56e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----------SLSYAGQEAWVFGS-TVRQNILFG 570
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRNAMKPAlTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 QP-YDRHRYQKVVKACSL-LRDFKQFPqsdqtvvgerGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHLF 648
Cdd:PRK13539 98 AAfLGGEELDIAAALEAVgLAPLAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALF 166
|
170 180
....*....|....*....|
gi 383847295 649 EECIQRYLA-GKTRILATHQ 667
Cdd:PRK13539 167 AELIRAHLAqGGIVIAATHI 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1112-1350 |
5.83e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1112 AKKSEKQIALPANAPKNWPKDgMIRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALfrlakvEGV 1191
Cdd:COG0488 294 PPRRDKTVEIRFPPPERLGKK-VLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL------AGE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1192 IEIDdidTGSIcledlRR----HISIIPQDpvlfsgtlRRNLDPfnefsDAALWEVLEEV--ELKDAVVI--------SG 1257
Cdd:COG0488 365 LEPD---SGTV-----KLgetvKIGYFDQH--------QEELDP-----DKTVLDELRDGapGGTEQEVRgylgrflfSG 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1258 NGLESRVldrgSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQT-----DALIQntirrkFtKCTVLTIAH-R--L 1329
Cdd:COG0488 424 DDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETlealeEALDD------F-PGTVLLVSHdRyfL 492
|
250 260
....*....|....*....|.
gi 383847295 1330 NTImdSDKVLVMDKGRMAEYD 1350
Cdd:COG0488 493 DRV--ATRILEFEDGGVREYP 511
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
484-698 |
7.21e-13 |
|
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: 73.83 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQsENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLS 550
Cdd:TIGR00957 1285 VEFRNYCLRYREDL-DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 551 YAGQEAWVFGSTVRQNIlfgQPYDRHRYQKVVKACSL--LRDF-KQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQA 627
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELahLKTFvSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 628 DVYLLDDPLSAVDTHvSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQR 698
Cdd:TIGR00957 1441 KILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR 1510
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
504-684 |
9.89e-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: 69.98 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 504 NLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG-------QEAWVFGS-------TVRQ 565
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaAMSRKElrelrrkKISMVFQSfallphrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 566 NILFG---QPYDRH-RYQKVVKACSL--LRDFK-QFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSA 638
Cdd:cd03294 122 NVAFGlevQGVPRAeREERAAEALELvgLEGWEhKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 383847295 639 VDTHVSKHLFEEC--IQRYLaGKTRILATHQL-QYVKNVDAIILIEQGK 684
Cdd:cd03294 191 LDPLIRREMQDELlrLQAEL-QKTIVFITHDLdEALRLGDRIAIMKDGR 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1134-1305 |
1.02e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.66 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELpvLKGLNLVINPGEKIGIVGRTGAGKSSLISAL-------FRlakVEGVIEID--DIDTGSIcl 1204
Cdd:COG4136 1 MLSLENLTITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFS---ASGEVLLNgrRLTALPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1205 edLRRHISIIPQDPVLFSG-TLRRNLdPF---NEFS----DAALWEVLEEVEL-----KDAVVISGnglesrvldrgsny 1271
Cdd:COG4136 74 --EQRRIGILFQDDLLFPHlSVGENL-AFalpPTIGraqrRARVEQALEEAGLagfadRDPATLSG-------------- 136
|
170 180 190
....*....|....*....|....*....|....
gi 383847295 1272 svGQRQLVCLARAILRNNKILMLDEATANVDPQT 1305
Cdd:COG4136 137 --GQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1151-1346 |
1.08e-12 |
|
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: 67.84 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDID-TGSICLEDLRRHISIIPQDP----VLFSGT 1224
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPvTRRSPRDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1225 LRRNLdpfnefsdaALwevleevelkdAVVISGnglesrvldrgsnysvGQRQLVCLARAILRNNKILMLDEATANVDPQ 1304
Cdd:cd03215 95 VAENI---------AL-----------SSLLSG----------------GNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 1305 TDALIQNTIRRkFTK--CTVLTIAHRLNTIMD-SDKVLVMDKGRM 1346
Cdd:cd03215 139 AKAEIYRLIRE-LADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1148-1315 |
1.29e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1148 ELPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAkvEGVIEIDDIDTgsicleDLRRHISII----PQD--- 1217
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLPPA--AGTIKLDGGDI------DDPDVAEAChylgHRNamk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1218 PVLfsgTLRRNLDPFNEF---SDAALWEVLEEVELkdavvisgngleSRVLDRGSNY-SVGQRQLVCLARAILRNNKILM 1293
Cdd:PRK13539 86 PAL---TVAENLEFWAAFlggEELDIAAALEAVGL------------APLAHLPFGYlSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|..
gi 383847295 1294 LDEATANVDPQTDALIQNTIRR 1315
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRA 172
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1150-1341 |
1.32e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIddidTGSICLEDLRRHISIIPQDPVLFSGTL--- 1225
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgVLRPTSGTVRR----AGGARVAYVPQRSEVPDSLPLTVRDLVamg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1226 ----RRNLDPFNEFSDAALWEVLEEVELKDavvisgngLESRVLDrgsNYSVGQRQLVCLARAILRNNKILMLDEATANV 1301
Cdd:NF040873 82 rwarRGLWRRLTRDDRAAVDDALERVGLAD--------LAGRQLG---ELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 383847295 1302 DPQTDALIQNTIRRKF-TKCTVLTIAHRLNTIMDSDKVLVM 1341
Cdd:NF040873 151 DAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
483-692 |
1.53e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.01 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 483 AVKMTNFTAKWEpGQSenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAI-------LGEIDVveGHVKVNGSLSYAGQE 555
Cdd:PRK11264 3 AIEVKNLVKKFH-GQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 556 A----------WVFGS-------TVRQNILFG------QPydrhRYQKVVKACSLLRDfkqfpqsdqtvVGERGSS---- 608
Cdd:PRK11264 78 GlirqlrqhvgFVFQNfnlfphrTVLENIIEGpvivkgEP----KEEATARARELLAK-----------VGLAGKEtsyp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 609 --LSGGQKARINLARSLYRQADVYLLDDPLSAVDthvsKHLFEECIQ--RYLA--GKTRILATHQLQYVKNV-------D 675
Cdd:PRK11264 143 rrLSGGQQQRVAIARALAMRPEVILFDEPTSALD----PELVGEVLNtiRQLAqeKRTMVIVTHEMSFARDVadraifmD 218
|
250
....*....|....*...
gi 383847295 676 AIILIEQGKA-TVFSHYQ 692
Cdd:PRK11264 219 QGRIVEQGPAkALFADPQ 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1148-1302 |
1.73e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1148 ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVL-FSGTL 1225
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINgTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1226 RR-----------NLDPFNEFSDAALWEVLEEVELkdavvisgngleSRVLDRG-SNYSVGQRQLVCLARAILRNNKILM 1293
Cdd:PRK09536 95 RQvvemgrtphrsRFDTWTETDRAAVERAMERTGV------------AQFADRPvTSLSGGERQRVLLARALAQATPVLL 162
|
....*....
gi 383847295 1294 LDEATANVD 1302
Cdd:PRK09536 163 LDEPTASLD 171
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1135-1352 |
2.04e-12 |
|
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: 68.52 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDlrRHISI 1213
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSG-TLRRNL------DPFNEFSDAAlwEVLEEV-ELKDAVVISGngLESRVldrGSNYSVGQRQLVCLARAI 1285
Cdd:cd03296 79 VFQHYALFRHmTVFDNVafglrvKPRSERPPEA--EIRAKVhELLKLVQLDW--LADRY---PAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1286 LRNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTI--AHRLNTIMD-SDKVLVMDKGRMAE-------YDHP 1352
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQvgtpdevYDHP 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
502-697 |
2.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFL------------SAILGEIDVVEGHVKVNG--------SLSYAGQEAWVFGS 561
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngliisetgQTIVGDYAIPANLKKIKEvkrlrkeiGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 TVRQNILFGQPYDRHRYQKVVKACSLLRDFKQFPQSdqtVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPED---YVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 642 HVSK---HLFEECIQRYlaGKTRILATHQL-QYVKNVDAIILIEQGKAT-------VFSHyQDLLSQ 697
Cdd:PRK13645 184 KGEEdfiNLFERLNKEY--KKRIIMVTHNMdQVLRIADEVIVMHEGKVIsigspfeIFSN-QELLTK 247
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
502-635 |
2.66e-12 |
|
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: 67.84 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS--------------LSYAGQEAWVFGS-TVRQN 566
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 567 ILFGQpydRHRYQKVVKAcSLLRDFKQFPqsdqtVVGER----GSSLSGGQKARINLARSLYRQADVYLLDDP 635
Cdd:cd03224 96 LLLGA---YARRRAKRKA-RLERVYELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
488-666 |
2.74e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.25 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 488 NFTAKWEpGQseNTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLS----YAGQEAWVFGS- 561
Cdd:PRK11607 24 NLTKSFD-GQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLShvppYQRPINMMFQSy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 ------TVRQNILFGQPYDR----HRYQKVVKACSLLRDfkqfpqsdQTVVGERGSSLSGGQKARINLARSLYRQADVYL 631
Cdd:PRK11607 101 alfphmTVEQNIAFGLKQDKlpkaEIASRVNEMLGLVHM--------QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 383847295 632 LDDPLSAVDTHVSKHLFEEC---IQRylAGKTRILATH 666
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVvdiLER--VGVTCVMVTH 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1135-1356 |
3.10e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVegvieiddiDTGSICLEDL------- 1207
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP---------DAGKITVLGVpvparar 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 --RRHISIIPQ-DPVLFSGTLRRNLDPFNEF-------SDAALWEVLEEVELkdavvisgnglESRVLDRGSNYSVGQRQ 1277
Cdd:PRK13536 111 laRARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARL-----------ESKADARVSDLSGGMKR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKC-TVLTIAHrlntIMDS-----DKVLVMDKGRMAEYDH 1351
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTH----FMEEaerlcDRLCVLEAGRKIAEGR 255
|
....*
gi 383847295 1352 PHMLL 1356
Cdd:PRK13536 256 PHALI 260
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
835-1059 |
3.25e-12 |
|
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: 68.95 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 835 NLDISSMYNYMYIYTAIVVGLFCIGITRSLTFYEVcivcSQK-LHDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMG 910
Cdd:cd18544 34 QGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKL----GQRiIYDLrrdLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 911 TIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGTVFY--WIRKVYLKTSKNIKRLEgmsrspvfT 982
Cdd:cd18544 110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWrlalisLLVLPLLLLATYLFrkKSRKAYREVREKLSRLN--------A 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 983 HLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLV--TFSFLLLEQSFSGGEV 1059
Cdd:cd18544 182 FLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVlwYGGGQVLSGAVTLGVL 260
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
93-384 |
3.88e-12 |
|
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: 68.73 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 93 VVLGLMQILNEFVIRLGTPILLGGLLRYFRKSTDetYETALWYAAGICIATAINVITLNQAIFGAFHVGARIRVATCSVV 172
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD--LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 173 YRKALRLSKTALGETAPGKVVNLVANDVNRF-DLVSIFIHHMWSAPLSALIIAYFLYTEAGYAGLIGIAAVFVVVPIQSY 251
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVqNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 252 TGKLSSKFRLQTAIKTDERVRLMDEIISGVQVIKMYAWEKSFCALIETARKLELRVVKKSSYIRGIYMTFNLFTTRMALF 331
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 332 CTLI--SMLLFGNELSADKVFVFSSYFNILAHTMTgMFVRGFAEIAECLVAVRRL 384
Cdd:cd07346 239 LVLLygGYLVLQGSLTIGELVAFLAYLGMLFGPIQ-RLANLYNQLQQALASLERI 292
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
502-669 |
4.18e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGhVKVNGSLSYAGQEAW---VFGSTVRQNI--LFGQP---- 572
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTFHGKNLYapdVDPVEVRRRIgmVFQKPnpfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 573 ---YDRHRYQKVVKACS------LLRDFKQFPQSDQTV--VGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:PRK14243 105 ksiYDNIAYGARINGYKgdmdelVERSLRQAALWDEVKdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180
....*....|....*....|....*...
gi 383847295 642 hVSKHLFEECIQRYLAGKTRILATHQLQ 669
Cdd:PRK14243 185 -ISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
502-697 |
4.50e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGS-------------TVRQNIL 568
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIgvvpqfdnldlefTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTvvgeRGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHLF 648
Cdd:PRK13536 137 VFGRYFGMSTREIEAVIPSLLEFARLESKADA----RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLI 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 383847295 649 EECIQRYLA-GKTRILATHQLQYVKNV-DAIILIEQGKATVFSHYQDLLSQ 697
Cdd:PRK13536 212 WERLRSLLArGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-674 |
6.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 483 AVKMTNFTAKWEpgqSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAiLGEIDVVEGHVKVNGSLSYAGQ---EAWVF 559
Cdd:PRK14258 7 AIKVNNLSFYYD---TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 560 GSTVRQNI--LFGQP-------YDRHRY-----------------QKVVKACSLLRDFKQfpqsdqtVVGERGSSLSGGQ 613
Cdd:PRK14258 83 LNRLRRQVsmVHPKPnlfpmsvYDNVAYgvkivgwrpkleiddivESALKDADLWDEIKH-------KIHKSALDLSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 614 KARINLARSLYRQADVYLLDDPLSAVDTHVSKHLfEECIQ--RYLAGKTRILATHQLQYVKNV 674
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQslRLRSELTMVIVSHNLHQVSRL 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
483-671 |
7.95e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 483 AVKMTNFTAKWEPGQSenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS----------LSYA 552
Cdd:PRK15056 6 GIVVNDVTVTWRNGHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 553 GQEA---WVFGSTVRQNILFGQ-----------PYDRHRYQKVVKACSLLrDFKQfpqsdqTVVGErgssLSGGQKARIN 618
Cdd:PRK15056 84 PQSEevdWSFPVLVEDVVMMGRyghmgwlrrakKRDRQIVTAALARVDMV-EFRH------RQIGE----LSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 619 LARSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYV 671
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSV 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
502-684 |
9.54e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 9.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVK-----VNGSLSYAGQEAWVFGS--------TVRQNIL 568
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepVPSRARHARQRVGVVPQfdnldpdfTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 -FGQPYDRHRYQKVVKACSLLrDFKQFPQSDQTVVGErgssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHL 647
Cdd:PRK13537 103 vFGRYFGLSAAAARALVPPLL-EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 383847295 648 FEECIQRYLA-GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:PRK13537 177 MWERLRSLLArGKTILLTTHFMEEAERLcDRLCVIEEGR 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1135-1359 |
1.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNV---YMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDID----TGSICLED 1206
Cdd:PRK13646 3 IRFDNVsytYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDP--VLFSGTLRRNLdpfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGS-NYSVGQRQLVCLAR 1283
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVEREI----IFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1284 AILRNNKILMLDEATANVDPQTDALIQNTIRRKFTK--CTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQNT 1359
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
502-684 |
1.08e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKV-NGSLSYAG-------QEA----WvfgSTVRQNILF 569
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgTAPLAEARedtrlmfQDArllpW---KKVIDNVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 GQPYD-RHRYQKVVKACSLLRDFKQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD--THVS-K 645
Cdd:PRK11247 105 GLKGQwRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPLGALDalTRIEmQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 383847295 646 HLFEECIQRYlaGKTRILATHQL-QYVKNVDAIILIEQGK 684
Cdd:PRK11247 174 DLIESLWQQH--GFTVLLVTHDVsEAVAMADRVLLIEEGK 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1161-1348 |
1.18e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1161 PGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDD--IDTGSIC-LEDLRRHISIIPQDPVlfsgtlrRNLDPFNEFS 1236
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESqGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPY-------ASLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1237 DAalweVLEEVELKDavVISGNGLESRV---LDR-----------GSNYSVGQRQLVCLARAILRNNKILMLDEATANVD 1302
Cdd:PRK10261 422 DS----IMEPLRVHG--LLPGKAAAARVawlLERvgllpehawryPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 383847295 1303 PQTDALIQN---TIRRKFtKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAE 1348
Cdd:PRK10261 496 VSIRGQIINlllDLQRDF-GIAYLFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
502-684 |
1.26e-11 |
|
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: 65.85 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYAGQEA-----WVFGS-------TVRQNIL 568
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEArrrlgFVSDStglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 -FGQPY--DRHRYQKVVKACSLLRDFKQFpqsdqtvVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSK 645
Cdd:cd03266 101 yFAGLYglKGDELTARLEELADRLGMEEL-------LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 383847295 646 HLFEECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03266 174 ALREFIRQLRALGKCILFSTHIMQEVERLcDRVVVLHRGR 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1156-1373 |
1.48e-11 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 66.51 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1156 NLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSIC---LEDLRRH-ISIIPQDPVLFSG-TLRRNL 1229
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1230 D--------PFNEFSDAALwEVLEEVelkdavvisgnGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANV 1301
Cdd:cd03294 124 AfglevqgvPRAEREERAA-EALELV-----------GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1302 DPQTDALIQNT---IRRKFTKcTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQNTYSQFTS-LVKETDRA 1373
Cdd:cd03294 192 DPLIRREMQDEllrLQAELQK-TIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDYVReFFRGVDRA 267
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
502-684 |
1.49e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 65.24 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEID--VVEGHVKVNGslsyagqeawvfgstvrQNILFGQPYDRHR-- 577
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKG-----------------EDITDLPPEERARlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 578 ----YQKV-----VKACSLLRDfkqfpqsdqtvVGErgsSLSGGQKARINLARSLYRQADVYLLDDPLSAVDThVSKHLF 648
Cdd:cd03217 79 iflaFQYPpeipgVKNADFLRY-----------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 383847295 649 EECIQRYL-AGKTRILATHQ---LQYVKnVDAIILIEQGK 684
Cdd:cd03217 144 AEVINKLReEGKSVLIITHYqrlLDYIK-PDRVHVLYDGR 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
502-684 |
1.75e-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: 65.82 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVfgstVRQNILFGQ---------P 572
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL----RRIGVVFGQktqlwwdlpV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 573 YD-----RH-------RYQKVVKACSLLRDFKQFpqSDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:cd03267 113 IDsfyllAAiydlppaRFKKRLDELSELLDLEEL--LDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 383847295 641 ThVSKHLFEECIQRYLA--GKTRILATHqlqYVKNVDA----IILIEQGK 684
Cdd:cd03267 186 V-VAQENIRNFLKEYNRerGTTVLLTSH---YMKDIEAlarrVLVIDKGR 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
502-684 |
2.11e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGeidvVEGHVkvNGSLSYAGQE-----------AWVFGS-------TV 563
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG----LEHQT--SGHIRFHGTDvsrlhardrkvGFVFQHyalfrhmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RQNILFG--------QPYDRHRYQKVVKacslLRDFKQFPQsdqtvVGER-GSSLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:PRK10851 92 FDNIAFGltvlprreRPNAAAIKAKVTQ----LLEMVQLAH-----LADRyPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 635 PLSAVDTHVSKHLfeeciQRYLAGK------TRILATH-QLQYVKNVDAIILIEQGK 684
Cdd:PRK10851 163 PFGALDAQVRKEL-----RRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGN 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
502-697 |
2.15e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.34 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------------SLSYAGQEAWVFGST 562
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkriGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGQPYDRHRYQKV-VKACSLLRDFKqFPQSdqtVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVkNYAHRLLMDLG-FSRD---VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 642 HvSKHLFEECIQRYLA--GKTRILATHQLQYV-KNVDAIILIEQGKATVFSHYQDLLSQ 697
Cdd:PRK13646 179 Q-SKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
483-684 |
2.21e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.17 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 483 AVKMTNFTAKWePGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------SLSYA-GQE 555
Cdd:PRK13632 7 MIKVENVSFSY-PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIrKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 556 AWVF--------GSTVRQNILFG---QPYDRHRYQKVVKACSLLRDFKQF----PQsdqtvvgergsSLSGGQKARINLA 620
Cdd:PRK13632 86 GIIFqnpdnqfiGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYldkePQ-----------NLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 621 RSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQ-RYLAGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITHDMDEAILADKVIVFSEGK 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
501-696 |
2.25e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.93 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS---------------LSYAGQEAWVFGSTVRQ 565
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnfeklrkhigIVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 566 NILFGQ-----PYDR-HRyqKVVKAcslLRDFKQFPQSDqtvvgERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAV 639
Cdd:PRK13648 104 DVAFGLenhavPYDEmHR--RVSEA---LKQVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 640 DTHVSKHLFeECIQRYLAGK--TRILATHQLQYVKNVDAIILIEQGKA-------TVFSHYQDLLS 696
Cdd:PRK13648 174 DPDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVykegtptEIFDHAEELTR 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1134-1347 |
2.42e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAlfrLAKVE----GVIEIDdidtGSIC--LEDL 1207
Cdd:PRK15439 11 LLCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKI---IAGIVppdsGTLEIG----GNPCarLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRH---ISIIPQDPVLFSG-TLRRNLD---PFNEFSDAALWEVLEE--VELKDAVviSGNGLEsrvldrgsnysVGQRQL 1278
Cdd:PRK15439 82 KAHqlgIYLVPQEPLLFPNlSVKENILfglPKRQASMQKMKQLLAAlgCQLDLDS--SAGSLE-----------VADRQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1279 VCLARAILRNNKILMLDEATANVDP-QTDALIQNtIRRKFTK-CTVLTIAHRLNTIMD-SDKVLVMDKGRMA 1347
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPaETERLFSR-IRELLAQgVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
501-708 |
2.49e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 67.05 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDnLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-----------------SLSYAGQEAWVFGS-T 562
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGQ-----PYDRHRYQKVVKAC---SLLrdfKQFPQSdqtvvgergssLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:COG4148 94 VRGNLLYGRkraprAERRISFDEVVELLgigHLL---DRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 635 PLSAVDTHvSKHLFEECIQRyLAGKTRI---LATHQLQYVKNV-DAIILIEQGKATVFSHYQDLLSqRPEYAELLAAE 708
Cdd:COG4148 160 PLAALDLA-RKAEILPYLER-LRDELDIpilYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS-RPDLLPLAGGE 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
502-684 |
2.73e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 64.74 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----------------SLSYAGQEAWVFGS-TVR 564
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPDrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILFGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGErgssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVS 644
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 383847295 645 KHLFEECIQRYLAGKTRILATHQLQYVKNVDA-IILIEQGK 684
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGK 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
502-684 |
2.85e-11 |
|
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: 65.15 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS--------------LSYAGQEAWVFGS-TVRQN 566
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 567 ILFGQPYDRHRYQkvvkacSLLRDFKQFPQSDQTV------VG------ERGSSLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:cd03219 96 VMVAAQARTGSGL------LLARARREEREARERAeellerVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 635 P---LSAVDTHVSKHLFEECIQRylaGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03219 170 PaagLNPEETEELAELIRELRER---GITVLLVEHDMDVVMSLaDRVTVLDQGR 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
502-684 |
2.92e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAW---------------VFGSTVRQN 566
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvglvfqdpddqVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 567 ILFGqPYD--------RHRYQKVVKACSLlRDFKQFPQSdqtvvgergsSLSGGQKARINLARSLYRQADVYLLDDPLSA 638
Cdd:PRK13647 101 VAFG-PVNmgldkdevERRVEEALKAVRM-WDFRDKPPY----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 383847295 639 VDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKN-VDAIILIEQGK 684
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGR 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1135-1352 |
3.02e-11 |
|
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: 64.95 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLisaLFRLAKVEGVieiddiDTGSICLEDL------- 1207
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTL---LRLIAGFETP------TSGEILLDGKditnlpp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 -RRHISIIPQDPVLF---------SGTLRRNLDPFNEFsDAALWEVLEEVELKdavvisgnGLESRvldRGSNYSVGQRQ 1277
Cdd:cd03300 70 hKRPVNTVFQNYALFphltvfeniAFGLRLKKLPKAEI-KERVAEALDLVQLE--------GYANR---KPSQLSGGQQQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAE------ 1348
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQigtpee 217
|
....*
gi 383847295 1349 -YDHP 1352
Cdd:cd03300 218 iYEEP 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1131-1352 |
3.21e-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: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1131 KDGMIRFRNVYMRYAEEELPVLK---GLNLVINPGEKIGIVGRTGAGKSSLisalfrlAKV-EGVIE------------- 1193
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTL-------SKIiAGVLEptsgevnvrvgde 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1194 -IDDIDTGSICLEDLRRHISIIPQDPVLFS-GTLRRNLdpfnefSDAALWEVLEEVELKDAV-VISGNGLESR----VLD 1266
Cdd:TIGR03269 349 wVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRTVLDNL------TEAIGLELPDELARMKAViTLKMVGFDEEkaeeILD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1267 R-GSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTI--RRKFTKCTVLTIAHRLNTIMD-SDKVLVMD 1342
Cdd:TIGR03269 423 KyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMR 502
|
250
....*....|
gi 383847295 1343 KGRMAEYDHP 1352
Cdd:TIGR03269 503 DGKIVKIGDP 512
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1152-1345 |
3.50e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAKVEGVIEID--DIDTGSIClEDLRRHISIIPQDPVLFSGT-- 1224
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTYEGEIIFEgeELQASNIR-DTERAGIAIIHQELALVKELsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1225 -----LRRNLDPFNEFSDAALW----EVLEEVELKDAVvisgnglESRVldrgSNYSVGQRQLVCLARAILRNNKILMLD 1295
Cdd:PRK13549 100 lenifLGNEITPGGIMDYDAMYlraqKLLAQLKLDINP-------ATPV----GNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1296 EATANV-DPQTDAL--IQNTIRRKFTKCtvLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:PRK13549 169 EPTASLtESETAVLldIIRDLKAHGIAC--IYISHKLNEVKAiSDTICVIRDGR 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
497-684 |
4.14e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.04 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 497 QSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAIlgeidvveghVKVN----GSLSYAGQEAWVFGS----------- 561
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF----------ARLLtpqsGTVFLGDKPISMLSSrqlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 ---------TVRQNILFGQ-PY----------DRHRYQKVVKACSLLrdfkqfpqsdqTVVGERGSSLSGGQKARINLAR 621
Cdd:PRK11231 83 qhhltpegiTVRELVAYGRsPWlslwgrlsaeDNARVNQAMEQTRIN-----------HLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 622 SLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQL-QYVKNVDAIILIEQGK 684
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGH 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
495-695 |
4.24e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.42 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYagQEAW--------VF------ 559
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmVLSE--ETVWdvrrqvgmVFqnpdnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 560 --GSTVRQNILF-----GQPYDR--HRYQKVVKACSLLRDFKQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVY 630
Cdd:PRK13635 94 fvGATVQDDVAFgleniGVPREEmvERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 631 LLDDPLSAVD-------THVSKHLFEEciqrylAGKTRILATHQLQYVKNVDAIILIEQGK-------ATVFSHYQDLL 695
Cdd:PRK13635 163 ILDEATSMLDprgrrevLETVRQLKEQ------KGITVLSITHDLDEAAQADRVIVMNKGEileegtpEEIFKSGHMLQ 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1135-1345 |
4.44e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 63.81 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDTGSICLEDlrRHISI 1213
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLF---------SGTLRRNLDPFNEFsDAALWEVLEEVELkdavvisgngleSRVLDR-GSNYSVGQRQLVCLAR 1283
Cdd:cd03301 77 VFQNYALYphmtvydniAFGLKLRKVPKDEI-DERVREVAELLQI------------EHLLDRkPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1284 AILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQ 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
502-669 |
5.71e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.67 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGhVKVNGSLSYAGQE---------------AWVFG------ 560
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPG-ARVEGEILLDGEDiydpdvdvvelrrrvGMVFQkpnpfp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 561 STVRQNILFG----QPYDRHRYQKVVKACslLRDfkqfpqsdqtvVG----------ERGSSLSGGQKARINLARSLYRQ 626
Cdd:COG1117 106 KSIYDNVAYGlrlhGIKSKSELDEIVEES--LRK-----------AAlwdevkdrlkKSALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 627 ADVYLLDDPLSAVDtHVSKHLFEECIQRyLAGK-TRILATHQLQ 669
Cdd:COG1117 173 PEVLLMDEPTSALD-PISTAKIEELILE-LKKDyTIVIVTHNMQ 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1135-1348 |
6.91e-11 |
|
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: 66.63 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNvymryAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSslISAL--FRL-----AKVEGVIEIDDIDTGSICLEDL 1207
Cdd:COG4172 14 VAFGQ-----GGGTVEAVKGVSFDIAAGETLALVGESGSGKS--VTALsiLRLlpdpaAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RR----HISIIPQDP----------------VLfsgTLRRNLdpfnefSDAALW----EVLEEVELKDAvvisgnglESR 1263
Cdd:COG4172 87 RRirgnRIAMIFQEPmtslnplhtigkqiaeVL---RLHRGL------SGAAARaralELLERVGIPDP--------ERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1264 vLDRgsnY----SVGQRQLVCLARAILRNNKILMLDEatanvdPQT--DALIQNTI-------RRKFtKCTVLTIAHRLN 1330
Cdd:COG4172 150 -LDA---YphqlSGGQRQRVMIAMALANEPDLLIADE------PTTalDVTVQAQIldllkdlQREL-GMALLLITHDLG 218
|
250
....*....|....*....
gi 383847295 1331 TIMD-SDKVLVMDKGRMAE 1348
Cdd:COG4172 219 VVRRfADRVAVMRQGEIVE 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1152-1363 |
7.46e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLR----RHISIIPQDPVLFSG-TL 1225
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1226 RRNLDPFNEFSDAALwevlEEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQT 1305
Cdd:PRK10070 124 LDNTAFGMELAGINA----EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1306 DALIQNTIRRKFTKC--TVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQNTYSQF 1363
Cdd:PRK10070 200 RTEMQDELVKLQAKHqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
496-704 |
8.83e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 496 GQSEnTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVN-----------GSLSYAGQEAWVFGSTvR 564
Cdd:PRK10619 16 GEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkdGQLKVADKNQLRLLRT-R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILFgQPYDRHRYQKVV--------------KACSLLRDFKQFPQS--DQTVVGERGSSLSGGQKARINLARSLYRQAD 628
Cdd:PRK10619 94 LTMVF-QHFNLWSHMTVLenvmeapiqvlglsKQEARERAVKYLAKVgiDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 629 VYLLDDPLSAVDTHVSKHLFEecIQRYLA--GKTRILATHQLQYVKNVDA-IILIEQGKATVFSHYQDLLSQrPEYAEL 704
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLR--IMQQLAeeGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFGN-PQSPRL 248
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
497-683 |
9.58e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 497 QSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEI---DVVEGHVKVNG-SLSYAG-----------QEAWVFGS 561
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrTVQREGrlardirksraNTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 -------TVRQNILFGQPYDRHRYQKVVKACSllRDFKQFPQSDQTVVG------ERGSSLSGGQKARINLARSLYRQAD 628
Cdd:PRK09984 95 fnlvnrlSVLENVLIGALGSTPFWRTCFSWFT--REQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 629 VYLLDDPLSAVDTHVSKHLFEECIQ-RYLAGKTRILATHQLQY-VKNVDAIILIEQG 683
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYaLRYCERIVALRQG 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
502-684 |
1.18e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGS-TVRQNI--LFGQP------ 572
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVgmVFQQPnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 573 --YDRHRYQKVVKACSLLRDFKQFPQSDQTVVG----------ERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:PRK14246 106 siYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlwkevydrlnSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 641 ThVSKHLFEECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:PRK14246 186 I-VNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGE 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1151-1358 |
1.23e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEIDDIDTGSICL-EDLRRHISIIPQDPVLFsgtlrRN 1228
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIF-----RR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1229 LDPFNEFsdAALWEVLEEVELKDAVVISGNGLE----SRVLDR-GSNYSVGQRQLVCLARAILRNNKILMLDEATANVDP 1303
Cdd:PRK10895 93 LSVYDNL--MAVLQIRDDLSAEQREDRANELMEefhiEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1304 QTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQN 1358
Cdd:PRK10895 171 ISVIDIKRIIEHlRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1144-1351 |
1.34e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1144 YAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSL---ISALfrLAKVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVL 1220
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLlkiVASL--ISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1221 FSGTLRRNLdpfnefsdAALWEVLEEVELKDAVV--ISGNGLESRVLDRGSN-YSVGQRQLVCLARAILRNNKILMLDEA 1297
Cdd:PRK10247 93 FGDTVYDNL--------IFPWQIRNQQPDPAIFLddLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1298 TANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMDSDKVLVMDK--GRMAEYDH 1351
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITLQPhaGEMQEARY 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
502-667 |
1.81e-10 |
|
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: 61.99 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLSYAGQEAWVFGS-TVRQNIL 568
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKPElSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPYDRHRYQKVVKACSL--LRDFKQFPqsdqtvvgerGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTH-VSK 645
Cdd:TIGR01189 96 FWAAIHGGAQRTIEDALAAvgLTGFEDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAgVAL 165
|
170 180
....*....|....*....|....
gi 383847295 646 --HLFEECIQRylaGKTRILATHQ 667
Cdd:TIGR01189 166 laGLLRAHLAR---GGIVLLTTHQ 186
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1135-1359 |
2.14e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.50 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEE---ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDD--IDTGSIC--LED 1206
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGErvITAGKKNkkLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1207 LRRHISIIPQDP--VLFSGTLRRNL--DPFNeF--SDaalwevlEEVELKDAVVISGNGLESRVLDRGS-NYSVGQRQLV 1279
Cdd:PRK13634 83 LRKKVGIVFQFPehQLFEETVEKDIcfGPMN-FgvSE-------EDAKQKAREMIELVGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1280 CLARAILRNNKILMLDEATANVDPQTdaliQNTIRRKFTKC------TVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHP 1352
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYKLhkekglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
....*..
gi 383847295 1353 HMLLQNT 1359
Cdd:PRK13634 231 REIFADP 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
501-698 |
2.21e-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: 62.81 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDNLNLEIEKGKIY--AVIGMVG---AGKSSFLSAILGEIDVVEGHVKV-NGSLSYAGQEAWV-FGSTVRQ------NI 567
Cdd:cd03237 9 TLGEFTLEVEGGSISesEVIGILGpngIGKTTFIKMLAGVLKPDEGDIEIeLDTVSYKPQYIKAdYEGTVRDllssitKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFGQPYDRHRYQKVVKACSLLrdfkqfpqsDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPlsavdthvSKHL 647
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQIL---------DREV-----PELSGGELQRVAIAACLSKDADIYLLDEP--------SAYL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 648 FEEciQRYLAGKtrilathqlqyvknvdaII--LIEQGKATVF--SH---YQDLLSQR 698
Cdd:cd03237 147 DVE--QRLMASK-----------------VIrrFAENNEKTAFvvEHdiiMIDYLADR 185
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1161-1356 |
2.24e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 63.97 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1161 PGEKI-GIVGRTGAGKSSLISA---LFRLAkvEGVIEIDD---IDTGS-ICLEDLRRHISIIPQDPVLFSG-TLRRNLdp 1231
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTLLRAiagLERPD--SGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFPHlSVRGNL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1232 fnEFSDAALWEVLEEVELkDAVV----ISGnglesrVLDRG-SNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTD 1306
Cdd:COG4148 99 --LYGRKRAPRAERRISF-DEVVellgIGH------LLDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1307 ALIQ---NTIRRKFtKCTVLTIAH------RLntimdSDKVLVMDKGRMAEYDHPHMLL 1356
Cdd:COG4148 170 AEILpylERLRDEL-DIPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
484-684 |
2.35e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.14 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQ--SENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------- 547
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 548 ---SLSYAGQEAWVFGSTVRQNILFGqPY-----DRHRYQKVVKACSL-------LRDFKQFpqsdqtvvgergsSLSGG 612
Cdd:PRK13637 83 kkvGLVFQYPEYQLFEETIEKDIAFG-PInlglsEEEIENRVKRAMNIvgldyedYKDKSPF-------------ELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 613 QKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEEcIQ----RYlaGKTRILATHQLQYV-KNVDAIILIEQGK 684
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK-IKelhkEY--NMTIILVSHSMEDVaKLADRIIVMNKGK 222
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
502-698 |
2.48e-10 |
|
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: 62.62 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------SLSYAGQEAWVFGSTVRQNIL 568
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDThVSKHLF 648
Cdd:cd03288 117 PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-ATENIL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 383847295 649 EECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQR 698
Cdd:cd03288 196 QKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1151-1363 |
2.53e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEID--DIDTGSIcledLRRHISIIPQDPVLFS----- 1222
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDgeDVTHRSI----QQRDICMVFQSYALFPhmslg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1223 ---GTLRRNLDPFNEFSDAALWEVLEEVELKdavvisgnGLESRVLDRGSNysvGQRQLVCLARAILRNNKILMLDEATA 1299
Cdd:PRK11432 97 envGYGLKMLGVPKEERKQRVKEALELVDLA--------GFEDRYVDQISG---GQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1300 NVDPQTDALIQNTIR--RKFTKCTVLTIAH-RLNTIMDSDKVLVMDKGRMAEYDHPHMLLQNTYSQF 1363
Cdd:PRK11432 166 NLDANLRRSMREKIRelQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
502-684 |
2.92e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.81 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYAGQEA----WVFGS-------TVRQNILF 569
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENrhvnTVFQSyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 GQpydrhRYQKVVKA--CSLLRDFKQFPQSDQTVvGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHL 647
Cdd:PRK09452 110 GL-----RMQKTPAAeiTPRVMEALRMVQLEEFA-QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 383847295 648 FEEC--IQRYLaGKTRILATH-QLQYVKNVDAIILIEQGK 684
Cdd:PRK09452 184 QNELkaLQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGR 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
502-640 |
2.92e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.48 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSL--SYAGQE------------AWVFGSTVRQNI 567
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPlaDWSPAElarrravlpqhsSLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFG-QPY--DRHRYQKVVKA------CSLLRDfKQFPQsdqtvvgergssLSGGQKARINLARSL---YRQAD---VYLL 632
Cdd:PRK13548 98 AMGrAPHglSRAEDDALVAAalaqvdLAHLAG-RDYPQ------------LSGGEQQRVQLARVLaqlWEPDGpprWLLL 164
|
....*...
gi 383847295 633 DDPLSAVD 640
Cdd:PRK13548 165 DEPTSALD 172
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
483-684 |
3.56e-10 |
|
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: 65.03 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 483 AVKMTNFTAKWEPgQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLS 550
Cdd:TIGR01257 928 GVCVKNLVKIFEP-SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 551 YAGQEAWVFGS-TVRQNILF-GQPYDRHRYQKVVKACSLLRDFKQFPQSDqtvvgERGSSLSGGQKARINLARSLYRQAD 628
Cdd:TIGR01257 1007 MCPQHNILFHHlTVAEHILFyAQLKGRSWEEAQLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 629 VYLLDDPLSAVDTHVSKHLFeECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIW-DLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGR 1137
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
502-696 |
3.57e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----------------SLSYAGQEAWVFGSTVRQ 565
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgirklvGIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 566 NILFGQ------PYD-RHRYQKVVKACSLLRDFKQFPQSdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSA 638
Cdd:PRK13644 98 DLAFGPenlclpPIEiRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 639 VDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLS 696
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
502-684 |
3.59e-10 |
|
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: 61.62 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLS------------AILGEIDVVEGHVKVNGSLSYAGQEAWVFGS-TVRQNI- 567
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKmlttllkptsgrATVAGHDVVREPREVRRRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 ----LFGQPYD--RHRYQKVVKACSLLrDFKqfpqsDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:cd03265 96 iharLYGVPGAerRERIDELLDFVGLL-EAA-----DRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 383847295 642 HVSKHLFEEcIQRYLA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:cd03265 165 QTRAHVWEY-IEKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGR 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1146-1305 |
3.97e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1146 EEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-------VEGViEIDDIDTGSicLEDLRR-HISIIPQD 1217
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKptsgtyrVAGQ-DVATLDADA--LAQLRReHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1218 PVLFSgtlrrNLDPFNEFSDAALWEVLEEVE-LKDAVVISGN-GLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLD 1295
Cdd:PRK10535 95 YHLLS-----HLTAAQNVEVPAVYAGLERKQrLLRAQELLQRlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170
....*....|
gi 383847295 1296 EATANVDPQT 1305
Cdd:PRK10535 170 EPTGALDSHS 179
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
499-688 |
4.47e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 499 ENTLDNLNLEIE-----KGkIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSL-----------------SYAGQEA 556
Cdd:PRK11144 7 KQQLGDLCLTVNltlpaQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 557 WVFGS-TVRQNILFG-QPYDRHRYQKVVKACSLLRDFKQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:PRK11144 86 RLFPHyKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 635 PLSAVDTHVSKHL--FEECIQRYLagKTRIL-ATHQLQYVKNV-DAIILIEQGKATVF 688
Cdd:PRK11144 155 PLASLDLPRKRELlpYLERLAREI--NIPILyVSHSLDEILRLaDRVVVLEQGKVKAF 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1151-1309 |
4.74e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEIDDIDTGSIC---LEDLRRHISIIPQDPvlfSGTLRR 1227
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1228 NLDPFN---------------EFSDAALWEVLEEVelkdavvisgnGLESRVLDR-GSNYSVGQRQLVCLARAILRNNKI 1291
Cdd:PRK15134 378 RLNVLQiieeglrvhqptlsaAQREQQVIAVMEEV-----------GLDPETRHRyPAEFSGGQRQRIAIARALILKPSL 446
|
170
....*....|....*...
gi 383847295 1292 LMLDEATANVDPQTDALI 1309
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQI 464
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1135-1352 |
4.75e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.86 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALfrlAKVE----GVIEIDDIDTGSIcLEDLRRH 1210
Cdd:COG1118 3 IEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGLEtpdsGRIVLNGRDLFTN-LPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLFsgtlrRNLD-------------PFNEFSDAALWEVLEEVELkdavvisgNGLESRvldRGSNYSVGQRQ 1277
Cdd:COG1118 77 VGFVFQHYALF-----PHMTvaeniafglrvrpPSKAEIRARVEELLELVQL--------EGLADR---YPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1278 LVCLARAILRNNKILMLDEATANVdpqtDALIQNTIRR------KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAE-- 1348
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGAL----DAKVRKELRRwlrrlhDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQvg 216
|
....*....
gi 383847295 1349 -----YDHP 1352
Cdd:COG1118 217 tpdevYDRP 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1135-1350 |
5.33e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.01 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRY--------------------AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRlakvegvieI 1194
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG---------I 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1195 DDIDTGSIcledlRRHISIIP--------------QDPVLFSGTLrRNLDPfnEFSDAALWEVLEEVELKDAvvisgngL 1260
Cdd:cd03220 72 YPPDSGTV-----TVRGRVSSllglgggfnpeltgRENIYLNGRL-LGLSR--KEIDEKIDEIIEFSELGDF-------I 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1261 ESRVldrgSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTKC-TVLTIAHRLNTIMD-SDKV 1338
Cdd:cd03220 137 DLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRA 212
|
250
....*....|..
gi 383847295 1339 LVMDKGRMAEYD 1350
Cdd:cd03220 213 LVLEKGKIRFDG 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1134-1346 |
6.47e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.66 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEElPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVI-----EIDDIDTGSICLedL 1207
Cdd:PRK10908 1 MIRFEHVSKAYLGGR-QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERpSAGKIwfsghDITRLKNREVPF--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDP-VLFSGTLRRNLDPFNEFSDAALwevlEEVELKDAVVISGNGLesrvLDRGSNYSV----GQRQLVCLA 1282
Cdd:PRK10908 78 RRQIGMIFQDHhLLMDRTVYDNVAIPLIIAGASG----DDIRRRVSAALDKVGL----LDKAKNFPIqlsgGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1283 RAILRNNKILMLDEATANVDpqtDALIQNTIR--RKFTK--CTVLTIAHRLNTIMDSD-KVLVMDKGRM 1346
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLD---DALSEGILRlfEEFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1134-1358 |
6.81e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDID-TGSICLEDLRRHI 1211
Cdd:PRK11614 5 MLSFDKVSAHYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAtSGRIVFDGKDiTDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 SIIPQDPVLFSG-TLRRNLDPFNEFSDAALWEvlEEVElkdAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNK 1290
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQ--ERIK---WVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQN 1358
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1148-1359 |
8.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1148 ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-----AKVEGVIEIDDIDTGSICLE----------------- 1205
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtGTIEWIFKDEKNKKKTKEKEkvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1206 ---DLRRHISIIPQ--DPVLFSGTLRRNLdpfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGS-NYSVGQRQLV 1279
Cdd:PRK13651 99 kikEIRRRVGVVFQfaEYQLFEQTIEKDI----IFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1280 CLARAILRNNKILMLDEATANVDPQTDALIQNtIRRKFTKC--TVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLL 1356
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQgkTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDTYDIL 253
|
...
gi 383847295 1357 QNT 1359
Cdd:PRK13651 254 SDN 256
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1143-1348 |
9.29e-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: 59.85 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1143 RYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK---VEGVIEIDDIDTGSICLED-LRRHISIIPQDP 1218
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEILFKGEDITDLPPEErARLGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1219 VLFSGtlrrnldpfnefsdaalwevleeVELKDAVvisgnglesRVLDRGsnYSVGQRQLVCLARAILRNNKILMLDEAT 1298
Cdd:cd03217 87 PEIPG-----------------------VKNADFL---------RYVNEG--FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1299 ANVDpqTDAL--IQNTIRR-KFTKCTVLTIAH--RLNTIMDSDKVLVMDKGRMAE 1348
Cdd:cd03217 133 SGLD--IDALrlVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1138-1330 |
1.19e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1138 RNVYMRYAEEEL--PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLakvegvieiDDIDTGSICLE---------- 1205
Cdd:PRK11629 9 DNLCKRYQEGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---------DTPTSGDVIFNgqpmsklssa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1206 ---DLR-RHISIIPQdpvlfsgtLRRNLDPFNEFSDAALWEVL-----EEVELKDAVVISGNGLESRVLDRGSNYSVGQR 1276
Cdd:PRK11629 80 akaELRnQKLGFIYQ--------FHHLLPDFTALENVAMPLLIgkkkpAEINSRALEMLAAVGLEHRANHRPSELSGGER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQT-DA---LIQNTIRRKFTKCTVLT----IAHRLN 1330
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNaDSifqLLGELNRLQGTAFLVVThdlqLAKRMS 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
471-698 |
1.22e-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: 62.49 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 471 RSSSIRINE-EPYAVKMTNFTAKWepGQSENTLDNLNLEIEKGKIYA--VIGMVGA---GKSSFLSAILGEIDVVEGHVK 544
Cdd:COG1245 321 RDEPIEFEVhAPRREKEEETLVEY--PDLTKSYGGFSLEVEGGEIREgeVLGIVGPngiGKTTFAKILAGVLKPDEGEVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 545 VNGSLSYAGQ--EAWVFGsTVRQNI--LFGQPYDRHRYQ-KVVKACSLLRDFkqfpqsDQTVvgergSSLSGGQKARINL 619
Cdd:COG1245 399 EDLKISYKPQyiSPDYDG-TVEEFLrsANTDDFGSSYYKtEIIKPLGLEKLL------DKNV-----KDLSGGELQRVAI 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 620 ARSLYRQADVYLLDDPlsavdthvSKHLFEEciQRYLAGKTrilathqlqyVKNVdaiilIEQGKATVF--SH---YQDL 694
Cdd:COG1245 467 AACLSRDADLYLLDEP--------SAHLDVE--QRLAVAKA----------IRRF-----AENRGKTAMvvDHdiyLIDY 521
|
....
gi 383847295 695 LSQR 698
Cdd:COG1245 522 ISDR 525
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
817-1010 |
1.23e-09 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 61.27 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 817 TYLLQQtalnATNETSTENLDISSM-YNYMYIYTAIVVGLFCIGITRSLTFYEVCIVCSQK-LHDM---AFSALIRTGMR 891
Cdd:cd18547 19 PYLLGK----AIDLIIEGLGGGGGVdFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRtVYDLrkdLFEKLQRLPLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 892 FFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGTVF--YWIRKVYL 963
Cdd:cd18547 95 YFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPlltlivLVTVPLSLLVTKFiaKRSQKYFR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 383847295 964 KTSKNIKRLEGmsrspvftHLNATLNGLTTIRAYCAQDILKKEFDKL 1010
Cdd:cd18547 175 KQQKALGELNG--------YIEEMISGQKVVKAFNREEEAIEEFDEI 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1152-1381 |
1.53e-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: 62.15 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSL---ISALFRLAKVEGVIEIDDIDTGSICLEDL-RRHISIIPQDPVLFSG-TLR 1226
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1227 RNLDPFNEFS-------DAALW----EVLEEVELKDAVVisgngleSRVLdrgSNYSVGQRQLVCLARAILRNNKILMLD 1295
Cdd:TIGR02633 97 ENIFLGNEITlpggrmaYNAMYlrakNLLRELQLDADNV-------TRPV---GDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1296 EATANVDPQTDALIQNTIR---RKFTKCtvLTIAHRLNTIMD-SDKVLVMDKGR------MAEYDHPHMLLQNTYSQFTS 1365
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRdlkAHGVAC--VYISHKLNEVKAvCDTICVIRDGQhvatkdMSTMSEDDIITMMVGREITS 244
|
250
....*....|....*.
gi 383847295 1366 LVKETDRAMFDQLVRI 1381
Cdd:TIGR02633 245 LYPHEPHEIGDVILEA 260
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1133-1358 |
1.57e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1133 GMIRFRNVYMRYAEE---ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-------------GVIEIDD 1196
Cdd:PRK13645 5 KDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivgdyaipaNLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1197 IdtgsiclEDLRRHISIIPQDP--VLFSGTLRRNLdpfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGS-NYSV 1273
Cdd:PRK13645 85 V-------KRLRKEIGLVFQFPeyQLFQETIEKDI----AFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1274 GQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYD 1350
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIG 233
|
....*...
gi 383847295 1351 HPHMLLQN 1358
Cdd:PRK13645 234 SPFEIFSN 241
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
842-1009 |
1.62e-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: 60.51 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 842 YNYMYIYTAIVVGLFcigITRSLTFY--EVCIV-CSQK-LHDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDE 914
Cdd:cd18552 35 LEALLLVPLAIIGLF---LLRGLASYlqTYLMAyVGQRvVRDLrndLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 915 LLPKAVLDAGQICMMMFGSLAVSCIVNP-LFLIPIVFLGTVFYWIRKVylktSKNIKRL-----EGMSRspVFTHLNATL 988
Cdd:cd18552 112 ALTSALTVLVRDPLTVIGLLGVLFYLDWkLTLIALVVLPLAALPIRRI----GKRLRKIsrrsqESMGD--LTSVLQETL 185
|
170 180
....*....|....*....|.
gi 383847295 989 NGLTTIRAYCAQDILKKEFDK 1009
Cdd:cd18552 186 SGIRVVKAFGAEDYEIKRFRK 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1134-1346 |
1.78e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEID--DIDTGSICLEDLRRH 1210
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKgePIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDP--VLFSGTLRRNL--DPFNefsdaaLWEVLEEVE--LKDAV-VISGNGLESRVldrGSNYSVGQRQLVCLAR 1283
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVafGPLN------LGLSKEEVEkrVKEALkAVGMEGFENKP---PHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1284 AILRNNKILMLDEATANVDPQTDALIQNTIRRKFTK-CTVLTIAHRLNTI-MDSDKVLVMDKGRM 1346
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVpVYADKVYVMSDGKI 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1147-1350 |
1.90e-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: 59.65 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1147 EELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHISIIPQD-------P 1218
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKtqlwwdlP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1219 VLFSGTLRR---NLDPFnEFSD--AALWEVLEEVELKDAVVisgnglesRVLdrgsnySVGQRQLVCLARAILRNNKILM 1293
Cdd:cd03267 112 VIDSFYLLAaiyDLPPA-RFKKrlDELSELLDLEELLDTPV--------RQL------SLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1294 LDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAeYD 1350
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL-YD 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
466-684 |
2.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.63 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 466 MEEKKRSSSIRINEEPYAVKmtNFTAKWEPGQSEN--TLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEI------- 536
Cdd:PRK13631 6 MKKKLKVPNPLSDDIILRVK--NLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygti 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 537 ---DVVEG-HVKVNGSLSYAGQ--------------------EAWVFGSTVRQNILFGQ-PYDRHRYQKVVKACSLLRDF 591
Cdd:PRK13631 84 qvgDIYIGdKKNNHELITNPYSkkiknfkelrrrvsmvfqfpEYQLFKDTIEKDIMFGPvALGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 592 KQfpqsDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYV 671
Cdd:PRK13631 164 GL----DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHV 239
|
250
....*....|....
gi 383847295 672 KNV-DAIILIEQGK 684
Cdd:PRK13631 240 LEVaDEVIVMDKGK 253
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
831-1014 |
2.29e-09 |
|
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: 60.22 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 831 TSTENLDISSMYNYMYIYTAIVVGLFCIGitrSLTFYeVCIVC--------SQKLHDMAFSALIRTGMRFFDTNPSGRIL 902
Cdd:cd18573 26 ASKESGDIEIFGLSLKTFALALLGVFVVG---AAANF-GRVYLlriageriVARLRKRLFKSILRQDAAFFDKNKTGELV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 903 NRFSKDMGTIDELLPKAVLD--------AGQICMMMFGSLAVSCIVnpLFLIPIVFLGTVFY--WIRKVYLKTSKNIKRL 972
Cdd:cd18573 102 SRLSSDTSVVGKSLTQNLSDglrslvsgVGGIGMMLYISPKLTLVM--LLVVPPIAVGAVFYgrYVRKLSKQVQDALADA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 383847295 973 EGMSrspvfthlNATLNGLTTIRAYCAQDILKKEF-DKLQDVH 1014
Cdd:cd18573 180 TKVA--------EERLSNIRTVRAFAAERKEVERYaKKVDEVF 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1143-1365 |
2.33e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1143 RYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLF 1221
Cdd:PRK10619 14 RYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1222 SgTLRRNLDPFNEFSD-AALWEVLE---------EVELKDAVV--ISGNGLESRVLDR-GSNYSVGQRQLVCLARAILRN 1288
Cdd:PRK10619 92 T-RLTMVFQHFNLWSHmTVLENVMEapiqvlglsKQEARERAVkyLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1289 NKILMLDEATANVDPQtdaLIQNTIR--RKFTK--CTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQNTYS-- 1361
Cdd:PRK10619 171 PEVLLFDEPTSALDPE---LVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQSpr 247
|
....*.
gi 383847295 1362 --QFTS 1365
Cdd:PRK10619 248 lqQFLK 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
501-698 |
2.48e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDNLNLEIEKGKIYA--VIGMVGA---GKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWV-FGSTVRQnILFGQP-- 572
Cdd:PRK13409 349 KLGDFSLEVEGGEIYEgeVIGIVGPngiGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPdYDGTVED-LLRSITdd 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 573 YDRHRYQ-KVVKACSLLRDFkqfpqsDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPlsavdthvSKHLFEEc 651
Cdd:PRK13409 428 LGSSYYKsEIIKPLQLERLL------DKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEP--------SAHLDVE- 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 652 iQRYLAGKT--RIlathqlqyvknvdaiilIEQGKATVF--SH---YQDLLSQR 698
Cdd:PRK13409 488 -QRLAVAKAirRI-----------------AEEREATALvvDHdiyMIDYISDR 523
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
501-669 |
3.10e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAI--LGEIDvveGHVKVNGSLSYAG---------------------QEAW 557
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLN---PEVTITGSIVYNGhniysprtdtvdlrkeigmvfQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 558 VFGSTVRQNILFG----QPYDRHRYQKVV----KACSLLRDFKQfpqsdqtVVGERGSSLSGGQKARINLARSLYRQADV 629
Cdd:PRK14239 97 PFPMSIYENVVYGlrlkGIKDKQVLDEAVekslKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 383847295 630 YLLDDPLSAVDThVSKHLFEECIQRYLAGKTRILATHQLQ 669
Cdd:PRK14239 170 ILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
502-684 |
3.29e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.76 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-------------------LSYAGQEAWVFGST 562
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvgLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGqPYDRHRYQKvvKACSLLRDFKQFPQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTH 642
Cdd:PRK13649 103 VLKDVAFG-PQNFGVSQE--EAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 383847295 643 VSKHLFEECIQRYLAGKTRILATHQLQYVKN-VDAIILIEQGK 684
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGK 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
488-720 |
6.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 488 NFTAKWEPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------------------S 548
Cdd:PRK13643 8 NYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvrkkvG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 549 LSYAGQEAWVFGSTVRQNILFG-QPY--DRHRYQKVV-KACSLLRDFKQFPQSDQTvvgergsSLSGGQKARINLARSLY 624
Cdd:PRK13643 88 VVFQFPESQLFEETVLKDVAFGpQNFgiPKEKAEKIAaEKLEMVGLADEFWEKSPF-------ELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 625 RQADVYLLDDPLSAVDTHVS---KHLFEECIQrylAGKTRILATHQLQYVKN-VDAIILIEQGKATVFSHYQDLLsQRPE 700
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARiemMQLFESIHQ---SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF-QEVD 236
|
250 260
....*....|....*....|..
gi 383847295 701 Y--AELLAAENETHDDSSLEKS 720
Cdd:PRK13643 237 FlkAHELGVPKATHFADQLQKT 258
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
502-694 |
6.44e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.88 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQ-------------------EAWVFGST 562
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkklkplrkkvgivfqfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGqPYD--------RHRYQKVVKACSLlrdfkqfpqsDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:PRK13634 103 VEKDICFG-PMNfgvseedaKQKAREMIELVGL----------PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 635 PLSAVDTHVSKHL---FEECIQRylAGKTRILATHQLQYVKN-VDAIILIEQG--KAT-----VFSHYQDL 694
Cdd:PRK13634 172 PTAGLDPKGRKEMmemFYKLHKE--KGLTTVLVTHSMEDAARyADQIVVMHKGtvFLQgtpreIFADPDEL 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
500-671 |
6.57e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 500 NTLDNLNLEIEKGKIYAVIGMVGAGKSSF---LSAIL----GEIDVV--------------EGHVKVNGSLSYAGQ---- 554
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtGTIEWIfkdeknkkktkekeKVLEKLVIQKTRFKKikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 555 --------------EAWVFGSTVRQNILFG-------QPYDRHRYQKVVKACSLLRDFKQ---FpqsdqtvvgergsSLS 610
Cdd:PRK13651 101 keirrrvgvvfqfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDESYLQrspF-------------ELS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 611 GGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYV 671
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNV 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1148-1345 |
7.11e-09 |
|
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: 57.83 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1148 ELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFR--LAKvEGVIEIDDiDTGSICLE--------DLRRH------- 1210
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPD-SGSILVRH-DGGWVDLAqaspreilALRRRtigyvsq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 -ISIIPQ--------DPVLFSGT------------LRR-NLDPfnefsdaALWEVLEevelkdavvisgnglesrvldrg 1268
Cdd:COG4778 101 fLRVIPRvsaldvvaEPLLERGVdreearararelLARlNLPE-------RLWDLPP----------------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1269 SNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDA----LIQNTIRRkftKCTVLTIAHRLNTiMD--SDKVLVMD 1342
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAvvveLIEEAKAR---GTAIIGIFHDEEV-REavADRVVDVT 226
|
...
gi 383847295 1343 KGR 1345
Cdd:COG4778 227 PFS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1146-1305 |
7.38e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.87 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1146 EEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLakvegvieiDDIDTGSICL---------EDLR-----RHI 1211
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---------DDGSSGEVSLvgqplhqmdEEARaklraKHV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1212 S-------IIP--------QDPVLFSGTLRRNldpfnefSDAALWEVLEEVelkdavvisgnGLESRVLDRGSNYSVGQR 1276
Cdd:PRK10584 91 GfvfqsfmLIPtlnalenvELPALLRGESSRQ-------SRNGAKALLEQL-----------GLGKRLDHLPAQLSGGEQ 152
|
170 180
....*....|....*....|....*....
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQT 1305
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
498-692 |
7.48e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 498 SENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAIlgeiDVVEghVKVNGSLSYAGQE-------------------AWV 558
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL----NLLE--MPRSGTLNIAGNHfdfsktpsdkairelrrnvGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 559 FGS-------TVRQNIL--------FGQPYDRHRYQKVVKACSLLRDFKQFPQSdqtvvgergssLSGGQKARINLARSL 623
Cdd:PRK11124 88 FQQynlwphlTVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFPLH-----------LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 624 YRQADVYLLDDPLSAVDTHVSKHLFEecIQRYLA--GKTRILATHQLQYVKNVDAIIL-------IEQGKATVFSHYQ 692
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVS--IIRELAetGITQVIVTHEVEVARKTASRVVymenghiVEQGDASCFTQPQ 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
504-684 |
8.40e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 504 NLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEA-----WVFGS-------TVRQNILFG- 570
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergvgMVFQSyalyphlSVAENMSFGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 571 ---QPYDRHRYQKVVKACSLLrdfkqfpQSDQtVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT------ 641
Cdd:PRK11000 101 klaGAKKEEINQRVNQVAEVL-------QLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqm 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 383847295 642 --HVSKhlfeecIQRYLaGKTRILATH-QLQYVKNVDAIILIEQGK 684
Cdd:PRK11000 173 riEISR------LHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGR 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
502-684 |
9.05e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.12 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSaILGEIDVveghvKVNGSLSYAGQEAwvfgSTVRQNIL-------FGQPYD 574
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDK-----PTSGTYRVAGQDV----ATLDADALaqlrrehFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 575 RH----------------------RYQKVVKACSLLrdfKQFPQSDQtvVGERGSSLSGGQKARINLARSLYRQADVYLL 632
Cdd:PRK10535 94 RYhllshltaaqnvevpavyagleRKQRLLRAQELL---QRLGLEDR--VEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 633 DDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
502-689 |
1.04e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEI--DVVEGHVKVngslsyagqeaWVFGSTVRQNIL--FGQPYDRHR 577
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-----------PDNQFGREASLIdaIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 578 YQKVVKACSL------LRDFKQfpqsdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHL---F 648
Cdd:COG2401 115 AVELLNAVGLsdavlwLRRFKE---------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVarnL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 383847295 649 EECIQRylAGKTRILATHQLQYVKNVDAIILIEQGKATVFS 689
Cdd:COG2401 180 QKLARR--AGITLVVATHHYDVIDDLQPDLLIFVGYGGVPE 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
882-1093 |
1.09e-08 |
|
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: 57.96 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 882 FSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDA--------GQICMMMFGSLAVSCIVnpLFLIPIVFLGT 953
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLlrnilqviGGLIILFILSWKLTLVL--LLVIPLLLIAS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 954 VFY--WIRKVYLKTSKNIKRLEgmsrspvfTHLNATLNGLTTIRAYCAQDILKKEFD-KLQDVHTSTVYMYVVSSSGFGF 1030
Cdd:cd18557 154 KIYgrYIRKLSKEVQDALAKAG--------QVAEESLSNIRTVRSFSAEEKEIRRYSeALDRSYRLARKKALANALFQGI 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 1031 -SLDIFCFVFTSLVTFSFLLLEQSFSGGEvglaITQVMAMTGMIQWGMRQNAEAANQMM----AVERV 1093
Cdd:cd18557 226 tSLLIYLSLLLVLWYGGYLVLSGQLTVGE----LTSFILYTIMVASSVGGLSSLLADIMkalgASERV 289
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
502-685 |
1.12e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.20 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-LSYAGQEAwvFG-----------STVRQNIL- 568
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpLDPEDRRR--IGylpeerglypkMKVGEQLVy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQ--PYDRHRYQKVVKAcsLLRDFKqfpqsdqtvVGERG----SSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTh 642
Cdd:COG4152 95 LARlkGLSKAEAKRRADE--WLERLG---------LGDRAnkkvEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 383847295 643 VSKHLFEECIqRYLA--GKTRILATHQLQYV-KNVDAIILIEQGKA 685
Cdd:COG4152 163 VNVELLKDVI-RELAakGTTVIFSSHQMELVeELCDRIVIINKGRK 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
498-697 |
1.18e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 498 SENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS---------------LSYAGQEAWVFGST 562
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGqPYD--------RHRYQKVVKACSLLRDFKQFPQSdqtvvgergssLSGGQKARINLARSLYRQADVYLLDD 634
Cdd:PRK13652 96 VEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 635 PLSAVDTHVSKHLFE---ECIQRYlaGKTRILATHQLQYVKNV-DAIILIEQGKATVFSHYQDLLSQ 697
Cdd:PRK13652 164 PTAGLDPQGVKELIDflnDLPETY--GMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
484-704 |
1.20e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLsYAGQEAW------ 557
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWdirhki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 558 --VF--------GSTVRQNILFGQ-----PYDRHRyQKVVKACSL--LRDFKQfpqsdqtvvgERGSSLSGGQKARINLA 620
Cdd:PRK13650 84 gmVFqnpdnqfvGATVEDDVAFGLenkgiPHEEMK-ERVNEALELvgMQDFKE----------REPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 621 RSLYRQADVYLLDDPLSAVDTHVSKHLF---EECIQRYlaGKTRILATHQLQYVKNVDAIILIEQGKATVFSHYQDLLSQ 697
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIktiKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 383847295 698 RPEYAEL 704
Cdd:PRK13650 231 GNDLLQL 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
502-684 |
1.30e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.20 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAW--------------VFGS-TVRQN 566
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimreavaivpegrrVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 567 ILFGQPY-DRHRYQKVVKacsllRDFKQFPQSDQTVVgERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSK 645
Cdd:PRK11614 101 LAMGGFFaERDQFQERIK-----WVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 383847295 646 HLFEECIQRYLAGKTRILATHQL-QYVKNVDAIILIEQGK 684
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGH 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1152-1364 |
1.43e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.48 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL------AKVEGVIEIDD--IDTGSICLEDLRRHISIIPQDPVLFSG 1223
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVEGKVTFHGknLYAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1224 TLRRN-------------LDPFNEFS--DAALWEvleevELKDAVVISGNGLesrvldrgsnySVGQRQLVCLARAILRN 1288
Cdd:PRK14243 106 SIYDNiaygaringykgdMDELVERSlrQAALWD-----EVKDKLKQSGLSL-----------SGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1289 NKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMD-SDKVLVMD---------KGRMAEYDHPHMLLQN 1358
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARvSDMTAFFNveltegggrYGYLVEFDRTEKIFNS 249
|
....*.
gi 383847295 1359 TYSQFT 1364
Cdd:PRK14243 250 PQQQAT 255
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
493-707 |
1.57e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 493 WEPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYAGQEAWvfgSTVRQNI--LF 569
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEW---RAVRSDIqmIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 GQPYdrhryqkvvkaCSL-------------LRDFkqFPQSDQTVVGERGSSL------------------SGGQKARIN 618
Cdd:PRK15079 105 QDPL-----------ASLnprmtigeiiaepLRTY--HPKLSRQEVKDRVKAMmlkvgllpnlinryphefSGGQCQRIG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 619 LARSLYRQADVYLLDDPLSAVDTHVSK---HLFEEcIQRYLaGKTRILATHQLQYVKNV-DAIILIEQGKATVFSHYQDL 694
Cdd:PRK15079 172 IARALILEPKLIICDEPVSALDVSIQAqvvNLLQQ-LQREM-GLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
250
....*....|....*
gi 383847295 695 LS--QRPEYAELLAA 707
Cdd:PRK15079 250 YHnpLHPYTKALMSA 264
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
502-684 |
1.84e-08 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 57.02 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIdvveghvkvngslsY--AGQEAWVFGST--------VRQNILF-- 569
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDL--------------PptYGNDVRLFGERrggedvweLRKRIGLvs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 570 ---GQPYDRH----------------RYQKV-----VKACSLLRDFKQFPQSDQTVvgergSSLSGGQKARINLARSLYR 625
Cdd:COG1119 85 palQLRFPRDetvldvvlsgffdsigLYREPtdeqrERARELLELLGLAHLADRPF-----GTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383847295 626 QADVYLLDDPLSAVDTHvSKHLFEECIQRyLAG---KTRILATHQLQYV-KNVDAIILIEQGK 684
Cdd:COG1119 160 DPELLILDEPTAGLDLG-ARELLLALLDK-LAAegaPTLVLVTHHVEEIpPGITHVLLLKDGR 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1134-1195 |
1.87e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.63 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRY--------------------AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAlfrLAKV----E 1189
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKL---IAGIleptS 80
|
....*.
gi 383847295 1190 GVIEID 1195
Cdd:COG1134 81 GRVEVN 86
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1150-1378 |
2.15e-08 |
|
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: 57.17 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIeiddidtgsicledlrRH---ISIIPQDPVLFSGTL 1225
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKI----------------KHsgrISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1226 RRNL------DPFNEFS---DAALWEVLEEVELKDAVVISGNGLesrvldrgsNYSVGQRQLVCLARAILRNNKILMLDE 1296
Cdd:cd03291 115 KENIifgvsyDEYRYKSvvkACQLEEDITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1297 ATANVDPQTDALIqntirrkFTKC--------TVLTIAHRLNTIMDSDKVLVMDKGRMAEYDhPHMLLQNTYSQFTSLVK 1368
Cdd:cd03291 186 PFGYLDVFTEKEI-------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYG-TFSELQSLRPDFSSKLM 257
|
250
....*....|
gi 383847295 1369 ETDRamFDQL 1378
Cdd:cd03291 258 GYDT--FDQF 265
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
502-667 |
2.17e-08 |
|
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: 55.96 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG------------SLSYAGQEAWVFGS-TVRQNIL 568
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiarGLLYLGHAPGIKTTlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FGQPYdrHRYQKVVKACSL--LRDFKQFPqsdqtvvgerGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKH 646
Cdd:cd03231 96 FWHAD--HSDEQVEEALARvgLNGFEDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA-GVA 162
|
170 180
....*....|....*....|..
gi 383847295 647 LFEECIQRYLA-GKTRILATHQ 667
Cdd:cd03231 163 RFAEAMAGHCArGGMVVLTTHQ 184
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1134-1357 |
3.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.67 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELPVLKGL---NLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSIC----LE 1205
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALfdiDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1206 DLRRHISIIPQDP--VLFSGTLRRNLdpfnEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRGS-NYSVGQRQLVCLA 1282
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDV----AFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1283 RAILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQ 1357
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
502-640 |
3.52e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.35 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGeidVVEGHVKVNGSLSYAGQEAWVFGSTVRQNILFGQPYDRHRYQKV 581
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 582 VKAcslLRDFKQFPQSDQTVvgeRGssLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:cd03233 100 VRE---TLDFALRCKGNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
502-640 |
4.18e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEID--------VVEGHVKVNGS----------------LSYAGQEAW 557
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEplaaidaprlarlravLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 558 VFgsTVRQNILFGQ-PYDR------HRYQKVVKACSLLRDfkqfpqsDQTVVGERGSSLSGGQKARINLARSL------- 623
Cdd:PRK13547 97 AF--SAREIVLLGRyPHARragaltHRDGEIAWQALALAG-------ATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170
....*....|....*....
gi 383847295 624 --YRQADVYLLDDPLSAVD 640
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALD 186
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1155-1350 |
4.30e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.81 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1155 LNLVIN---PGEKI-GIVGRTGAGKSSLISALFRLAKV-EGVIEIDD---IDTGS-ICLEDLRRHISIIPQDPVLF---- 1221
Cdd:PRK11144 13 LCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPqKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFphyk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1222 -SGTLRRNLDPFN--EFSDaalwevleevelkdavVISGNGLESrVLDR-GSNYSVGQRQLVCLARAILRNNKILMLDEA 1297
Cdd:PRK11144 93 vRGNLRYGMAKSMvaQFDK----------------IVALLGIEP-LLDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1298 TANVD-PQTDALIQ--NTIRRKFtKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYD 1350
Cdd:PRK11144 156 LASLDlPRKRELLPylERLAREI-NIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1131-1352 |
4.42e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1131 KDGMIRFRNVYMRYaeEELPVLKGLNLVINPGEKIGIVGRTGAGKSS---LISALFRLAkvEGVIEIDDIDTGSICLEdl 1207
Cdd:PRK09452 11 LSPLVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTvlrLIAGFETPD--SGRIMLDGQDITHVPAE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 RRHISIIPQDPVLFSG-TLRRNLD--------PFNEFSDAALwEVLEEVELKDavvisgngLESRvldRGSNYSVGQRQL 1278
Cdd:PRK09452 85 NRHVNTVFQSYALFPHmTVFENVAfglrmqktPAAEITPRVM-EALRMVQLEE--------FAQR---KPHQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1279 VCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAH-RLNTIMDSDKVLVMDKGRMAEYDHP 1352
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAlqRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
826-1069 |
4.99e-08 |
|
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: 56.33 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 826 NATNETSTENLDISSMYNYMYIYTAIVVGLFCIGITRSLTFYEVCIVCSQKLHDMAFSALIRTGMRFFDTNPSGRILNRF 905
Cdd:cd18577 31 DFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 906 SKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLgtVFYWIRKVYLKTSKNIKRLEGMSRSp 979
Cdd:cd18577 111 TSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWkltlvlLATLPLIAI--VGGIMGKLLSKYTKKEQEAYAKAGS- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 980 vftHLNATLNGLTTIRAYCAQDILKKEFDK-LQDVHTSTVYMYVVSSSGFGFsldIFCFVFTSLV-TF---SFLLLEQSF 1054
Cdd:cd18577 188 ---IAEEALSSIRTVKAFGGEEKEIKRYSKaLEKARKAGIKKGLVSGLGLGL---LFFIIFAMYAlAFwygSRLVRDGEI 261
|
250
....*....|....*
gi 383847295 1055 SGGEVglaITQVMAM 1069
Cdd:cd18577 262 SPGDV---LTVFFAV 273
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
502-669 |
5.20e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS-LSYAGQE-AWVFGS-------TVRQNILFG-Q 571
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpVEGPGAErGVVFQNegllpwrNVQDNVAFGlQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 572 PYDRHRYQKVVKACSLLRdfkqfpqsdqtVVGERGS------SLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSK 645
Cdd:PRK11248 97 LAGVEKMQRLEIAHQMLK-----------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|....*
gi 383847295 646 HLFEECIQRYL-AGKTRILATHQLQ 669
Cdd:PRK11248 166 QMQTLLLKLWQeTGKQVLLITHDIE 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1135-1362 |
5.29e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSslISAL--FRLAKVEGVI----EI-----DDIDTGSIC 1203
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALsiLRLLPSPPVVypsgDIrfhgeSLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1204 LEDLR-RHISIIPQDPVLfsgtlrrNLDPFNEFsDAALWEVL-------------EEVELKDAVVIsgNGLESRVLDRGS 1269
Cdd:PRK15134 86 LRGVRgNKIAMIFQEPMV-------SLNPLHTL-EKQLYEVLslhrgmrreaargEILNCLDRVGI--RQAAKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1270 NYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRM 1346
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRC 235
|
250
....*....|....*....
gi 383847295 1347 AEYDHPHMLL---QNTYSQ 1362
Cdd:PRK15134 236 VEQNRAATLFsapTHPYTQ 254
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
835-1012 |
5.78e-08 |
|
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: 55.94 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 835 NLDISSMYNYMYIYTAIVVGLFCIGITRSLTFYEVcivcSQK-LHDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMG 910
Cdd:cd18545 33 NGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKV----GQRiLYDLrqdLFSHLQKLSFSFFDSRPVGKILSRVINDVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 911 TIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGtVFYW---IRKVYLKTSKNIkrlegmsrSPVF 981
Cdd:cd18545 109 SLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVrlalvtLAVLPLLVLV-VFLLrrrARKAWQRVRKKI--------SNLN 179
|
170 180 190
....*....|....*....|....*....|.
gi 383847295 982 THLNATLNGLTTIRAYCAQDILKKEFDKLQD 1012
Cdd:cd18545 180 AYLHESISGIRVIQSFAREDENEEIFDELNR 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
502-684 |
6.99e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGslsyagqEAWVFGS-------------------- 561
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-------KPVRIRSprdaialgigmvhqhfmlvp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 --TVRQNILFGQP------YDRHRYQKVVKACSllrdfKQF-----PqsDQTVvgergSSLSGGQKARINLARSLYRQAD 628
Cdd:COG3845 94 nlTVAENIVLGLEptkggrLDRKAARARIRELS-----ERYgldvdP--DAKV-----EDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 629 VYLLDDPlSAVDT-HVSKHLFEecIQRYLA--GKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:COG3845 162 ILILDEP-TAVLTpQEADELFE--ILRRLAaeGKSIIFITHKLREVMAIaDRVTVLRRGK 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1143-1346 |
7.34e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1143 RYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAL----FRLAKVEGVIEIDDIDtGSICLEDLRRHISIIPQD- 1217
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSVEGDIHYNGIP-YKEFAEKYPGEIIYVSEEd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1218 ---PVLfsgTLRRNLDpfneFSdaalwevleeVELK-DAVVisgnglesrvldRGsnYSVGQRQLVCLARAILRNNKILM 1293
Cdd:cd03233 93 vhfPTL---TVRETLD----FA----------LRCKgNEFV------------RG--ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 1294 LDEATANVDPQTDALIQNTIRrkftkctvlTIAHRLN-TIMDS------------DKVLVMDKGRM 1346
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIR---------TMADVLKtTTFVSlyqasdeiydlfDKVLVLYEGRQ 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
484-684 |
7.40e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.48 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKWEPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSlSYAGQEAW------ 557
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 558 --VF--------GSTVRQNILFG---QPYDRHRYQKVVKACSLLRDFKQFPQSDQtvvgergSSLSGGQKARINLARSLY 624
Cdd:PRK13642 84 gmVFqnpdnqfvGATVEDDVAFGmenQGIPREEMIKRVDEALLAVNMLDFKTREP-------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 625 RQADVYLLDDPLSAVD----THVSKHLFEECIQRYLagkTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL---TVLSITHDLDEAASSDRILVMKAGE 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
503-667 |
7.51e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 503 DNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSL------SYAGQEAWVfGS--------TVRQNIL 568
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdEYHQDLLYL-GHqpgiktelTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 569 FgqpydrhryqkvvkACSLLRdfkqfPQSDQTV------VGERG------SSLSGGQKARINLARSLYRQADVYLLDDPL 636
Cdd:PRK13538 97 F--------------YQRLHG-----PGDDEALwealaqVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|....
gi 383847295 637 SAVDTH---VSKHLFEECIQRylaGKTRILATHQ 667
Cdd:PRK13538 158 TAIDKQgvaRLEALLAQHAEQ---GGMVILTTHQ 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1132-1328 |
8.47e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.68 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1132 DGMIRFRNVYMRYAEEELpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDidtgsicledlRRH 1210
Cdd:TIGR00954 449 DNGIKFENIPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVyGGRLTKPA-----------KGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLFSGTLRRNL------DPFNE--FSDAALWEVLEEVELKDaVVISGNGLESrVLDRGSNYSVGQRQLVCLA 1282
Cdd:TIGR00954 517 LFYVPQRPYMTLGTLRDQIiypdssEDMKRrgLSDKDLEQILDNVQLTH-ILEREGGWSA-VQDWMDVLSGGEKQRIAMA 594
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 383847295 1283 RAILRNNKILMLDEATANVDPQTDALIQNTIRRKftKCTVLTIAHR 1328
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1134-1342 |
8.70e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEIDDidtgsicleDLRrhIS 1212
Cdd:PRK09544 4 LVSLENVSVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNG---------KLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQ----DPVLfSGTLRRNLDPFNEFSDAALWEVLEEVElkdavviSGNGLESRVldrgSNYSVGQRQLVCLARAILRN 1288
Cdd:PRK09544 71 YVPQklylDTTL-PLTVNRFLRLRPGTKKEDILPALKRVQ-------AGHLIDAPM----QKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1289 NKILMLDEATANVDPQTDA----LIqNTIRRKFtKCTVLTIAHRLNTIM-DSDKVLVMD 1342
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQValydLI-DQLRREL-DCAVLMVSHDLHLVMaKTDEVLCLN 195
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
882-1093 |
8.71e-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: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 882 FSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGTVF 955
Cdd:cd18563 83 YEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWklallvLIPVPLVVWGSYF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 956 YW--IRKVYLKTSKnikrlegmSRSPVFTHLNATLNGLTTIRAYcAQDilKKEFDKLQDV--HTSTVYMYVVSSSGFGFS 1031
Cdd:cd18563 163 FWkkIRRLFHRQWR--------RWSRLNSVLNDTLPGIRVVKAF-GQE--KREIKRFDEAnqELLDANIRAEKLWATFFP 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 1032 LDIFCFVFTSLVTFSF---LLLEQSFSGGEvglaITQVMAMTGM----IQWGMRQNAEAANQMMAVERV 1093
Cdd:cd18563 232 LLTFLTSLGTLIVWYFggrQVLSGTMTLGT----LVAFLSYLGMfygpLQWLSRLNNWITRALTSAERI 296
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1134-1345 |
8.94e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 8.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGvieiddidtGSICLEDlrRHISI 1213
Cdd:PRK11300 5 LLSVSGLMMRFGG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG---------GTILLRG--QHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVLFSGTLR--RNLDPFNEFS------------------------------------DAALWevLEEVELKDavvi 1255
Cdd:PRK11300 72 LPGHQIARMGVVRtfQHVRLFREMTvienllvaqhqqlktglfsgllktpafrraesealdRAATW--LERVGLLE---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1256 sgngLESRvldRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQT----DALIQNtIRRKFtKCTVLTIAHRLNT 1331
Cdd:PRK11300 146 ----HANR---QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKEtkelDELIAE-LRNEH-NVTVLLIEHDMKL 216
|
250
....*....|....*
gi 383847295 1332 IMD-SDKVLVMDKGR 1345
Cdd:PRK11300 217 VMGiSDRIYVVNQGT 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1145-1314 |
9.85e-08 |
|
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: 54.04 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1145 AEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLA-KVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSG 1223
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1224 TLRRNLDPFNEF-SDAALWEVLEEVELkdavvisgNGLEsrvlDRGSNY-SVGQRQLVCLARAILRNNKILMLDEATANV 1301
Cdd:cd03231 89 SVLENLRFWHADhSDEQVEEALARVGL--------NGFE----DRPVAQlSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|...
gi 383847295 1302 DPQTDALIQNTIR 1314
Cdd:cd03231 157 DKAGVARFAEAMA 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1159-1353 |
1.14e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.34 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1159 INPGEKIGIVGRTGAGKSSLISALfrlakvEGVIEIDDIDTGSicledLRRHISIIPQD-PVLFSGTLRRNL-DPFNEFS 1236
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKML------AGVLKPDEGDIEI-----ELDTVSYKPQYiKADYEGTVRDLLsSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1237 DAALW--EVLEEVELKDAvvisgngLESRVLDrgsnYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIR 1314
Cdd:cd03237 91 THPYFktEIAKPLQIEQI-------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 383847295 1315 R--KFTKCTVLTIAHRLNTI-MDSDKVLVMDkGRMAEYDHPH 1353
Cdd:cd03237 160 RfaENNEKTAFVVEHDIIMIdYLADRLIVFE-GEPSVNGVAN 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
502-684 |
1.15e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.50 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS--LSYAGQE---AWVFGS-------TVRQNI-- 567
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvTHRSIQQrdiCMVFQSyalfphmSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 ---LFGQPYDRhRYQKVVKACSLLrDFKQFpqSDQTVvgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVS 644
Cdd:PRK11432 102 glkMLGVPKEE-RKQRVKEALELV-DLAGF--EDRYV-----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 645 KHLFE---ECIQRYlaGKTRILATH-QLQYVKNVDAIILIEQGK 684
Cdd:PRK11432 173 RSMREkirELQQQF--NITSLYVTHdQSEAFAVSDTVIVMNKGK 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-547 |
1.21e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 54.71 E-value: 1.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 383847295 499 ENT-LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG 547
Cdd:COG1101 18 EKRaLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG 67
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1152-1357 |
1.28e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISAL-FRLAK---VEGVIEIDDIDTGSiclEDLRRHISIIPQDPVL------- 1220
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKgvkGSGSVLLNGMPIDA---KEMRAISAYVQQDDLFiptltvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1221 ----FSGTLRRNLDPFNEFSDAALWEVLEEVELKDAV-VISGNGLESRVLdrgsnySVGQRQLVCLARAILRNNKILMLD 1295
Cdd:TIGR00955 118 ehlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCAnTRIGVPGRVKGL------SGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1296 EATANVDPQTDALIQNTIRRKFTKCT--VLTIAHRLNTIMDS-DKVLVMDKGRMAEYDHPHMLLQ 1357
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKtiICTIHQPSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
502-684 |
1.29e-07 |
|
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: 55.99 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGeidvVEGHVKVNGSLSYAGQE---------------------AWVFG 560
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG----VYPHGTWDGEIYWSGSPlkasnirdteragiviihqelTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 561 STVRQNILFGQ----PYDRHRYQKVVKAC-SLLRDFKQFPQSDQTVVGERGsslsGGQKARINLARSLYRQADVYLLDDP 635
Cdd:TIGR02633 93 LSVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 636 ---LSAVDTHVSKHLFEECIQRYLAGktrILATHQLQYVKNV-DAIILIEQGK 684
Cdd:TIGR02633 169 sssLTEKETEILLDIIRDLKAHGVAC---VYISHKLNEVKAVcDTICVIRDGQ 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
498-698 |
1.57e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.08 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 498 SENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAI-----LGEIDVVEGHVKVNGSLSYAG---------QEAWVFGS-- 561
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPdvdpievrrEVGMVFQYpn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 562 -----TVRQNILFGQPYDR---------HRYQKVVKACSLLRDFKQfpqsdqtVVGERGSSLSGGQKARINLARSLYRQA 627
Cdd:PRK14267 96 pfphlTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEVKD-------RLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 628 DVYLLDDPLSAVDThVSKHLFEECIQRYLAGKTRILATH---QLQYVKNVDAII----LIEQGKA-TVFSHYQDLLSQR 698
Cdd:PRK14267 169 KILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLylgkLIEVGPTrKVFENPEHELTEK 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1162-1346 |
1.67e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1162 GEKIGIVGRTGAGKSSLISALFRL--AKVEGVIEIDD-----------IDTGsICL--EDLRRHiSIIPQDPVLFSGTLR 1226
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAypGRWEGEIFIDGkpvkirnpqqaIAQG-IAMvpEDRKRD-GIVPVMGVGKNITLA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1227 rNLDPFNEFS--DAALWEVLEEVELKDAVVISGNgLESRVldrgSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQ 1304
Cdd:PRK13549 366 -ALDRFTGGSriDDAAELKTILESIQRLKVKTAS-PELAI----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 383847295 1305 TDALIQNTIrRKFTK--CTVLTIAHRLNTIMD-SDKVLVMDKGRM 1346
Cdd:PRK13549 440 AKYEIYKLI-NQLVQqgVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
502-640 |
1.82e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILG--------------EIDVVEGHVKVNGSLSYAGQEAWVFGS-TVRQN 566
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivprdagniiiddeDISLLPLHARARRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 567 IL--FGQPYDRHRYQKVVKACSLLRDFKQFPQSDQTvvgerGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:PRK10895 99 LMavLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1148-1345 |
1.89e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1148 ELPVLKGLNLVINPGEKIGIVGRTGAGKSSlisalfrLAKV----------EGVIEIDDIdtgSIC-LE-DLRRHISIIP 1215
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKST-------LSKViaghpaykilEGDILFKGE---SILdLEpEERAHLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1216 --QDPVLFSGT-----LR------RNLDPFNEFSDAALWEVLEEvelKDAVVisgnGLESRVLDRGSN--YSVGQRQLVC 1280
Cdd:CHL00131 89 afQYPIEIPGVsnadfLRlaynskRKFQGLPELDPLEFLEIINE---KLKLV----GMDPSFLSRNVNegFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1281 LARAILRNNKILMLDEATANVDpqTDAL--IQNTIRRKFTKCT-VLTIAH--RLNTIMDSDKVLVMDKGR 1345
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLD--IDALkiIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGK 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1150-1369 |
1.99e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEI--DDIDTGsicLEDLRRHISIIPQDPVLFSG-TL 1225
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTgLLPPTSGTVLVggKDIETN---LDAVRQSLGMCPQHNILFHHlTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1226 RRNLDPFNEFSDAAlWEvleEVELKDAVVISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQT 1305
Cdd:TIGR01257 1021 AEHILFYAQLKGRS-WE---EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1306 DALIQNTIRRKFTKCTVLTIAHRLNTI-MDSDKVLVMDKGRMAEYDHPhMLLQNTYSQ--FTSLVKE 1369
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP-LFLKNCFGTgfYLTLVRK 1162
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
484-684 |
2.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAKW---EPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAW--- 557
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 558 -----VF--------GSTVRQNILFG------QPYD-RHRYQKVVKACSLLrDFKQFPQSdqtvvgergsSLSGGQKARI 617
Cdd:PRK13633 85 nkagmVFqnpdnqivATIVEEDVAFGpenlgiPPEEiRERVDESLKKVGMY-EYRRHAPH----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 618 NLARSLYRQADVYLLDDPLSAVDTHVSKHL---FEECIQRYlaGKTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVvntIKELNKKY--GITIILITHYMEEAVEADRIIVMDSGK 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1150-1347 |
2.80e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.02 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDD--IDTGS--------ICL--EDlRRHISIIPQ 1216
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAdSGEIRLDGkpVRIRSprdairagIAYvpED-RKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1217 DPVLFSGTLRrNLDPFNEF---SDAALWEVLEEveLKDAVVISGNGLESRVldrgSNYSVGQRQLVCLARAILRNNKILM 1293
Cdd:COG1129 345 LSIRENITLA-SLDRLSRGgllDRRRERALAEE--YIKRLRIKTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1294 LDEATANVDPQTDALIQNTIRRkFTK--CTVLTIAHRLNTIMD-SDKVLVMDKGRMA 1347
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIV 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
481-684 |
3.13e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 481 PYAVKMTNFTAKWePGQseNTLDNLNLEIEKGKIYAVIGMVGAGKSSF---LSAIL------GEIdVVEGHVKVNGSLS- 550
Cdd:PRK13549 3 EYLLEMKNITKTF-GGV--KALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYphgtyeGEI-IFEGEELQASNIRd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 551 --YAG-----QE-AWVFGSTVRQNILFGQ---PYDRHRYQKVVKACS-LLRDFKQFPQSDQTVvgergSSLSGGQKARIN 618
Cdd:PRK13549 79 teRAGiaiihQElALVKELSVLENIFLGNeitPGGIMDYDAMYLRAQkLLAQLKLDINPATPV-----GNLGLGQQQLVE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 619 LARSLYRQADVYLLDDP---LSAVDTHVSKHLFEECIQRylaGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:PRK13549 154 IAKALNKQARLLILDEPtasLTESETAVLLDIIRDLKAH---GIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1132-1356 |
3.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1132 DGMIRFRNVYMRYaEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEIDDIDTGSICLEDLRRH 1210
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQrGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDP--VLFSGTLRRNL--DPFNEFSDAAlwEVLEEVELKDAVVisgnGLESRVLDRGSNYSVGQRQLVCLARAIL 1286
Cdd:PRK13647 81 VGLVFQDPddQVFSSTVWDDVafGPVNMGLDKD--EVERRVEEALKAV----RMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1287 RNNKILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIA-HRLNTIMD-SDKVLVMDKGRMAEYDHPHMLL 1356
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1144-1344 |
3.20e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1144 YAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRlAKVEGVIEIDDIDTGSICL-EDLRRHISIIPQDPV--- 1219
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE-RVTTGVITGGDRLVNGRPLdSSFQRSIGYVQQQDLhlp 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1220 --------LFSGTLRR----NLDPFNEFSDAALwEVLEEVELKDAVV-ISGNGLesrvldrgsnySVGQRQLVCLARAIL 1286
Cdd:TIGR00956 850 tstvreslRFSAYLRQpksvSKSEKMEYVEEVI-KLLEMESYADAVVgVPGEGL-----------NVEQRKRLTIGVELV 917
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1287 RNNK-ILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMDS-DKVLVMDKG 1344
Cdd:TIGR00956 918 AKPKlLLFLDEPTSGLDSQTAWSICKLMRKlaDHGQAILCTIHQPSAILFEEfDRLLLLQKG 979
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
499-703 |
3.38e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.56 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 499 ENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHvKVNGSLSYAGQEAWVFGSTV----RQNILFGQP-- 572
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGGRSIFNYRDVLefrrRVGMLFQRPnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 573 YDRHRYQKV---VKACSLL--RDFKQFPQSDQTVVG------ERGSS----LSGGQKARINLARSLYRQADVYLLDDPLS 637
Cdd:PRK14271 113 FPMSIMDNVlagVRAHKLVprKEFRGVAQARLTEVGlwdavkDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 638 AVDTHVSKHLfEECIQRYLAGKTRILATHQL-QYVKNVDAIILIEQGKATVFSHYQDLLSQrPEYAE 703
Cdd:PRK14271 193 ALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS-PKHAE 257
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1161-1344 |
3.47e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1161 PGEKIG-IVGRTGAGKSSLISALF---RLAKveGVIEIDDIDTGSICLEDLrrhISIIPQD-------PVLFS------- 1222
Cdd:PRK15056 31 PGGSIAaLVGVNGSGKSTLFKALMgfvRLAS--GKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVEdvvmmgr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1223 ----GTLRRNLDPFNEFSDAALWEVleevelkdavvisgNGLESRVLDRGSnYSVGQRQLVCLARAILRNNKILMLDEAT 1298
Cdd:PRK15056 106 yghmGWLRRAKKRDRQIVTAALARV--------------DMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 383847295 1299 ANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMDSDKVLVMDKG 1344
Cdd:PRK15056 171 TGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1349 |
3.82e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.27 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAK-VEGVIEIDDIDTGSICLEDLRRHISIIPQDP--VLFSGTLRR 1227
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1228 NL--DPFNEFSDAalwevlEEVELKDAVVISGNGLESrVLDRGSNY-SVGQRQLVCLARAILRNNKILMLDEATANVDPQ 1304
Cdd:PRK13652 99 DIafGPINLGLDE------ETVAHRVSSALHMLGLEE-LRDRVPHHlSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 383847295 1305 TDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEY 1349
Cdd:PRK13652 172 GVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAY 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1151-1364 |
3.85e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLA-------KVEGVIEIDDIDTGSICLEDLRRHISIIPQDPvlfsg 1223
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQP----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1224 tlrrnlDPFNEFS--DAALWE-----VLEEVELKDAV--VISGNGLESRVLDR----GSNYSVGQRQLVCLARAILRNNK 1290
Cdd:PRK14246 100 ------NPFPHLSiyDNIAYPlkshgIKEKREIKKIVeeCLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1291 ILMLDEATANVDPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQNTYSQFT 1364
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1150-1327 |
4.22e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKvegvieidDIDTGSICLEDLRrhISIIPQDPVL-FSGTLRRN 1228
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--------DFNGEARPQPGIK--VGYLPQEPQLdPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1229 -----------LDPFNEFS------DAALWEVLEEVELKDAVVISGNG--LESRvLDRG-------------SNYSVGQR 1276
Cdd:TIGR03719 89 veegvaeikdaLDRFNEISakyaepDADFDKLAAEQAELQEIIDAADAwdLDSQ-LEIAmdalrcppwdadvTKLSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1277 QLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRkfTKCTVLTIAH 1327
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTH 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1142-1313 |
6.00e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1142 MRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIeidDIDTGSICLEDLRRHISIIPQDPvl 1220
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQI---QIDGKTATRGDRSRFMAYLGHLP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1221 fsgTLRRNLDPF-NEFSDAALWEVLEEVELKDAVVISGNGLESRVLDRgsNYSVGQRQLVCLARAILRNNKILMLDEATA 1299
Cdd:PRK13543 92 ---GLKADLSTLeNLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR--QLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170
....*....|....
gi 383847295 1300 NVDPQTDALIQNTI 1313
Cdd:PRK13543 167 NLDLEGITLVNRMI 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1150-1315 |
6.65e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.95 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDDIDtgsicLEDL------RRHISIIPQDPVLFS 1222
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGED-----ITHLpmhkraRLGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1223 G-TLRRNLDPFNEFSD-------AALWEVLEE---VELKD--AVVISGnglesrvldrgsnysvGQRQLVCLARAILRNN 1289
Cdd:COG1137 92 KlTVEDNILAVLELRKlskkereERLEELLEEfgiTHLRKskAYSLSG----------------GERRRVEIARALATNP 155
|
170 180
....*....|....*....|....*.
gi 383847295 1290 KILMLDEATANVDPQTDALIQNTIRR 1315
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRH 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
499-711 |
6.66e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 499 ENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSL--SYAGQ--EAWVFGSTVRQNILFGQP-- 572
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLevAYFDQhrAELDPEKTVMDNLAEGKQev 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 573 ----YDRHryqkvvkACSLLRDFKQFPQSDQTVVgergSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHvSKHLF 648
Cdd:PRK11147 412 mvngRPRH-------VLGYLQDFLFHPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE-TLELL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 649 EECIQRYLAgkTRILATHQLQYVKNVDAIILIEQGKATVFSH---YQDLLSQRPEYAELLAAENET 711
Cdd:PRK11147 480 EELLDSYQG--TVLLVSHDRQFVDNTVTECWIFEGNGKIGRYvggYHDARQQQAQYLALKQPAVKK 543
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
839-1039 |
7.21e-07 |
|
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: 52.84 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 839 SSMYNYMYIYTAIVVGLFCIGITRSLTfyevciVCSQKLHD----MAFSALIRTGMRFFD--TNPSGRILNRFSKDMGTI 912
Cdd:cd18578 51 ANFWALMFLVLAIVAGIAYFLQGYLFG------IAGERLTRrlrkLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 913 DELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGTVFYwIRKVYLKTSKNIKRLEGMSRspvftHLNA 986
Cdd:cd18578 125 RGLVGDRLGLILQAIVTLVAGLIIAFVYGWklalvgLATVPLLLLAGYLR-MRLLSGFEEKNKKAYEESSK-----IASE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 987 TLNGLTTIRAYCAQDILKKEFDK-LQDVHTSTVYMYVVSSSGFGFSLDIFCFVF 1039
Cdd:cd18578 199 AVSNIRTVASLTLEDYFLEKYEEaLEEPLKKGLRRALISGLGFGLSQSLTFFAY 252
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
497-696 |
7.29e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 497 QSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEI--DVVEGHVKVNGS---------LSYAGQEAWVFGS-TVR 564
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRkptkqilkrTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QNILFGQ----PYDRHRYQKVVKACSLLRDFKqFPQSDQTVVGE---RGssLSGGQKARINLARSLYRQADVYLLDDPLS 637
Cdd:PLN03211 159 ETLVFCSllrlPKSLTKQEKILVAESVISELG-LTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 638 AVDTHVSKHLFEECIQRYLAGKTRILATHQ--LQYVKNVDAIILIEQGKATVFSHYQDLLS 696
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1135-1348 |
7.31e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.94 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEEElpVLKGLNLVINPGEKIGIVGRTGAGKSSLISALfRLAKV--EGVIEIDD--------IDTGSICL 1204
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMprSGTLNIAGnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1205 edLRRHISIIPQD----PVLfsgTLRRNL--DPF-------NEFSDAALwEVLEEVELKDAVvisgnglesrvlDRGS-N 1270
Cdd:PRK11124 80 --LRRNVGMVFQQynlwPHL---TVQQNLieAPCrvlglskDQALARAE-KLLERLRLKPYA------------DRFPlH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1271 YSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAE 1348
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1135-1352 |
8.63e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.72 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1135 IRFRNVYMRYAEeeLPVLKGLNLVINPGEKIGIVGRTGAGKSSLisaLFRLAKVEgvieidDIDTGSICLEDLR------ 1208
Cdd:PRK11000 4 VTLRNVTKAYGD--VVISKDINLDIHEGEFVVFVGPSGCGKSTL---LRMIAGLE------DITSGDLFIGEKRmndvpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1209 --RHISIIPQDPVLFSG-TLRRNLDPFNEFSDAALWEVLEEVELKDAVVISGNGLESRVLDrgsnYSVGQRQLVCLARAI 1285
Cdd:PRK11000 73 aeRGVGMVFQSYALYPHlSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1286 LRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHP 1352
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRlhKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKP 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
478-683 |
8.80e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 478 NEEPYaVKMTNFTAKWEPGQSentLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG---------- 547
Cdd:PRK09700 1 MATPY-ISMAGIGKSFGPVHA---LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhkl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 548 ----SLSYAGQEAWVFGS-TVRQNILFGqpydRHRYQKVvkaCSL-LRDFKQFPQSDQTV---VG------ERGSSLSGG 612
Cdd:PRK09700 77 aaqlGIGIIYQELSVIDElTVLENLYIG----RHLTKKV---CGVnIIDWREMRVRAAMMllrVGlkvdldEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 613 QKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQG 683
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1151-1352 |
1.21e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.39 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEIDDIDTGSICLED-----------LRRHISIIpqDP 1218
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQTSGHIRFHGTDVSRLHARDrkvgfvfqhyaLFRHMTVF--DN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1219 VLFSGT-LRRNLDPFNEFSDAALWEVLEEVELkdavvisgngleSRVLDR-GSNYSVGQRQLVCLARAILRNNKILMLDE 1296
Cdd:PRK10851 95 IAFGLTvLPRRERPNAAAIKAKVTQLLEMVQL------------AHLADRyPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1297 ATANVDPQTDALIQNTIRR-----KFTKCTVltiAHRLNTIMD-SDKVLVMDKGRMAEYDHP 1352
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQlheelKFTSVFV---THDQEEAMEvADRVVVMSQGNIEQAGTP 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
502-699 |
1.34e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSfLSAILGEIDVVEGhvkvnGSLSYAGQEAWVFGSTVRQN------ILFGQPY-- 573
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKST-LARLLTMIETPTG-----GELYYQGQDLLKADPEAQKLlrqkiqIVFQNPYgs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 574 -------------------DRHRYQKVVKACSLLRdfkqfpqsdqtVVGERGSS-------LSGGQKARINLARSLYRQA 627
Cdd:PRK11308 105 lnprkkvgqileepllintSLSAAERREKALAMMA-----------KVGLRPEHydryphmFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 628 DVYLLDDPLSAVDTHVSK---HLFEECIQRYlaGKTRILATHQLQYVKNV--DAIIL-----IEQG-KATVFSH----Y- 691
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAqvlNLMMDLQQEL--GLSYVFISHDLSVVEHIadEVMVMylgrcVEKGtKEQIFNNprhpYt 251
|
....*...
gi 383847295 692 QDLLSQRP 699
Cdd:PRK11308 252 QALLSATP 259
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
502-651 |
1.50e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.84 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVkvngslsyagqeawvfGSTVRQNILF--GQPYdrhryq 579
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------GMPEGEDLLFlpQRPY------ 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 580 kvVKACSLlRDFKQFPQSDQtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLFEEC 651
Cdd:cd03223 75 --LPLGTL-REQLIYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1161-1348 |
1.65e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1161 PGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEIDDIDTGSICLEDL----RRHIS-----IIPQDPvlfSGTLRRNLD 1230
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSaRLAPDAGEVHYRMRDGQLRDLYALseaeRRRLLrtewgFVHQHP---RDGLRMQVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1231 P---------------FNEFSDAAL-WevLEEVELkDAvvisgngleSRVLDRGSNYSVGQRQLVCLARAILRNNKILML 1294
Cdd:PRK11701 108 AggnigerlmavgarhYGDIRATAGdW--LERVEI-DA---------ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1295 DEATANVDPQTDALIQNTIRRKFTK--CTVLTIAHRLNTI-MDSDKVLVMDKGRMAE 1348
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRElgLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1138-1350 |
1.74e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1138 RNVYMRyAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVE-GVIEID--DIDTGSIclEDLRRH-ISI 1213
Cdd:COG3845 261 ENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAsGSIRLDgeDITGLSP--RERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDP-----VLfSGTLRRNL------DPfnEFSDAAL--WEVLEE--VELKDAVVISGNGLESRVldrgSNYSVGQRQL 1278
Cdd:COG3845 338 IPEDRlgrglVP-DMSVAENLilgryrRP--PFSRGGFldRKAIRAfaEELIEEFDVRTPGPDTPA----RSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1279 VCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRKFTK-CTVLTIAHRLNTIMD-SDKVLVMDKGR-MAEYD 1350
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILAlSDRIAVMYEGRiVGEVP 485
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1155-1346 |
1.81e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1155 LNLVINPGEKIGIVGRTGAGKSSLISALFRLAKVEGVIEIDDIDTGSICLEDLRRHISIIPQD-------PVLFSGTLRR 1227
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppfamPVFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1228 NLDPFNEFSDAALWEVLEEVELKDAvvisgngLESRVldrgSNYSVGQRQLVCLARAILR-------NNKILMLDEATAN 1300
Cdd:PRK03695 95 PDKTRTEAVASALNEVAEALGLDDK-------LGRSV----NQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1301 VD-PQTDALIQntIRRKFtkC----TVLTIAHRLN-TIMDSDKVLVMDKGRM 1346
Cdd:PRK03695 164 LDvAQQAALDR--LLSEL--CqqgiAVVMSSHDLNhTLRHADRVWLLKQGKL 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1132-1357 |
1.82e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1132 DGMIRFRNVYMRYAEEELpvLKGLNLVINPGEKIGIVGRTGAGKSSLISALFR-LAKVEGVIEIDDIDTGSICLEDLRRH 1210
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRhQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLFSGTLRRNLDPFNEFS-DAALW----EVLEEVElkDAVVISG-NGLESRVLDrgsNYSVGQRQLVCLARA 1284
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVAIGRYPwHGALGrfgaADREKVE--EAISLVGlKPLAHRLVD---SLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1285 ILRNNKILMLDEATANVD--PQTD--ALIQNTIRRKftKCTVLTIAHRLNtiMDS---DKVLVMDKGRMAEYDHPHMLLQ 1357
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDiaHQVDvlALVHRLSQER--GLTVIAVLHDIN--MAArycDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1154-1342 |
1.95e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1154 GLNLVINPGEKIGIVGRTGAGKSSLISALFRLAkvegvieidDIDTGSICL--EDLRR-------------HISIIpqDP 1218
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLA---------RPDAGEVLWqgEPIRRqrdeyhqdllylgHQPGI--KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1219 VLfsgTLRRNLDPF----NEFSDAALWEVLEEVELK---DAVVisgnglesRVLdrgsnySVGQRQLVCLARAILRNNKI 1291
Cdd:PRK13538 88 EL---TALENLRFYqrlhGPGDDEALWEALAQVGLAgfeDVPV--------RQL------SAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1292 LMLDEA-TAnVDPQTDALIQNTIRRKFTK--CTVLTIAHRLNtiMDSDKVLVMD 1342
Cdd:PRK13538 151 WILDEPfTA-IDKQGVARLEALLAQHAEQggMVILTTHQDLP--VASDKVRKLR 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
502-689 |
2.08e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEID---VVEGHVKVNGSL----------SYAGQEAWVFGS-TVRQNI 567
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPidakemraisAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LF--------GQPYD--RHRYQKVVKACSLLRdfkqfpqSDQTVVGERGS--SLSGGQKARINLARSLYRQADVYLLDDP 635
Cdd:TIGR00955 121 MFqahlrmprRVTKKekRERVDEVLQALGLRK-------CANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 383847295 636 LSAVDTHVSKHLFEecIQRYLA--GKTRILATHQLQY--VKNVDAIILIEQGKaTVFS 689
Cdd:TIGR00955 194 TSGLDSFMAYSVVQ--VLKGLAqkGKTIICTIHQPSSelFELFDKIILMAEGR-VAYL 248
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
882-1014 |
3.56e-06 |
|
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: 50.57 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 882 FSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP-LFLI-----PIVFLGTVF 955
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPrLALValaalPPLALATRW 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 956 YWIR--KVYLKTSKNIkrlegmsrSPVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVH 1014
Cdd:cd18546 159 FRRRssRAYRRARERI--------AAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDY 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1134-1387 |
4.59e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEELpvLKGLNLVINPGEKIGIVGRTGAGKSSLISALfrlakvEGVIEiddIDTGSICLEDLRRHISI 1213
Cdd:PRK10636 1 MIVFSSLQIRRGVRVL--LDNATATINPGQKVGLVGKNGCGKSTLLALL------KNEIS---ADGGSYTFPGNWQLAWV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1214 IPQDPVL--------FSG-----TLRRNLDPFNEFSD----AALWEVLEEVEL-----KDAVVISGNGLESRVLDRG-SN 1270
Cdd:PRK10636 70 NQETPALpqpaleyvIDGdreyrQLEAQLHDANERNDghaiATIHGKLDAIDAwtirsRAASLLHGLGFSNEQLERPvSD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1271 YSVGQRQLVCLARAILRNNKILMLDEATANVDpqTDALIQNTIRRKFTKCTVLTIAHR---LNTIMdsDKVLVMDKGRMA 1347
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIWLEKWLKSYQGTLILISHDrdfLDPIV--DKIIHIEQQSLF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 383847295 1348 EYdhphmllQNTYSQF-----TSLVKEtdRAMFD-QLVRIAK-QSYI 1387
Cdd:PRK10636 226 EY-------TGNYSSFevqraTRLAQQ--QAMYEsQQERVAHlQSYI 263
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1134-1352 |
6.55e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYaEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRLAKV-EGVIEIDD--IDTgsicLEDLRRH 1210
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERItSGEIWIGGrvVNE----LEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1211 ISIIPQDPVLFSG-TLRRNLdpfnefsdaalwevleEVELKdavvISGNG---LESRV------------LDRGSN-YSV 1273
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENM----------------AYGLK----IRGMPkaeIEERVaeaarileleplLDRKPReLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1274 GQRQLVCLARAILRNNKILMLDEATANVDP----QTDALIQNTIRR-KFTKCTV-------LTIAHRLntimdsdkvLVM 1341
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRlKTTSLYVthdqveaMTLADRV---------VVM 208
|
250
....*....|....*....
gi 383847295 1342 DKGRmAE--------YDHP 1352
Cdd:PRK11650 209 NGGV-AEqigtpvevYEKP 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
502-635 |
8.25e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG----SLSYAG--------------QEAWVFGSTV 563
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGeditGLSPRErrrlgvayipedrlGRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RQNILFGQpYDRHRYQK---------VVKACSLLRDFKQFPQSDQTVVGergsSLSGG--QKArInLARSLYRQADVYLL 632
Cdd:COG3845 354 AENLILGR-YRRPPFSRggfldrkaiRAFAEELIEEFDVRTPGPDTPAR----SLSGGnqQKV-I-LARELSRDPKLLIA 426
|
...
gi 383847295 633 DDP 635
Cdd:COG3845 427 AQP 429
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
877-1093 |
9.68e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 49.10 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 877 LHDM---AFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIP 947
Cdd:cd18565 86 QHDLrtdTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWqlalvaLLPVP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 948 IVFLGTVFY--WIRKVYLKTSKNIKRLEgmsrspvfTHLNATLNGLTTIRAYCAQDilkKEFDKLQDV------------ 1013
Cdd:cd18565 166 LIIAGTYWFqrRIEPRYRAVREAVGDLN--------ARLENNLSGIAVIKAFTAED---FERERVADAseeyrdanwrai 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1014 HTSTVY---MYVVSSSGFGFSLdifcFVFTSLVTFSFLLLEQSFSggeVGLAITQVMaMTGMIQWGMRQNAEAANQ---- 1086
Cdd:cd18565 235 RLRAAFfpvIRLVAGAGFVATF----VVGGYWVLDGPPLFTGTLT---VGTLVTFLF-YTQRLLWPLTRLGDLIDQyqra 306
|
....*..
gi 383847295 1087 MMAVERV 1093
Cdd:cd18565 307 MASAKRV 313
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1152-1380 |
1.01e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.86 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISALfrlakvEGVIEIDDIdTGSicledlrrHISIIPQDpVLFSGTLRRNLDP 1231
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHL------SGLITGDKS-AGS--------HIELLGRT-VQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1232 --------FNEFSDAALWEVLEEV---------------------ELKDAV-VISGNGLESRVLDRGSNYSVGQRQLVCL 1281
Cdd:PRK09984 84 srantgyiFQQFNLVNRLSVLENVligalgstpfwrtcfswftreQKQRALqALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1282 ARAILRNNKILMLDEATANVDPQTDALIQNTIR--RKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGrmaeydhpHMLLQN 1358
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQG--------HVFYDG 235
|
250 260
....*....|....*....|..
gi 383847295 1359 TYSQFtslvketDRAMFDQLVR 1380
Cdd:PRK09984 236 SSQQF-------DNERFDHLYR 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1120-1180 |
1.24e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 1.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383847295 1120 ALPANAPKnwpkdgmIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLIS 1180
Cdd:PRK10938 253 ALPANEPR-------IVLNNGVVSYNDR--PILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1142-1345 |
1.40e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1142 MRYAEEELPVLKGL---NLVINPGEKIGIVGRTGAGKSSLIsalfrlaKV----------EGVIEIDdidtGSIC-LEDL 1207
Cdd:NF040905 4 MRGITKTFPGVKALddvNLSVREGEIHALCGENGAGKSTLM-------KVlsgvyphgsyEGEILFD----GEVCrFKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1208 R----RHISIIPQD----PVL------FSG--TLRRNLDPFNE-FSDAAlwEVLEEVELKDAvvisgngLESRVLDRGsn 1270
Cdd:NF040905 73 RdseaLGIVIIHQElaliPYLsiaeniFLGneRAKRGVIDWNEtNRRAR--ELLAKVGLDES-------PDTLVTDIG-- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1271 ysVGQRQLVCLARAILRNNKILMLDEATANV-DPQTDALIQNTIRRKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:NF040905 142 --VGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGR 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1146-1358 |
1.48e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1146 EEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-----AKVEGVIEIDDIdtgSICLEDLR-RHISIIPQDPv 1219
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagvRQTAGRVLLDGK---PVAPCALRgRKIATIMQNP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1220 lfsgtlRRNLDPFNEF---------------SDAALWEVLEEVELKDAvvisgngleSRVLDRGS-NYSVGQRQLVCLAR 1283
Cdd:PRK10418 89 ------RSAFNPLHTMhtharetclalgkpaDDATLTAALEAVGLENA---------ARVLKLYPfEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1284 AILRNNKILMLDEATANVDPQTDA----LIQNTIRRKftKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAEYDHPHMLLQN 1358
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQArildLLESIVQKR--ALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
882-1058 |
1.48e-05 |
|
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: 48.60 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 882 FSALIRTGMRFFDTNPSGRILNRFSkDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP-LFLI---PIVFLGTVFYW 957
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWkLFLItllIIPLYILIILL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 958 IRKVYLKtsKNIKRLEGMSRspVFTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCF 1037
Cdd:cd18570 161 FNKPFKK--KNREVMESNAE--LNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISL 236
|
170 180
....*....|....*....|...
gi 383847295 1038 VFTSLVTF--SFLLLEQSFSGGE 1058
Cdd:cd18570 237 IGSLLILWigSYLVIKGQLSLGQ 259
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
833-961 |
2.09e-05 |
|
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: 47.92 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 833 TENLDISSMYNYMYIYTAI-VVGLFCIGItRSLTFY--EVCIVCsqKLHDMAFSALIRTGMRFFDTNPSGRILNRFSKDM 909
Cdd:cd18572 27 VADGSREAFYRAVLLLLLLsVLSGLFSGL-RGGCFSyaGTRLVR--RLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDC 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 910 GTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGTVFY--WIRKV 961
Cdd:cd18572 104 QKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltllaFITVPVIALITKVYgrYYRKL 163
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
503-640 |
2.19e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 503 DNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGSLSYAGQEAWVFGSTVRQNILF--GQPY-DRHRYQ 579
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFqsGALFtDMNVFD 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 580 KVVKAcslLRDFKQFPQS--DQTV------VGERG------SSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:PRK11831 104 NVAYP---LREHTQLPAPllHSTVmmkleaVGLRGaaklmpSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1152-1344 |
2.34e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLISALfrlakvegvIEIDDIDTGSICLEDLRRH-----------ISIIPQDPVL 1220
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVL---------TGIYTRDAGSILYLGKEVTfngpkssqeagIGIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1221 FSG-TLRRNLDPFNEFSDA---ALWEVLEEvelkdavviSGNGLESRV-LDRGS-----NYSVGQRQLVCLARAILRNNK 1290
Cdd:PRK10762 91 IPQlTIAENIFLGREFVNRfgrIDWKKMYA---------EADKLLARLnLRFSSdklvgELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 1291 ILMLDEAT-ANVDPQTDALIqNTIRR-KFTKCTVLTIAHRLNTIMD-SDKVLVMDKG 1344
Cdd:PRK10762 162 VIIMDEPTdALTDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
502-648 |
2.43e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS----LSYAG----------QEAWVFGS-TVRQN 566
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarLTPAKahqlgiylvpQEPLLFPNlSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 567 ILFGQPYDRHRYQKVVK-----ACSLLRDFKqfpqsdqtvvgerGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDT 641
Cdd:PRK15439 107 ILFGLPKRQASMQKMKQllaalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
....*..
gi 383847295 642 HVSKHLF 648
Cdd:PRK15439 174 AETERLF 180
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1165-1210 |
2.47e-05 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 47.84 E-value: 2.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 383847295 1165 IGIVGRTGAGKSSLISALFRlakvEGVIEIDDID--TGSICLEDLRRH 1210
Cdd:COG3596 42 IALVGKTGAGKSSLINALFG----AEVAEVGVGRpcTREIQRYRLESD 85
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
502-707 |
2.48e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.53 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVvEGHVKVNG-SLSYAGQEAW---------VF----GS-----T 562
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGqDLDGLSRRALrplrrrmqvVFqdpfGSlsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQ------NILFGQPYDRHRYQKVVKAcslLRDfkqfpqsdqtvVGERGSSL-------SGGQKARINLARSLYRQADV 629
Cdd:COG4172 381 VGQiiaeglRVHGPGLSAAERRARVAEA---LEE-----------VGLDPAARhryphefSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 630 YLLDDPLSAVDTHVSK---HLFEECIQRYlaGKTRILATHQLQYVKNV-DAII------LIEQGKA-TVFSHYQDllsqr 698
Cdd:COG4172 447 LVLDEPTSALDVSVQAqilDLLRDLQREH--GLAYLFISHDLAVVRALaHRVMvmkdgkVVEQGPTeQVFDAPQH----- 519
|
250
....*....|
gi 383847295 699 pEYA-ELLAA 707
Cdd:COG4172 520 -PYTrALLAA 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
502-682 |
2.77e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKV--NGSLSYAGQEAWVFGSTVRQNILFGQPYDRHRYQ 579
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgNWQLAWVNQETPALPQPALEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 580 KV----------------------------VKACSLLRD--FKQfPQSDQTVvgergSSLSGGQKARINLARSLYRQADV 629
Cdd:PRK10636 97 QLhdanerndghaiatihgkldaidawtirSRAASLLHGlgFSN-EQLERPV-----SDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383847295 630 YLLDDPLSAVDTHVSKHLfEECIQRYLAgkTRILATHQLQYVKN-VDAIILIEQ 682
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWL-EKWLKSYQG--TLILISHDRDFLDPiVDKIIHIEQ 221
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
482-673 |
3.00e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 482 YAVKMTNFTAKW-----------------EPGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVK 544
Cdd:PRK13545 3 YKVKFEHVTKKYkmynkpfdklkdlffrsKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 545 VNGSLSYAGQEAWVFGS-TVRQNI-LFG--QPYDRHRYQKVVKACSLLRDFKQFpqSDQTVvgergSSLSGGQKARINLA 620
Cdd:PRK13545 83 IKGSAALIAISSGLNGQlTGIENIeLKGlmMGLTKEKIKEIIPEIIEFADIGKF--IYQPV-----KTYSSGMKSRLGFA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 621 RSLYRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKN 673
Cdd:PRK13545 156 ISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKS 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1134-1305 |
3.28e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1134 MIRFRNVYMRYAEEelPVLKGLNLVINPGEKIGIVGRTGAGKSSLISALfrlakvEGVIEIDDidtGSICLE-DLRrhIS 1212
Cdd:PRK11147 3 LISIHGAWLSFSDA--PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDD---GRIIYEqDLI--VA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1213 IIPQDP------VLFS------GTLRRNLDPFNEFSDAALWE----VLEEVELKDAVVISGNG--LESRV--------LD 1266
Cdd:PRK11147 70 RLQQDPprnvegTVYDfvaegiEEQAEYLKRYHDISHLVETDpsekNLNELAKLQEQLDHHNLwqLENRInevlaqlgLD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 383847295 1267 ---RGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQT 1305
Cdd:PRK11147 150 pdaALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1101-1342 |
3.51e-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: 48.24 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1101 PEPNLRDRgkfakksEKQIALPANAPK-NWPKDGMIRFRNVYMRYAEEELPVLKGlnlVINPGEKIGIVGRTGAGKSSLI 1179
Cdd:COG1245 314 PEENVRIR-------DEPIEFEVHAPRrEKEEETLVEYPDLTKSYGGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1180 SALfrlakvEGVIEiddIDTGSIcLEDLRrhISIIPQ----DpvlFSGTLRRNLDPFN--EFSDAALW-EVLEEVELKDA 1252
Cdd:COG1245 384 KIL------AGVLK---PDEGEV-DEDLK--ISYKPQyispD---YDGTVEEFLRSANtdDFGSSYYKtEIIKPLGLEKL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1253 vvisgngLESRVldrgSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRR--KFTKCTVLTIAHRLN 1330
Cdd:COG1245 449 -------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaENRGKTAMVVDHDIY 517
|
250
....*....|...
gi 383847295 1331 TI-MDSDKVLVMD 1342
Cdd:COG1245 518 LIdYISDRLMVFE 530
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
484-684 |
4.31e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.10 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 484 VKMTNFTAkwePGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSS---FLSAILGEIDVVEGHVKVNGsLSYAGQEAW--- 557
Cdd:PRK13640 8 FKHVSFTY---PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 558 -----VF--------GSTVRQNILFG---QPYDRHRYQKVVKACSLLRDFKQFPQSDQtvvgergSSLSGGQKARINLAR 621
Cdd:PRK13640 84 ekvgiVFqnpdnqfvGATVGDDVAFGlenRAVPRPEMIKIVRDVLADVGMLDYIDSEP-------ANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383847295 622 SLYRQADVYLLDDPLSAVDTHVSKHLFEecIQRYLAGK---TRILATHQLQYVKNVDAIILIEQGK 684
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILK--LIRKLKKKnnlTVISITHDIDEANMADQVLVLDDGK 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1161-1345 |
4.41e-05 |
|
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: 45.06 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1161 PGEKIGIVGRTGAGKSSLISALFRLAKVE--GVIEIDDIDTGSICLEDLRRHIsiipqdpvlfsgtlrrnldpfnefsda 1238
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPggGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1239 alwevleevelkdavvisgnglesrVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQ-------N 1311
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 383847295 1312 TIRRKFTKCTVLTIAHRLNTIMD------SDKVLVMDKGR 1345
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-667 |
5.06e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 497 QSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS------------LSYAGQEAWVFGS-TV 563
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGHRSGINPYlTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RQNILfgqpYDRHRYQKVVKACSLLRDFK-----QFPqsdqtvvgerGSSLSGGQKARINLARSLYRQADVYLLDDPLSA 638
Cdd:PRK13540 92 RENCL----YDIHFSPGAVGITELCRLFSlehliDYP----------CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*....
gi 383847295 639 VDTHVSKHLFEECIQRYLAGKTRILATHQ 667
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1150-1327 |
6.80e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1150 PVLKGLNLVINPGEKIGIVGRTGAGKSSLisaLFRLAKVEgvieiDDIDTGSICLEDLRrhISIIPQDPVL-FSGTLRRN 1228
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTL---LRIMAGVD-----KEFEGEARPAPGIK--VGYLPQEPQLdPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1229 -----------LDPFNEFS------DAALWEVLEEV-ELKDAVViSGNG--LESRvLDRG-------------SNYSVGQ 1275
Cdd:PRK11819 91 veegvaevkaaLDRFNEIYaayaepDADFDALAAEQgELQEIID-AADAwdLDSQ-LEIAmdalrcppwdakvTKLSGGE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 383847295 1276 RQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTIRRkfTKCTVLTIAH 1327
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD--YPGTVVAVTH 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
607-706 |
8.29e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 607 SSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKH---LFEECIQRY-LAgktRILATHQLQYVKNV--DAIIL- 679
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQKHqLA---YLFISHDLHVVRALchQVIVLr 500
|
90 100 110
....*....|....*....|....*....|..
gi 383847295 680 ----IEQGKA-TVFSHYQDLLSQrpeyaELLA 706
Cdd:PRK15134 501 qgevVEQGDCeRVFAAPQQEYTR-----QLLA 527
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
842-1079 |
8.56e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 46.27 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 842 YNYMYIYTAIVVGlfcIGITRSLTFY--EVCI-VCSQK----LHDMAFSALIRTGMRFFDTNPSGRILNRFSKDMGTIDE 914
Cdd:cd18542 35 RELLWLLALLILG---VALLRGVFRYlqGYLAeKASQKvaydLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 915 LLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGTVFYW--IRKVYLKTSknikrlEGMSRspvfthLNA 986
Cdd:cd18542 112 FLAFGLVELVRAVLLFIGALIIMFSINWkltlisLAIIPFIALFSYVFFkkVRPAFEEIR------EQEGE------LNT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 987 T----LNGLTTIRAYCAQDILKKEFDKLQDVHTSTVYMYVVSSSGFGFSLDIFCFVFTSLVTF--SFLLLEQSFSGGEvg 1060
Cdd:cd18542 180 VlqenLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWvgGYLVINGEITLGE-- 257
|
250
....*....|....*....
gi 383847295 1061 laITQVMAMTGMIQWGMRQ 1079
Cdd:cd18542 258 --LVAFISYLWMLIWPVRQ 274
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1164-1199 |
8.69e-05 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 43.38 E-value: 8.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 1164 KIGIVGRTGAGKSSLISALF-RLAKV-----------EGVIEIDD-----IDT 1199
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTgAKAIVsdypgttrdpnEGRLELKGkqiilVDT 53
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
882-1012 |
8.72e-05 |
|
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: 45.94 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 882 FSALIRTGMRFFDTNPSGRILNRFSKDMGTIDEL--------LPKAVLDAGQICMMMFGSL---AVSCIVNPLFLIPIVF 950
Cdd:cd18575 76 FAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVvgsslsiaLRNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLPIIL 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383847295 951 LGtvfywiRKVYLKTSKNIKRLEGMSrspvfTHLNATLNGLTTIRAYCAQDILKKEFDKLQD 1012
Cdd:cd18575 156 FG------RRVRRLSRASQDRLADLS-----AFAEETLSAIKTVQAFTREDAERQRFATAVE 206
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
826-1077 |
9.03e-05 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 46.25 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 826 NATNETSTENLDISSMYNYMYIYTAIVVGlfcIGITRSLTFYEVcIVCSQKL-HDM---AFSALIRTGMRFFDTNPSGRI 901
Cdd:cd18541 24 RAIDALTAGTLTASQLLRYALLILLLALL---IGIFRFLWRYLI-FGASRRIeYDLrndLFAHLLTLSPSFYQKNRTGDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 902 LNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP---LF-LIPIVFLGTVFYWIRKVYLKTSKNI-KRLEGMS 976
Cdd:cd18541 100 MARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPkltLIaLLPLPLLALLVYRLGKKIHKRFRKVqEAFSDLS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 977 rspvfTHLNATLNGLTTIRAYCAQDILKKEFDKLQDVHTSTvYMYVVSSSGFGFSLDIFCFVFTSLVTFSF---LLLEQS 1053
Cdd:cd18541 180 -----DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEK-NLRLARVDALFFPLIGLLIGLSFLIVLWYggrLVIRGT 253
|
250 260
....*....|....*....|....
gi 383847295 1054 FSGGEvglaITQVMAMTGMIQWGM 1077
Cdd:cd18541 254 ITLGD----LVAFNSYLGMLIWPM 273
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
603-678 |
1.74e-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: 46.16 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 603 GERGSSLSGGQKARINLARSLYRQAD---VYLLDDPLSAVDTHVSKHLFeECIQRYL-AGKTRILATHQLQYVKNVDAII 678
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLL-EVLQRLVdKGNTVVVIEHNLDVIKTADYII 902
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1159-1342 |
2.07e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1159 INPGEKIGIVGRTGAGKSSLISALfrlakvEGVIEIDDidtGSIcLEDLRrhISIIPQ----DpvlFSGTLRRNLDPFNE 1234
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLL------AGVLKPDE---GEV-DPELK--ISYKPQyikpD---YDGTVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1235 FSDAALWEVLeevelkdavVISGNGLEsRVLDRG-SNYSVGQRQLVCLARAILRNNKILMLDEATANVDPQTDALIQNTI 1313
Cdd:PRK13409 427 DLGSSYYKSE---------IIKPLQLE-RLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190
....*....|....*....|....*....|..
gi 383847295 1314 RR--KFTKCTVLTIAHRLNTI-MDSDKVLVMD 1342
Cdd:PRK13409 497 RRiaEEREATALVVDHDIYMIdYISDRLMVFE 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1272-1351 |
2.13e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1272 SVGQRQLVCLARAILRNNKILMLDEATANVD-PQTDALIQnTIRRKFTKCTV-LTIAHRLNTIMD-SDKVLVMDKGR--- 1345
Cdd:PRK11288 142 SIGQRQMVEIAKALARNARVIAFDEPTSSLSaREIEQLFR-VIRELRAEGRViLYVSHRMEEIFAlCDAITVFKDGRyva 220
|
90
....*....|
gi 383847295 1346 ----MAEYDH 1351
Cdd:PRK11288 221 tfddMAQVDR 230
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1125-1309 |
2.40e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1125 APKNWPkDGMIRFRNVYMRYAEEELPVLKGLNLVinPGEKIGIVGRTGAGKSSLISALF-RLAKVEGVIEI-DDIDTGSI 1202
Cdd:PRK10636 304 APESLP-NPLLKMEKVSAGYGDRIILDSIKLNLV--PGSRIGLLGRNGAGKSTLIKLLAgELAPVSGEIGLaKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1203 CLEDLRrhisiipqdpvlfsgTLRRNLDPFNEFSDAALWEVleEVELKDavVISGNGLE-SRVLDRGSNYSVGQRQLVCL 1281
Cdd:PRK10636 381 AQHQLE---------------FLRADESPLQHLARLAPQEL--EQKLRD--YLGGFGFQgDKVTEETRRFSGGEKARLVL 441
|
170 180 190
....*....|....*....|....*....|...
gi 383847295 1282 ARAILRNNKILMLDEATANVD-----PQTDALI 1309
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDldmrqALTEALI 474
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
496-672 |
2.83e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.29 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 496 GQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNGS----LSYAGQEAW------VFG----- 560
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplakLNRAQRKAFrrdiqmVFQdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 561 ----STVRQNIlfGQPYdRH-----RYQKVVKACSLLRDFkqfpQSDQTVVGERGSSLSGGQKARINLARSLYRQADVYL 631
Cdd:PRK10419 102 vnprKTVREII--REPL-RHllsldKAERLARASEMLRAV----DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 383847295 632 LDDPLSAVDTHVSKH---LFEECIQRYlaGKTRILATHQLQYVK 672
Cdd:PRK10419 175 LDEAVSNLDLVLQAGvirLLKKLQQQF--GTACLFITHDLRLVE 216
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1166-1185 |
3.16e-04 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 42.33 E-value: 3.16e-04
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
495-640 |
3.21e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.01 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-------SLSYAGQEAWV-------FG 560
Cdd:PRK10575 22 PGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsSKAFARKVAYLpqqlpaaEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 561 STVRQNILFGQpYDRH----RY-----QKVVKACSLLrDFKQFPQSdqtVVgergSSLSGGQKARINLARSLYRQADVYL 631
Cdd:PRK10575 100 MTVRELVAIGR-YPWHgalgRFgaadrEKVEEAISLV-GLKPLAHR---LV----DSLSGGERQRAWIAMLVAQDSRCLL 170
|
....*....
gi 383847295 632 LDDPLSAVD 640
Cdd:PRK10575 171 LDEPTSALD 179
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
608-684 |
3.22e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 3.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 608 SLSGGQKARINLARSLYRQADVYLLDDPLSAVDTHVSKHLfeeciQRYLAG--KTRILATHQLQYVKNVDAIILIEQGK 684
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-----ETYLLKwpKTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
126-381 |
3.43e-04 |
|
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: 44.39 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 126 DETYETALWY---AAGICIATAINVITLNqaIFGAfHVGARIRVAtcsvVYRKALRLSKTALGETAPGKVVNLVANDVNR 202
Cdd:cd18577 44 DDVNKYALYFvylGIGSFVLSYIQTACWT--ITGE-RQARRIRKR----YLKALLRQDIAWFDKNGAGELTSRLTSDTNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 203 F-----DLVSIFIHHMwSAPLSALIIAYFLY---TeagyagLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIKTDERVRLM 274
Cdd:cd18577 117 IqdgigEKLGLLIQSL-STFIAGFIIAFIYSwklT------LVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 275 DEIISGVQVIKmyawekSFCALIETARKLE--LRVVKKSSYIRGIYMTFNLFTTRMALFCTLISMLLFGNELSADKVF-- 350
Cdd:cd18577 190 EEALSSIRTVK------AFGGEEKEIKRYSkaLEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEIsp 263
|
250 260 270
....*....|....*....|....*....|...
gi 383847295 351 --VFSSYFNIlahtMTGMFvrGFAEIAECLVAV 381
Cdd:cd18577 264 gdVLTVFFAV----LIGAF--SLGQIAPNLQAF 290
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
502-548 |
5.42e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 5.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGE--IDVVEGHVKVNGS 548
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGE 71
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
608-688 |
5.66e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 608 SLSGGQKARINLARSLYRQADVYLLDDPLSAVDT----HVS---KHLFEEciqrylAGKTRILATHQLQYVKNVDAIILI 680
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAAraiRRLSEE------GKKTALVVEHDLAVLDYLSDRIHV 144
|
....*...
gi 383847295 681 EQGKATVF 688
Cdd:cd03222 145 FEGEPGVY 152
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
467-554 |
6.20e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 467 EEKKRSS----SIRINEEP----YAVKMTNFTAKWEPGQsenTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDV 538
Cdd:PRK15064 295 EEVKPSSrqnpFIRFEQDKklhrNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP 371
|
90
....*....|....*...
gi 383847295 539 VEGHVK--VNGSLSYAGQ 554
Cdd:PRK15064 372 DSGTVKwsENANIGYYAQ 389
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
157-312 |
7.72e-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: 43.29 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 157 AFHVGARIRVAtcsvVYRKALRLSKTALGETAPGKVVNLVANDVNRFDLVsiFIHHMWSAPLSALII----AYFLYTEAG 232
Cdd:cd18778 68 EQKVVADLRSD----LYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERL--IADGIPQGITNVLTLvgvaIILFSINPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 233 YAGLIGIAAVFVVVPIQSYTGKLSSKFRLQTAIKTDERVRLMDEIiSGVQVIKMYAWE----KSFCALIETARKLELRVV 308
Cdd:cd18778 142 LALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNL-SGIREIQAFGREeeeaKRFEALSRRYRKAQLRAM 220
|
....
gi 383847295 309 KKSS 312
Cdd:cd18778 221 KLWA 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
885-1009 |
8.01e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 43.19 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 885 LIRTGMRFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPIVFLGTVFYW- 957
Cdd:cd18551 79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWvltlvtLAVVPLAFLIILPLGr 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 383847295 958 -IRKVYLKTSKNIKRLEGmsrspvftHLNATLNGLTTIRAYCAQDILKKEFDK 1009
Cdd:cd18551 159 rIRKASKRAQDALGELSA--------ALERALSAIRTVKASNAEERETKRGGE 203
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1152-1350 |
8.73e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.15 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1152 LKGLNLVINPGEKIGIVGRTGAGKSSLIsalfrlaKV--------EGVIEIDDIDtgsiclEDLRRHISII----PQ--- 1216
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTI-------KMltgilvptSGEVRVLGYVpfk-rrKEFARRIGVVfgqrSQlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1217 D-PVLFSGTL------------RRNLDpfnEFSdaalwEVLEEVELKDAVVisgnglesRVLdrgsnySVGQRQLVCLAR 1283
Cdd:COG4586 110 DlPAIDSFRLlkaiyripdaeyKKRLD---ELV-----ELLDLGELLDTPV--------RQL------SLGQRMRCELAA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 1284 AILRNNKILMLDEATANVdpqtDALIQNTIR------RKFTKCTVLTIAHRLNTIMD-SDKVLVMDKGRMAeYD 1350
Cdd:COG4586 168 ALLHRPKILFLDEPTIGL----DVVSKEAIReflkeyNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRII-YD 236
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1134-1182 |
8.85e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 8.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 383847295 1134 MIRFRNvyMRYAEEELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAL 1182
Cdd:PRK09580 1 MLSIKD--LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL 47
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
495-688 |
1.19e-03 |
|
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: 41.46 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 495 PGQSENTLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILG--EIDVVEGHVKVNG---------SLSYAGQEAWVFG-ST 562
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGrpldknfqrSTGYVEQQDVHSPnLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 563 VRQNILFGqpydrhryqkvvkacSLLRDfkqfpqsdqtvvgergssLSGGQKARINLARSLYRQADVYLLDDPLSAVDTh 642
Cdd:cd03232 96 VREALRFS---------------ALLRG------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 383847295 643 VSKHLFEECIQRY-LAGKTRILATHQ--LQYVKNVDAIILIEQGKATVF 688
Cdd:cd03232 142 QAAYNIVRFLKKLaDSGQAILCTIHQpsASIFEKFDRLLLLKRGGKTVY 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1151-1330 |
1.22e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 42.28 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1151 VLKGLNLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEIDDIDTGSICLEDLRRHISIIPQDPVLFSGTLRRNL 1229
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1230 DPFNEFSDAALWEVLEEvELKDAV--VISGNGLESRVLDRGSNYSVGQRQLVCLARAILRNNKILMLDEATA--NVDPQT 1305
Cdd:PRK10253 102 VARGRYPHQPLFTRWRK-EDEEAVtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTwlDISHQI 180
|
170 180
....*....|....*....|....*...
gi 383847295 1306 D--ALIQNTIRRK-FTKCTVLtiaHRLN 1330
Cdd:PRK10253 181 DllELLSELNREKgYTLAAVL---HDLN 205
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
875-972 |
1.23e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 42.47 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 875 QKLHDMAFSalirtgmrFFDTNPSGRILNRFSKDMGTIDELLPKAVLDAGQICMMMFGSLAVSCIVNP------LFLIPI 948
Cdd:cd18540 83 EHLQTLSFS--------YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalivLAVVPV 154
|
90 100
....*....|....*....|....
gi 383847295 949 VFLgtVFYWIRKVYLKTSKNIKRL 972
Cdd:cd18540 155 LAV--VSIYFQKKILKAYRKVRKI 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
502-723 |
1.38e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.00 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKG-KIyAVIGMVGAGKSSFL-------SAILGEIDVVEGhVKVngslSYAGQEAWVFGS-TVRQNI----- 567
Cdd:TIGR03719 21 LKDISLSFFPGaKI-GVLGLNGAGKSTLLrimagvdKDFNGEARPQPG-IKV----GYLPQEPQLDPTkTVRENVeegva 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 --------------LFGQPYDRH--------RYQKVVKACSL-------------LRdfkqFPQSDQTVvgergSSLSGG 612
Cdd:TIGR03719 95 eikdaldrfneisaKYAEPDADFdklaaeqaELQEIIDAADAwdldsqleiamdaLR----CPPWDADV-----TKLSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 613 QKARINLARSLYRQADVYLLDDPlsavdthvSKHLFEECI---QRYLAG--KTRILATHQLQYVKNVDAIIL-IEQGKAT 686
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEP--------TNHLDAESVawlERHLQEypGTVVAVTHDRYFLDNVAGWILeLDRGRGI 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 383847295 687 VF-SHYQDLLSQRpeyAELLaaENETHDDSSLEKSVMR 723
Cdd:TIGR03719 238 PWeGNYSSWLEQK---QKRL--EQEEKEESARQKTLKR 270
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
130-312 |
1.45e-03 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 42.41 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 130 ETALWYAAGICIATAI--NVITLNQAIFGAF---HVGARIRVAtcsvVYRKALRLSKTALGETAPGKVVNLVANDVNRF- 203
Cdd:cd18552 35 LEALLLVPLAIIGLFLlrGLASYLQTYLMAYvgqRVVRDLRND----LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVq 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 204 DLVSIFIHHMWSAPLSALI-IAYFLYTEAGYAGLIGIAAVFVVVPIqsytGKLSSKFR---LQTAIKTDERVRLMDEIIS 279
Cdd:cd18552 111 NALTSALTVLVRDPLTVIGlLGVLFYLDWKLTLIALVVLPLAALPI----RRIGKRLRkisRRSQESMGDLTSVLQETLS 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 383847295 280 GVQVIKMYAWEKS----FCALIETARKLELRVVKKSS 312
Cdd:cd18552 187 GIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARA 223
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
882-997 |
2.16e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 41.70 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 882 FSALIRTGMRFFDTNPSGRILNRFSKDM--------GTIDELLPKAVLDAGQICMMMFGSLAVSCIVnpLFLIPIVFLGT 953
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVtqiqdtltTTLAEFLRQILTLIGGVVLLFFISWKLTLLM--LATVPVVVLVA 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 383847295 954 VFY--WIRKVylktSKniKRLEGMSRSpvFTHLNATLNGLTTIRAY 997
Cdd:cd18576 154 VLFgrRIRKL----SK--KVQDELAEA--NTIVEETLQGIRVVKAF 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1147-1182 |
2.24e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|....*.
gi 383847295 1147 EELPVLKGLNLVINPGEKIGIVGRTGAGKSSLISAL 1182
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL 365
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
564-684 |
2.26e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 564 RQNI-LFGQPYDRHRYQKVVKACSLLRDFkqfpqSDQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVDTH 642
Cdd:NF000106 104 RENLyMIGR*LDLSRKDARARADELLERF-----SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 383847295 643 VSKHLFEECIQRYLAGKTRILATHQLQYVKNV-DAIILIEQGK 684
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLaHELTVIDRGR 221
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
609-678 |
2.37e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 2.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383847295 609 LSGGQKARINLARSL----YRQADVYLLDDPLSAVDTHVSKHLFEECIQRYLAGKTRILATHQLQYVKNVDAII 678
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
576-678 |
2.50e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 576 HRYQKVVKACSLLRDFkqFPqsdqtvVGERGSSLSGGQKARINLARSLY---RQADVYLLDDPLSAVDTHVSKHLFEECI 652
Cdd:PRK00635 785 SIHEKIHALCSLGLDY--LP------LGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQ 856
|
90 100
....*....|....*....|....*.
gi 383847295 653 QRYLAGKTRILATHQLQYVKNVDAII 678
Cdd:PRK00635 857 SLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1142-1345 |
2.77e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1142 MRYAEEELPVLKGL---NLVINPGEKIGIVGRTGAGKSSLISALFRL-AKVEGVIEID--DIDTGSiCLEDLRRHISIIP 1215
Cdd:PRK10982 1 MSNISKSFPGVKALdnvNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSILFQgkEIDFKS-SKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 1216 QDPVLfsgTLRRN-LDpfnefsdaALWE---------VLEEVELKDAVVISGN-GLESRVLDRGSNYSVGQRQLVCLARA 1284
Cdd:PRK10982 80 QELNL---VLQRSvMD--------NMWLgryptkgmfVDQDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383847295 1285 ILRNNKILMLDEATANV-DPQTDALIqnTIRRKFTK--CTVLTIAHRLNTIMD-SDKVLVMDKGR 1345
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLtEKEVNHLF--TIIRKLKErgCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
502-668 |
2.79e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 502 LDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEIDVVEGHVKVNG-SLSYAG---------QEAWVFGS-------TVR 564
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhDITRLKnrevpflrrQIGMIFQDhhllmdrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 565 QN-----ILFGQPYD--RHRYQKVVKACSLLRDFKQFPqsdqtvvgergSSLSGGQKARINLARSLYRQADVYLLDDPLS 637
Cdd:PRK10908 98 DNvaiplIIAGASGDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|....
gi 383847295 638 AVDTHVSK---HLFEEcIQRylAGKTRILATHQL 668
Cdd:PRK10908 167 NLDDALSEgilRLFEE-FNR--VGVTVLMATHDI 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
512-640 |
5.99e-03 |
|
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: 40.04 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 512 GKIYAVIGMVGAGKSSFLSAILGEI------------------------------DVVEGHVKVNGSLSYAGQEAWVFGS 561
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddppdwdeildefrgselqnyftKLLEGDVKVIVKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383847295 562 TVRQniLFGQPYDRHRYQKVVKACSLlrdfkqfpqsdQTVVGERGSSLSGGQKARINLARSLYRQADVYLLDDPLSAVD 640
Cdd:cd03236 106 KVGE--LLKKKDERGKLDELVDQLEL-----------RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| YlqF_related_GTPase |
cd01849 |
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ... |
442-543 |
7.23e-03 |
|
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.
Pssm-ID: 206746 [Multi-domain] Cd Length: 146 Bit Score: 38.52 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 442 DSEKRKHNGLVVVASDLLQKtanlmEEKKRSSSIRINEEPYAVKMTNFTA--KWEPGQSENTLDNLNLEIEKGKIYAVIG 519
Cdd:cd01849 24 INEKNKKLIMVLNKADLVPK-----EVLRKWVAELSELYGTKTFFISATNgqGILKLKAEITKQKLKLKYKKGIRVGVVG 98
|
90 100
....*....|....*....|....
gi 383847295 520 MVGAGKSSFLSAILGEIDVVEGHV 543
Cdd:cd01849 99 LPNVGKSSFINALLNKFKLKVGSI 122
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
421-688 |
7.51e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 421 KTSKPDIPYIDEETSTyeNLDDSEkrkhNGLVVVASDLLQKTANLMEEKKRSSSIriNEEPYAVKMTNFTAKWEpGQSEN 500
Cdd:TIGR00956 707 RGSLKRAKKAGETSAS--NKNDIE----AGEVLGSTDLTDESDDVNDEKDMEKES--GEDIFHWRNLTYEVKIK-KEKRV 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 501 TLDNLNLEIEKGKIYAVIGMVGAGKSSFLSAILGEID---VVEGHVKVNG---------SLSYAGQEAWVFG-STVRQNI 567
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGrpldssfqrSIGYVQQQDLHLPtSTVRESL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383847295 568 LFG----QP-----YDRHRY-QKVVKACSlLRDFKqfpqsdQTVVGERGSSLSGGQKARINLARSLYRQADVYL-LDDPL 636
Cdd:TIGR00956 858 RFSaylrQPksvskSEKMEYvEEVIKLLE-MESYA------DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 383847295 637 SAVDTHVSKHLFeeCIQRYLA--GKTrILAT-HQLQYV--KNVDAIILIEQGKATVF 688
Cdd:TIGR00956 931 SGLDSQTAWSIC--KLMRKLAdhGQA-ILCTiHQPSAIlfEEFDRLLLLQKGGQTVY 984
|
|
| |
