|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-1268 |
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: 777.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 2 SAVHEQRQPNPVTKANFFSKWFFIWTREILVKGLQRNLDPSDLYETEPSLESTQVSSFLLGHWEQELKRS---------- 71
Cdd:TIGR00957 193 SETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTrkqpvsavyg 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 72 -------------------------------KPNVLRMIFKAYGWSFVpASIVYSIMAIAVHTTQPLMLGGLVSFFSESt 120
Cdd:TIGR00957 273 kkdpskpkgssqldaneevealivksphkprKPSLFKVLYKTFGPYFL-MSFCFKAIHDLMMFIGPQILSLLIRFVNDP- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 121 gKITKHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYRKFLRVSVAADNSGVSGYAISLMATDLPTFN 200
Cdd:TIGR00957 351 -MAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFM 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 201 ESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAARAIARYKRSSADVGDERVKLMNEIIAAMQLI 280
Cdd:TIGR00957 430 DLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 281 KMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYA----GLQCTGMISKLSLFLSLVtYVFTGDIVTSQKVFIVASYYDHLND 356
Cdd:TIGR00957 510 KLYAWELAFLDKVEGIRQEELKVLKKSAYLHAvgtfTWVCTPFLVALITFAVYV-TVDENNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 357 SLlHSWPLAINMWVETFVVANRVKDFLFQHE-NPadggvhnfkeaeDNPEHgnffgRTHKPkAEVKSITVHKLSASWDQK 435
Cdd:TIGR00957 589 PL-NILPMVISSIVQASVSLKRLRIFLSHEElEP------------DSIER-----RTIKP-GEGNSITVHNATFTWARD 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 436 KQEKRHrhieDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLRGSLRDNILFTEPY 515
Cdd:TIGR00957 650 LPPTLN----GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKAL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 516 DEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLN 595
Cdd:TIGR00957 726 NEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 596 E--FLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL------------------------------------- 636
Cdd:TIGR00957 806 PegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELlqrdgafaeflrtyapdeqqghledswtalvsgegke 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 637 KKLIRFRMSVANDVEVAKLRAMRTDSVYEEPEPRKSLSQEEHMDRHEIEQQFK----EQQQIGSVKLQTYKEYFKVLGHp 712
Cdd:TIGR00957 886 AKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKlmeaDKAQTGQVELSVYWDYMKAIGL- 964
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 713 LVVVLILLMFVVARSSEATMDIFLSKWATWEETEPNQHEpipeyhrTRLRMMILYTFLILCTLIfyvlrTFGFFMMT--- 789
Cdd:TIGR00957 965 FITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNN-------TSLRLSVYGALGILQGFA-----VFGYSMAVsig 1032
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 790 -LRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAM---MDSIEFAVNALAVLaVVSTANIWLLI 865
Cdd:TIGR00957 1033 gIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIkmfMGSLFNVIGALIVI-LLATPIAAVII 1111
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 866 PATVVVALLygCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINR 945
Cdd:TIGR00957 1112 PPLGLLYFF--VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANR 1189
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 946 AFAFWTDLI--CVLYILAVtfsFLLFDKHrGYYSGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEYVNIPSE 1023
Cdd:TIGR00957 1190 WLAVRLECVgnCIVLFAAL---FAVISRH-SLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE 1265
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1024 PAYETEESVNlPKHWPSGGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFR-LAHINGHIS 1102
Cdd:TIGR00957 1266 APWQIQETAP-PSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRiNESAEGEII 1344
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1103 IDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSM 1182
Cdd:TIGR00957 1345 IDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1183 GQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPH 1262
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPS 1504
|
....*.
gi 221460257 1263 ELLHNR 1268
Cdd:TIGR00957 1505 NLLQQR 1510
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-1307 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 717.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 8 RQPNPVTKANFFSKWFFIWTREILVKGLQRNLDPSDLYETEPSLESTQVSSFLLGHWEQELKRSKPNVLRMIFKAYGWSF 87
Cdd:PLN03130 224 EQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKPWLLRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 88 VPASIvYSIMAIAVHTTQPLMLGGLVSffSESTGKITKHsAYLYA----MGVVLCSLISGLFFHPFMkylfRVGSRVRLA 163
Cdd:PLN03130 304 WLGGF-FKIGNDLSQFVGPLLLNLLLE--SMQNGEPAWI-GYIYAfsifVGVVLGVLCEAQYFQNVM----RVGFRLRST 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 164 CAGLVYRKFLRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIP 243
Cdd:PLN03130 376 LVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 244 LQAWAARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYA-GLQCTGMISK 322
Cdd:PLN03130 456 IQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAfNSFILNSIPV 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 323 LSLFLSLVTYVFTGDIVTSQKVFIVASYYDHLNdSLLHSWPLAINMWVETFVVANRVKDFLFQHEnpadggvhnfKEAED 402
Cdd:PLN03130 536 LVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLR-FPLFMLPNLITQAVNANVSLKRLEELLLAEE----------RVLLP 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 403 NPehgnffgrthkP-KAEVKSITVHKLSASWDQKKQEKRhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDII 481
Cdd:PLN03130 605 NP-----------PlEPGLPAISIKNGYFSWDSKAERPT---LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 482 S-GSVEVNGVLSYAPQEPWLLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVS 560
Cdd:PLN03130 671 SdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVS 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 561 LARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDALKK-- 638
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNng 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 639 -LIRFRMSVANDVEVAKLRAMRTDSVYEEPEPRK-----SLSQEEHMDRHEIEQQF----KEQQQIGSVKLQTYKEYFKV 708
Cdd:PLN03130 831 pLFQKLMENAGKMEEYVEENGEEEDDQTSSKPVAngnanNLKKDSSSKKKSKEGKSvlikQEERETGVVSWKVLERYKNA 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 709 LGHPLVVVLILLMFVVARSSEATMDIFLSKWAtwEETEPNQHEPipeyhrtrLRMMILYTFLILCTLIFYVLRTFGFFMM 788
Cdd:PLN03130 911 LGGAWVVMILFLCYVLTEVFRVSSSTWLSEWT--DQGTPKTHGP--------LFYNLIYALLSFGQVLVTLLNSYWLIMS 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 789 TLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLP---QAMMDSIEFAVNALAVLAVVSTANIWLLI 865
Cdd:PLN03130 981 SLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAvfvNMFLGQIFQLLSTFVLIGIVSTISLWAIM 1060
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 866 PATVvvaLLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINR 945
Cdd:PLN03130 1061 PLLV---LFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNR 1137
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 946 AFAFWTDLICVLYILaVTFSFLLFDKHRG----YYSGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEYVNIP 1021
Cdd:PLN03130 1138 WLAIRLETLGGLMIW-LTASFAVMQNGRAenqaAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLP 1216
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1022 SEpAYETEESVNLPKHWPSGGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGH 1100
Cdd:PLN03130 1217 SE-APLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELeRGR 1295
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1101 ISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANF 1180
Cdd:PLN03130 1296 ILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENF 1375
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1181 SMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGH 1260
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDT 1455
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*..
gi 221460257 1261 PHELLHNRHGYLHRFVEKTGVGTAQHLRHLAEQSyRKRVLGRKSEDQ 1307
Cdd:PLN03130 1456 PENLLSNEGSAFSKMVQSTGAANAQYLRSLVFGG-DEDRLAREESKA 1501
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-1290 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 681.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 12 PVTKANFFSKWFFIWTREILVKGLQRNLDPSDLYETEPSLESTQVSSFLLGHWEQELKRSKPNVLRMIFKAYGWSFVPAS 91
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKPWLLRALNNSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 92 IvYSIMAIAVHTTQPLMLGGLVSFFSESTGKITkhsAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYRK 171
Cdd:PLN03232 308 I-FKIGHDLSQFVGPVILSHLLQSMQEGDPAWV---GYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 172 FLRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAARA 251
Cdd:PLN03232 384 SLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 252 IARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGlqCTGMISKLSLFLSLV- 330
Cdd:PLN03232 464 MRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAF--NSFILNSIPVVVTLVs 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 331 --TYVFTGDIVTSQKVFIVASYYDHLNdSLLHSWPLAINMWVETFVVANRVKDFLFQHEnpadggvhnfKEAEDNP--EH 406
Cdd:PLN03232 542 fgVFVLLGGDLTPARAFTSLSLFAVLR-SPLNMLPNLLSQVVNANVSLQRIEELLLSEE----------RILAQNPplQP 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 407 GnffgrthkpkaeVKSITVHKLSASWDQKKQEKRhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDII-SGSV 485
Cdd:PLN03232 611 G------------APAISIKNGYFSWDSKTSKPT---LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSV 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 486 EVNGVLSYAPQEPWLLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAV 565
Cdd:PLN03232 676 VIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 566 YRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDALKK---LIRF 642
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKsgsLFKK 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 643 RMSVA-----------NDVEVAKLRAMRTDSVYEepepRKSLSQEEHMDRHEIEQQfKEQQQIGSVKLQTYKEYFKVLGH 711
Cdd:PLN03232 836 LMENAgkmdatqevntNDENILKLGPTVTIDVSE----RNLGSTKQGKRGRSVLVK-QEERETGIISWNVLMRYNKAVGG 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 712 PLVVVLILLMFVVARSSEATMDIFLSKWAtwEETEPNQHEpiPEYHrtrlrmMILYTFLILCTLIFYVLRTFGFFMMTLR 791
Cdd:PLN03232 911 LWVVMILLVCYLTTEVLRVSSSTWLSIWT--DQSTPKSYS--PGFY------IVVYALLGFGQVAVTFTNSFWLISSSLH 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 792 ISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAM---MDSIEFAVNALAVLAVVSTANIWLLIPat 868
Cdd:PLN03232 981 AAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMnmfMNQLWQLLSTFALIGTVSTISLWAIMP-- 1058
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 869 vVVALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFA 948
Cdd:PLN03232 1059 -LLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLT 1137
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 949 FWTD-LICVLYILAVTFSFLLF---DKHRGYYSgDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEYVNIPSEp 1024
Cdd:PLN03232 1138 IRLEtLGGVMIWLTATFAVLRNgnaENQAGFAS-TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSE- 1215
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1025 AYETEESVNLPKHWPSGGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISI 1103
Cdd:PLN03232 1216 ATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELeKGRIMI 1295
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1104 DGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMG 1183
Cdd:PLN03232 1296 DDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVG 1375
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1184 QRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHE 1263
Cdd:PLN03232 1376 QRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQE 1455
|
1290 1300
....*....|....*....|....*..
gi 221460257 1264 LLHNRHGYLHRFVEKTGVGTAQHLRHL 1290
Cdd:PLN03232 1456 LLSRDTSAFFRMVHSTGPANAQYLSNL 1482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-1268 |
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: 637.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 9 QPNPVTKANFFSKWFFIWTREILVKGLQRNLDPSDLYETePSLEST-QVSSFLLGHWEQELKRSK--PNVLRMIFKAYGW 85
Cdd:TIGR01271 2 QRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQI-PSFDSAdNLSERLEREWDRELASAKknPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 86 SFVpasiVYSIMAI---AVHTTQPLMLGGLVSFFsESTGKITKHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRL 162
Cdd:TIGR01271 81 RFV----FYGILLYfgeATKAVQPLLLGRIIASY-DPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 163 ACAGLVYRKFLRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFI 242
Cdd:TIGR01271 156 ALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 243 PLQAWAARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIR---------GSTYIYAG 313
Cdd:TIGR01271 236 LFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRkiaylryfySSAFFFSG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 314 LqctgmiskLSLFLSLVTYVFTGDIVTsQKVFIVASYYDHLNDSLLHSWPLAINMWVETFVVANRVKDFLFQHEnpadgg 393
Cdd:TIGR01271 316 F--------FVVFLSVVPYALIKGIIL-RRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEE------ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 394 vhnFKEAEDNpehgnffgrthkpkAEVKSITVHKLSASWDQK--------KQEKRHRH--------------------IE 445
Cdd:TIGR01271 381 ---YKTLEYN--------------LTTTEVEMVNVTASWDEGigelfekiKQNNKARKqpngddglffsnfslyvtpvLK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLRGSLRDNILFTEPYDEQRYLEVLR 525
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 526 VCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRIL 605
Cdd:TIGR01271 524 ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRIL 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 606 VTHRVQLLRHVDHLVLLEGGRISVQG--------------------HYDALKKLIR--------FRMSVANDVEVAKLRA 657
Cdd:TIGR01271 604 VTSKLEHLKKADKILLLHEGVCYFYGtfselqakrpdfsslllgleAFDNFSAERRnsiltetlRRVSIDGDSTVFSGPE 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 658 MRTDSVYEEP----EPRKS------------------------LSQEEHMDRHEIEQQFK-----EQQQIGSVKLQTYKE 704
Cdd:TIGR01271 684 TIKQSFKQPPpefaEKRKQsiilnpiasarkfsfvqmgpqkaqATTIEDAVREPSERKFSlvpedEQGEESLPRGNQYHH 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 705 YFKVLGHPLVVVLILL-------------------MFVVARSSEAT--MDIF---LSKWATWEETEP-----------NQ 749
Cdd:TIGR01271 764 GLQHQAQRRQSVLQLMthsnrgenrreqlqtsfrkKSSITQQNELAseLDIYsrrLSKDSVYEISEEineedlkecfaDE 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 750 HEPIPEYH--RTRLRMMI----LYTFLILCTLIF---------------------------------------------- 777
Cdd:TIGR01271 844 RENVFETTtwNTYLRYITtnrnLVFVLIFCLVIFlaevaasllglwlitdnpsapnyvdqqhanasspdvqkpviitpts 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 778 -------YV-----LRTFGFFM------MTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAM 839
Cdd:TIGR01271 924 ayyifyiYVgtadsVLALGFFRglplvhTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTL 1003
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 840 MDSIEFAVNALAVLAVVSTANIWLLIPATVVVALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGT 919
Cdd:TIGR01271 1004 FDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQ 1083
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 920 KYMERDFHYYQNENTSALYLHVSINRAFAFWTDLICVLYILAVTFSFLLFDKHRgyySGDVGLAITQSMKLVLMCQAGMR 999
Cdd:TIGR01271 1084 SYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNILSTLQWAVN 1160
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1000 QTVELENMMTSVERVMEYVNIPSEPAYETE-------------ESVNLPKHWPSGGQLDFRDLRLRYSNHGPYILKGLTF 1066
Cdd:TIGR01271 1161 SSIDVDGLMRSVSRVFKFIDLPQEEPRPSGgggkyqlstvlviENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSF 1240
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1067 TIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLDPFEEKTD 1146
Cdd:TIGR01271 1241 SVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSD 1320
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1147 EELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKF 1226
Cdd:TIGR01271 1321 EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF 1400
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|..
gi 221460257 1227 AHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHNR 1268
Cdd:TIGR01271 1401 SNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
76-1292 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 592.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 76 LRMIFKA---YGWSFVPASIVYSIMAIAVhttqPLMLGGLVSFFSESTGkiTKHSAYLYAMGVVLCSLISGLFFHPFMKY 152
Cdd:PTZ00243 235 LRTLFAAlpyYVWWQIPFKLLSDVCTLTL----PVLLKYFVKFLDADNA--TWGRGLGLVLTLFLTQLIQSVCLHRFYYI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 153 LFRVGSRVRLACAGLVYRKFLRVS--VAADNSGVSGYAISLMATDLPTFNE-SFYCFHeLWRGPLEGVVFVYIIYQLIGW 229
Cdd:PTZ00243 309 SIRCGLQYRSALNALIFEKCFTISskSLAQPDMNTGRIINMMSTDVERINSfMQYCMY-LWSSPMVLLLSILLLSRLVGW 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 230 PAVVGLGTIVAFIPLQAWAARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGsty 309
Cdd:PTZ00243 388 CALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRD--- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 310 IYAGLQCTGMIS----KLSLFLSLVTYVFTGDIVTSQKVFIVASYYDHLNDSLLHsWPLAINMWVETFVVANRVKDFLfQ 385
Cdd:PTZ00243 465 VQLARVATSFVNnatpTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFM-IPWVFTTVLQFLVSIKRISTFL-E 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 386 HENPADGGVHNFKE-AEDNPEHG------------------------------NFFGRTH--------KPKAEVKSITVH 426
Cdd:PTZ00243 543 CDNATCSTVQDMEEyWREQREHStacqlaavlenvdvtafvpvklprapkvktSLLSRALrmlcceqcRPTKRHPSPSVV 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 427 -------------------------------KLSASWDQKKQEKRHR-----HIEDVSFQAQDQQFVGIVGTVGAGKSTL 470
Cdd:PTZ00243 623 vedtdygspssasrhiveggtgggheatptsERSAKTPKMKTDDFFElepkvLLRDVSVSVPRGKLTVVLGATGSGKSTL 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 471 LQVILGELDIISGSVEVNGVLSYAPQEPWLLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGAS 550
Cdd:PTZ00243 703 LQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVN 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 551 LSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQ 630
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFS 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 631 GHYDAL---------------KKLIRFRMSVANDVEVAKLRAMRTDSVYEEPEPRKSLSQEEHMDRHEIEQQF--KEQQQ 693
Cdd:PTZ00243 863 GSSADFmrtslyatlaaelkeNKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGRLmtREEKA 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 694 IGSVKLQTYKEYFKVLGHPLVVVLILLMFVVARSSEATMDIFLSKWATWEETEPNQhepipeyhrtrlRMMILYTFLILC 773
Cdd:PTZ00243 943 SGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAA------------TYLYVYLGIVLL 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 774 TLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVL 853
Cdd:PTZ00243 1011 GTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSI 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 854 AVVSTANIWLLIPATVVVALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNEN 933
Cdd:PTZ00243 1091 LVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVV 1170
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 934 TSALYLHVSINRAFAFWTDLICVLYILAVTF-----SFLLFDKHRgyySGDVGLAITQSMKLVLMCQAGMRQTVELENMM 1008
Cdd:PTZ00243 1171 YSCSYLENVANRWLGVRVEFLSNIVVTVIALigvigTMLRATSQE---IGLVSLSLTMAMQTTATLNWLVRQVATVEADM 1247
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1009 TSVERVMEYV-NIPSEPAYETEESVNL------------------PKHWPS-------GGQLDFRDLRLRYSNHGPYILK 1062
Cdd:PTZ00243 1248 NSVERLLYYTdEVPHEDMPELDEEVDAlerrtgmaadvtgtvviePASPTSaaphpvqAGSLVFEGVQMRYREGLPLVLR 1327
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1063 GLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLDPF 1141
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPF 1407
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1142 EEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILI-MDEATANVDPETDNLIQE 1220
Cdd:PTZ00243 1408 LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQA 1487
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 1221 AIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHNRHGYLHRFVEKTGVGTAQHLRHLAE 1292
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGRSEAKRFLQLVG 1559
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1042-1261 |
3.44e-127 |
|
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: 391.09 E-value: 3.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRRI 1120
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKI 1200
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1201 LIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHP 1261
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
423-626 |
2.89e-102 |
|
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: 323.27 E-value: 2.89e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEkRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLR 502
Cdd:cd03250 1 ISVEDASFTWDSGEQE-TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 503 GSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:cd03250 80 GTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 583 SHVSKMLLDRCLNEFLSK-KIRILVTHRVQLLRHVDHLVLLEGGR 626
Cdd:cd03250 160 AHVGRHIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
761-1277 |
4.08e-97 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 323.27 E-value: 4.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 761 LRMMILYTFLILCTLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMM 840
Cdd:COG1132 61 LLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 841 DSIEFAVNALAVLAVVSTANIWLLIPATVVVALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTK 920
Cdd:COG1132 141 QLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 921 YMERDFHYYQNENTSALYLHVSINRAFAFWTDLICVL-YILAVTFSFLLFDkhRGYYS-GDVGLAITQSMKLVLMCQAGM 998
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLGNLgLALVLLVGGLLVL--SGSLTvGDLVAFILYLLRLFGPLRQLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 999 RQTVELENMMTSVERVMEYVNIPSEPAyETEESVNLPkhwPSGGQLDFRDLRLRYSNhGPYILKGLTFTIRGEEKIGIVG 1078
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIP-DPPGAVPLP---PVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1079 HTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfeEKTDEELWLALE 1154
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTsGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1155 AVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTI 1234
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 221460257 1235 AHRLHTVMDNDRVMVVDMGRVVELGHPHELLhNRHGYLHRFVE 1277
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELL-ARGGLYARLYR 573
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1038-1261 |
4.41e-88 |
|
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: 284.30 E-value: 4.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1038 WPSGGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDL 1116
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEavklkefvsnLKDGincrlhdcGANFSMGQRQLVCLARALLR 1196
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR----------VSEG--------GLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1197 QNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHP 1261
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
715-1018 |
1.58e-86 |
|
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: 283.63 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 715 VVLILLMFVVARSSEATMDIFLSKWATWEETEPNqhepipeyHRTRLRMMILYTFLILCTLIFYVLRTFGFFMMTLRISL 794
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPN--------SSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 795 RIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLIPATVVVALL 874
Cdd:cd18580 73 RLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 875 YGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWTDLI 954
Cdd:cd18580 153 YLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 955 CVLYILAVTFSFLLFdkHRGYYSGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEYV 1018
Cdd:cd18580 233 GALLALVVALLAVLL--RSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
91-379 |
6.77e-81 |
|
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: 267.43 E-value: 6.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 91 SIVYSIMAIAVHTTQPLMLGGLVSFFSESTGKiTKHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYR 170
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDE-PLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 171 KFLRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAAR 250
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 251 AIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGLQCTGMIS-KLSLFLSL 329
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTpVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 221460257 330 VTYVFTGDIVTSQKVFIVASYYDHLNDSLLhSWPLAINMWVETFVVANRV 379
Cdd:cd18579 241 ATYVLLGNPLTAAKVFTALSLFNLLRFPLL-MLPQAISSLIEALVSLKRI 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
763-1277 |
2.24e-80 |
|
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: 280.18 E-value: 2.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 763 MMILYTFLILCTLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSS-----DVLAidVNLPQ 837
Cdd:COG2274 198 LAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDvesirEFLT--GSLLT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 838 AMMDSIeFAVNALAVLAVVStanIWLLIPATVVVALLYGCRCL--YIGASRSLKRIETISRspIYSHTNATFKGLATIRA 915
Cdd:COG2274 276 ALLDLL-FVLIFLIVLFFYS---PPLALVVLLLIPLYVLLGLLfqPRLRRLSREESEASAK--RQSLLVETLRGIETIKA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 916 LNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWTDLI------CVLYILA-------------VTFSFLlfdkhrgyy 976
Cdd:COG2274 350 LGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLqqlatvALLWLGAylvidgqltlgqlIAFNIL--------- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 977 sgdVGLAITQSMKLVLMCQagmrqtvELENMMTSVERVMEYVNIPSEPAyETEESVNLPKHwpsGGQLDFRDLRLRYSNH 1056
Cdd:COG2274 421 ---SGRFLAPVAQLIGLLQ-------RFQDAKIALERLDDILDLPPERE-EGRSKLSLPRL---KGDIELENVSFRYPGD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1057 GPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLR 1135
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1136 FNL---DPfeEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDP 1212
Cdd:COG2274 567 ENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1213 ETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGhPHELLHNRHGYLHRFVE 1277
Cdd:COG2274 645 ETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDG-THEELLARKGLYAELVQ 708
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
105-379 |
1.00e-77 |
|
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: 258.69 E-value: 1.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 105 QPLMLGGLVSFFSESTGKITKHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYRKFLRVSVAADNSGV 184
Cdd:cd18593 16 QPIFLGKLIRYFEGNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 185 SGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAARAIARYKRSSADVGD 264
Cdd:cd18593 96 VGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 265 ERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGLQCTGMIS-KLSLFLSLVTYVFTGDIVTSQK 343
Cdd:cd18593 176 KRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSsKLILFLTFLAYILLGNILTAER 255
|
250 260 270
....*....|....*....|....*....|....*.
gi 221460257 344 VFIVASYYDHLNDSLLHSWPLAINMWVETFVVANRV 379
Cdd:cd18593 256 VFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
93-379 |
1.81e-71 |
|
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: 241.00 E-value: 1.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 93 VYSIMAIAVHTTQPLMLGGLVSFFSESTgKITKHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYRKF 172
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVAYFVPDS-TVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 173 LRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAARAI 252
Cdd:cd18594 83 LKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 253 ARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAG-----LQCTGMISklslFL 327
Cdd:cd18594 163 AKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFnmaffFFSPTLVS----FA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 328 SLVTYVFTGDIVTSQKVFIVASYYDHLNDSLLHSWPLAINMWVETFVVANRV 379
Cdd:cd18594 239 TFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
711-1017 |
2.31e-70 |
|
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: 238.76 E-value: 2.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 711 HPLVVVLILLMFVVARSSEATMDIFLSKWATWEE-----TEPNQHE---PIPEYHRTRLRMMILYTFLILCTLIFYVLRT 782
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEklndtTDRVQGEnstNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 783 FGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIW 862
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 863 LLIPATVVVALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVS 942
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 943 INRAFAFWTDLICVLYILAVTFSFLLFDKHRGyySGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEY 1017
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLD--AGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1041-1276 |
2.89e-70 |
|
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: 235.96 E-value: 2.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1041 GGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRR 1119
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNK 1199
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1200 ILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHNRHGYLHRFV 1276
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1008-1267 |
1.82e-68 |
|
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: 241.59 E-value: 1.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1008 MTSVERVMEYVNIPSEPAYETEESVNlpkhWPSGGQLDFRDLRLRYSNHGPyILKGLTFTIRGEEKIGIVGHTAAGKSSI 1087
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLP----AAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1088 VHALFRLAH-INGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVS 1163
Cdd:COG4988 380 LNLLLGFLPpYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGLDEFVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1164 NLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMD 1243
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
|
250 260
....*....|....*....|....
gi 221460257 1244 NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1042-1265 |
1.21e-66 |
|
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: 224.80 E-value: 1.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYsNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRI 1120
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLFSGSLRFNLDPF-EEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNK 1199
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGrPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1200 ILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELL 1265
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
69-636 |
7.30e-62 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 222.73 E-value: 7.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 69 KRSKPNVLRMIF---KAYGWSFVpASIVYSIMAIAVHTTQPLMLGGLVSFFsesTGKITKHSAYLYAMGVVLCSLISGLF 145
Cdd:COG1132 2 SKSPRKLLRRLLrylRPYRGLLI-LALLLLLLSALLELLLPLLLGRIIDAL---LAGGDLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 146 FHPFMKYLFRVGSRVRLACAGLVYRKFLRVSVAADNSGVSGYAISLMATDLPTFNESFY-CFHELWRGPLEGV-VFVYII 223
Cdd:COG1132 78 SYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIgALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 224 YqlIGWP-AVVGLGTIVAFIPLQAWAARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKS----FAKLIGKVRK 298
Cdd:COG1132 158 V--IDWRlALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 299 EEMDSIRGSTYIYAGLQctgMISKLSLFLSLVT---YVFTGDIVTSQkVFIVASYYDHLNDSLLH-SWplAINMWVETFV 374
Cdd:COG1132 236 ANLRAARLSALFFPLME---LLGNLGLALVLLVgglLVLSGSLTVGD-LVAFILYLLRLFGPLRQlAN--VLNQLQRALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 375 VANRVKDFLFQHENPADGgvhnfkeaEDNPEHGNFFGRthkpkaevksITVHKLSASWDQKKQEkrhrhIEDVSFQAQDQ 454
Cdd:COG1132 310 SAERIFELLDEPPEIPDP--------PGAVPLPPVRGE----------IEFENVSFSYPGDRPV-----LKDISLTIPPG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 455 QFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNILFTEP-YDEQRY 520
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGRPdATDEEV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 LEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSK 600
Cdd:COG1132 447 EEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKG 525
|
570 580 590
....*....|....*....|....*....|....*.
gi 221460257 601 KIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:COG1132 526 RTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1044-1254 |
3.07e-58 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 197.99 E-value: 3.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISI 1122
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTsGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLFSGSLRFNLdpfeektdeelwlaleavklkefvsnlkdgincrlhdcganFSMGQRQLVCLARALLRQNKILI 1202
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 1203 MDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGR 1254
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
715-1017 |
1.31e-57 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 201.16 E-value: 1.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 715 VVLILLMFVVARSSEATMDIFLSKWAT---WEETEPNQHEPIPEYhrtrlrmMILYTFLILCTLIFYVLRTFGFFMMTLR 791
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASayeTSSALPPSEVSVLYY-------LGIYALISLLSVLLGTLRYLLFFFGSLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 792 ISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLIPATVVV 871
Cdd:cd18604 74 ASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 872 ALlyGCRC--LYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAF 949
Cdd:cd18604 154 AL--YVYIgrLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 950 WTDLICVLYILAVTFSFLLFdkhRGYYSGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEY 1017
Cdd:cd18604 232 RIDLLGALFSFATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
46-636 |
5.07e-56 |
|
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: 208.53 E-value: 5.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 46 ETEPSLESTQVSSFLLGHWEQELKRSKPNVLRMIFkaygwsfvpASIVYSIMAIAVhttqPLMLGGLVSffsestgKITK 125
Cdd:COG2274 129 EPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLL---------ASLLINLLALAT----PLFTQVVID-------RVLP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 126 HSAY--LYAMGVVLcslISGLFFHPFMKYL-----FRVGSRVRLACAGLVYRKFLRVSVAA--------------DNSGV 184
Cdd:COG2274 189 NQDLstLWVLAIGL---LLALLFEGLLRLLrsyllLRLGQRIDLRLSSRFFRHLLRLPLSFfesrsvgdlasrfrDVESI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 185 ----SGYAISLMAtDLPTFnesfycfhelwrgplegVVFVYIIYqLIGWP-AVVGLGTIVAFIPLQAWAARAIARYKRSS 259
Cdd:COG2274 266 reflTGSLLTALL-DLLFV-----------------LIFLIVLF-FYSPPlALVVLLLIPLYVLLGLLFQPRLRRLSREE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 260 ADVGDERVKLMNEIIAAMQLIKMYA--------WEKSFAKLIgkvrKEEMDSIRGSTYIYAGlqcTGMISKLSLFLSL-- 329
Cdd:COG2274 327 SEASAKRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYL----NARFKLRRLSNLLSTL---SGLLQQLATVALLwl 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 330 -VTYVFTGDIVTSQkvfIVA--SYYDHLNDSLLhSWPLAINMWVETFVVANRVKDFLfqhenpadggvhnfkEAEDNPEH 406
Cdd:COG2274 400 gAYLVIDGQLTLGQ---LIAfnILSGRFLAPVA-QLIGLLQRFQDAKIALERLDDIL---------------DLPPEREE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 407 GNFFGRTHKPKAEvksITVHKLSASWDQKKQEkrhrHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVE 486
Cdd:COG2274 461 GRSKLSLPRLKGD---IELENVSFRYPGDSPP----VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 487 VNGV-------------LSYAPQEPWLLRGSLRDNILFTEPY-DEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLS 552
Cdd:COG2274 534 IDGIdlrqidpaslrrqIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLS 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 553 GGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGH 632
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
....
gi 221460257 633 YDAL 636
Cdd:COG2274 693 HEEL 696
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
713-1018 |
2.39e-55 |
|
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: 195.47 E-value: 2.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 713 LVVVLILLMFVVARSSEATMDIFLSKW-----ATWEETEPNQHEPIP-EYHRTRLRM-MILYTFLILCTLIFYVLRTFGF 785
Cdd:cd18599 3 VVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsGNTTNNVDNSTVDSGnISDNPDLNFyQLVYGGSILVILLLSLIRGFVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 786 FMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLI 865
Cdd:cd18599 83 VKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 866 PATVVVALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINR 945
Cdd:cd18599 163 ALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMR 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 946 AFAFWTDLICVLYILAVTFSFLLFdkhRGYYS-GDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEYV 1018
Cdd:cd18599 243 WLAVRLDILAVLITLITALLVVLL---KGSISpAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1046-1270 |
3.69e-55 |
|
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: 192.06 E-value: 3.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHGPyILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISIIP 1124
Cdd:cd03253 3 FENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSsGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QDPVLFSGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKIL 1201
Cdd:cd03253 82 QDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1202 IMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLhNRHG 1270
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGG 227
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
715-1017 |
2.08e-54 |
|
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: 191.92 E-value: 2.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 715 VVLILLMFVVARSSEATMDIFLSKWATWEETEPNQHepipeYHRTRLRMMIlYTFLILCTLIFYVLRTFGFFMMTLRISL 794
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQD-----TEQRDYRLGV-YGALGLGQAIFVFLGSLALALGCVRASR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 795 RIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLIpATVVVALL 874
Cdd:cd18603 75 NLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLV-VIIPLAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 875 YGC--RcLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWTD 952
Cdd:cd18603 154 YFFiqR-FYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 953 LICVLYILAVTFSFLLFdkhRGYYS-GDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEY 1017
Cdd:cd18603 233 FLGNLIVLFAALFAVLS---RDSLSpGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1044-1274 |
1.12e-53 |
|
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: 187.82 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISI 1122
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDsGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLFSGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNK 1199
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1200 ILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHpHELLHNRHGYLHR 1274
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGT-HEELLAQGGVYAK 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
416-636 |
2.31e-53 |
|
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: 197.29 E-value: 2.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 416 PKAEVKSITVHKLSASWDQkkqekRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----- 490
Cdd:COG4988 330 PAAGPPSIELEDVSFSYPG-----GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdl 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 --------LSYAPQEPWLLRGSLRDNILFTEP-YDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSL 561
Cdd:COG4988 405 dpaswrrqIAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 562 ARAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1045-1278 |
8.94e-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: 185.05 E-value: 8.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1045 DFRDLRLRY-SNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDLRRRISI 1122
Cdd:cd03249 2 EFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLFSGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNK 1199
Cdd:cd03249 82 VSQEPVLFDGTIAENIrygKP--DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1200 ILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLhNRHGYLHRFVEK 1278
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM-AQKGVYAKLVKA 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
444-639 |
7.25e-52 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 184.29 E-value: 7.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLRGSLRDNILFTEPYDEQRYLEV 523
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 524 LRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIR 603
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190
....*....|....*....|....*....|....*.
gi 221460257 604 ILVTHRVQLLRHVDHLVLLEGGRISVQGHYDALKKL 639
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
92-378 |
8.59e-52 |
|
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: 184.21 E-value: 8.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 92 IVYSIMAIAvhttQPLMLGGLVSFFSESTGKITKhsAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYRK 171
Cdd:cd18595 7 LLSDILLFA----SPQLLKLLINFVEDPDEPLWK--GYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 172 FLRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAARA 251
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 252 IARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAglqCTGMISKLSLFL-SLV 330
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNA---VSSFLWTCAPFLvSLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 221460257 331 T---YVFTGD--IVTSQKVFIVASYYDHLNDSLLHSwPLAINMWVETFVVANR 378
Cdd:cd18595 238 TfatYVLSDPdnVLDAEKAFVSLSLFNILRFPLSML-PMVISNLVQASVSLKR 289
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1042-1268 |
2.66e-49 |
|
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: 176.58 E-value: 2.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDGFETSQLGLHDLRRRIS 1121
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKIL 1201
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1202 IMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHNR 1268
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
769-1274 |
8.28e-49 |
|
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: 183.76 E-value: 8.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 769 FLILCTLIFYVLRTFGFFMMT---LRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEF 845
Cdd:TIGR02203 59 VVIGLAVLRGICSFVSTYLLSwvsNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 846 AVNALAVLAVVSTANiWLLIPATVVVALLYGCRCLYIgaSRSLKRIETISRSPIYSHTNA---TFKGLATIRALNGTKYM 922
Cdd:TIGR02203 139 TLTVIGLFIVLLYYS-WQLTLIVVVMLPVLSILMRRV--SKRLRRISKEIQNSMGQVTTVaeeTLQGYRVVKLFGGQAYE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 923 ERDFHYYQNENTSalyLHVSINRAFAFWTDLICVLYILAVTFSFL--LFDKHRGYYS-GDVGLAITqSMKLVLmcqAGMR 999
Cdd:TIGR02203 216 TRRFDAVSNRNRR---LAMKMTSAGSISSPITQLIASLALAVVLFiaLFQAQAGSLTaGDFTAFIT-AMIALI---RPLK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1000 QTVELENMM----TSVERVMEYVNIPSEPAYETEEsvnLPKhwpSGGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIG 1075
Cdd:TIGR02203 289 SLTNVNAPMqrglAAAESLFTLLDSPPEKDTGTRA---IER---ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1076 IVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfEEKTDEELWL 1151
Cdd:TIGR02203 363 LVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIER 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1152 ALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTV 1231
Cdd:TIGR02203 442 ALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT 521
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 221460257 1232 LTIAHRLHTVMDNDRVMVVDMGRVVELGhPHELLHNRHGY---LHR 1274
Cdd:TIGR02203 522 LVIAHRLSTIEKADRIVVMDDGRIVERG-THNELLARNGLyaqLHN 566
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
715-1017 |
2.96e-48 |
|
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: 174.71 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 715 VVLILLMFVVARSSEATMDIFLSKW---ATWEETEPNQHEPIPEYHRTRLRMMILYTFLILCTLIFYVLRTFGFFMMTLR 791
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWteaNHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 792 ISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLIPATVVV 871
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 872 ALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWT 951
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 952 DLICVLYILAVTFSFLLFDKHRGYYSGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEY 1017
Cdd:cd18602 241 DYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
715-1017 |
1.10e-47 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 172.71 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 715 VVLILLMFVVARSSEATMDIFLSKWatweeTEPNQHEPIPEYHRTRLRMMILYTFLILCTLIFYVLRTFGFFMMTLRISL 794
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYW-----VSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 795 RIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLIPATVVVALL 874
Cdd:cd18605 76 RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 875 YGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWTDLI 954
Cdd:cd18605 156 YRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 955 CVLYILAV-TFSFLLFDKHRGYYSGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEY 1017
Cdd:cd18605 236 GVLIVTFVaLTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
997-1265 |
1.79e-47 |
|
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: 180.40 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 997 GMRQ-TVELENMMTSVERVMEYVNIPSEPAyeteesvnLPkhwPSGGQLDFRDLRLRYSNHGPyILKGLTFTIRGEEKIG 1075
Cdd:COG5265 321 EIRQaLADMERMFDLLDQPPEVADAPDAPP--------LV---VGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1076 IVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfeEKTDEELWL 1151
Cdd:COG5265 389 IVGPSGAGKSTLARLLFRFYDVTsGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1152 ALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTV 1231
Cdd:COG5265 467 AARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTT 546
|
250 260 270
....*....|....*....|....*....|....
gi 221460257 1232 LTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELL 1265
Cdd:COG5265 547 LVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
715-1017 |
5.07e-47 |
|
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: 170.35 E-value: 5.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 715 VVLILLMFVVARSSEATMDIFLSKWATWEetepnqhepipeYHRTRLRMMILYTFLILCTLIFYVLRTFGFFMMTLRISL 794
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDF------------FGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 795 RIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLIPATVVVALL 874
Cdd:cd18606 69 RLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 875 YGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWTDLI 954
Cdd:cd18606 149 YFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 955 CVLYILAVTFSFLLFDKHRGyySGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVMEY 1017
Cdd:cd18606 229 GSLLVLIVALLCVTRRFSIS--PSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
91-379 |
6.79e-47 |
|
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: 170.33 E-value: 6.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 91 SIVYSIMAIAVHTTQPLMLGGLVSFFSESTGKITKHSA---YLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGL 167
Cdd:cd18597 2 AGLLKLLADVLQVLSPLLLKYLINFVEDAYLGGPPPSIgygIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 168 VYRKFLRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAW 247
Cdd:cd18597 82 IYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 248 AARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGLQCTGM-ISKLSLF 326
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFsLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 221460257 327 LSLVTYVFTGDIVTSQKVFIVASYYDHLNDSLLHsWPLAINMWVETFVVANRV 379
Cdd:cd18597 242 LSFITYYATGHTLDPANIFSSLALFNVLRMPLMF-LPLALSSLADALVALKRI 293
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
444-625 |
5.85e-46 |
|
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: 164.81 E-value: 5.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVL-----------------SYAPQEPWLLRGSLR 506
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfeatrsrnrysvAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 507 DNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVS 586
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 221460257 587 KMLLDRCLNEFL--SKKIRILVTHRVQLLRHVDHLVLLEGG 625
Cdd:cd03290 177 DHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
444-631 |
1.02e-45 |
|
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: 164.30 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVTLFYGTLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPY-DEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKML 589
Cdd:cd03245 100 LGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221460257 590 LDRcLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQG 631
Cdd:cd03245 180 KER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1042-1256 |
2.24e-45 |
|
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: 163.14 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDLRRRI 1120
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLFSGSLRFNL---DPFeeKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQ 1197
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1198 NKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRlhTVMDN--DRVMVVDMGRVV 1256
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR--PSLLDlvDRIIVMDSGRIV 217
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
93-379 |
6.32e-45 |
|
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: 164.26 E-value: 6.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 93 VYSIMAIAVHTTQPLMLGGLVSFFSESTGKITKhsAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYRKF 172
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSD--GYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 173 LRVSVAADNSGVSGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAARAI 252
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 253 ARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGL----QCTGMIskLSLfLS 328
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCvyfwATTPVL--ISI-LT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 329 LVTYVFTGDIVTSQKVF-IVAsyydhLNDSL---LHSWPLAINMWVETFVVANRV 379
Cdd:cd18598 239 FATYVLMGNTLTAAKVFtSLA-----LFNMLigpLNAFPWVLNGLVEAWVSLKRL 288
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1004-1271 |
1.18e-44 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 171.82 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1004 LENMMTSVERVMEYVNIPSEPAYETEESVnlpkhwpSGGQLDFRDLRLRYsNHGPYILKGLTFTIRGEEKIGIVGHTAAG 1083
Cdd:PRK10790 308 LQQAVVAGERVFELMDGPRQQYGNDDRPL-------QSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1084 KSSIVHAL---FRLAHinGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKE 1160
Cdd:PRK10790 380 KSTLASLLmgyYPLTE--GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1161 FVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHT 1240
Cdd:PRK10790 458 LARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLST 537
|
250 260 270
....*....|....*....|....*....|.
gi 221460257 1241 VMDNDRVMVVDMGRVVELGHPHELLHNRHGY 1271
Cdd:PRK10790 538 IVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1046-1278 |
5.72e-44 |
|
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: 159.96 E-value: 5.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-AHINGHISIDGFETSQLGLHDLRRRISIIP 1124
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QDPVLFSGSLRFNLDPFEEKTDEELwlALEAVKLK---EFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKIL 1201
Cdd:cd03252 83 QENVLFNRSIRDNIALADPGMSMER--VIEAAKLAgahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1202 IMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLhNRHGYLHRFVEK 1278
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLYQL 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
422-636 |
1.52e-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: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQKKQEKrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----------- 490
Cdd:COG4987 333 SLELEDVSFRYPGAGRPV----LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 --LSYAPQEPWLLRGSLRDNILFTEPY-DEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYR 567
Cdd:COG4987 409 rrIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 568 KADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:COG4987 489 DAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
764-1273 |
1.74e-42 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 167.21 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 764 MILYTFLilcTLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVlaidvnlpQAMMDSI 843
Cdd:TIGR00958 207 MCLLSIA---SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDT--------QTMSRSL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 844 EFAVNALA---VLAVVSTA-NIWL----------LIPATVVVALLYGCRclYIGASRSLKriETISRSpiyshTNATFKG 909
Cdd:TIGR00958 276 SLNVNVLLrnlVMLLGLLGfMLWLsprltmvtliNLPLVFLAEKVFGKR--YQLLSEELQ--EAVAKA-----NQVAEEA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 910 LATIRALngtkymeRDF--------HYYQN-ENTSALYLHVSINRAFAFWTDLICVLYILAVTFsfllfdkhrgYYSGDv 980
Cdd:TIGR00958 347 LSGMRTV-------RSFaaeegeasRFKEAlEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVL----------YYGGQ- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 981 gLAITQSMK-------LVLMCQAG--MRQTVELEN-MMTSV---ERVMEYVNipSEPAYETEESvnlpkHWPSG--GQLD 1045
Cdd:TIGR00958 409 -LVLTGKVSsgnlvsfLLYQEQLGeaVRVLSYVYSgMMQAVgasEKVFEYLD--RKPNIPLTGT-----LAPLNleGLIE 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHGPY-ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISII 1123
Cdd:TIGR00958 481 FQDVSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTgGQVLLDGVPLVQYDHHYLHRQVALV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1124 PQDPVLFSGSLRFNLD-PFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILI 1202
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1203 MDEATANVDPETDNLIQEAihTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHNRHGYLH 1273
Cdd:TIGR00958 641 LDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1030-1250 |
1.25e-40 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 158.60 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1030 ESVNLPKHWPSGGQLDFRDLRLRYSNHGPyILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFET 1108
Cdd:TIGR02857 308 LAGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPtEGSIAVNGVPL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1109 SQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQR 1185
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP--DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1186 QLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVV 1250
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
423-626 |
1.71e-40 |
|
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: 147.53 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEKrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV----LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 -LSYAPQEPWLLRGSLRDNILftepydeqrylevlrvchldrdveqlplgdstrvgeggaslSGGQKARVSLARAVYRKA 569
Cdd:cd03228 77 nIAYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 570 DIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGR 626
Cdd:cd03228 116 PILILDEATSALDPETEALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1042-1266 |
9.59e-39 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 153.96 E-value: 9.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHGPYIlKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRlAH--INGHISIDGFETSQLGLHDLRRR 1119
Cdd:PRK13657 333 GAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQR-VFdpQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSGSLRFNLD-PFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQN 1198
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRvGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 1199 KILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLH 1266
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA 558
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
91-379 |
1.74e-38 |
|
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: 146.49 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 91 SIVYSIMAIAvhttQPLMLGGLVSFFsESTGKITKHSAYLYAMGVVLCSLISGLFFHpfmKYLF---RVGSRVRLACAGL 167
Cdd:cd18596 6 AVLSSVLSFA----PPFFLNRLLRYL-EDPGEDATVRPWVWVLLLFLGPLLSSLLDQ---QYLWigrRLSVRLRAILTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 168 VYRKFLRVSVAADNSGVSGYA-------------------ISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIG 228
Cdd:cd18596 78 IFEKALRRRDKSGSSKSSESKkkdkeededekssasvgkiNNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 229 WPAVVGLGTIVAFIPLQAWAARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGST 308
Cdd:cd18596 158 WSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRF 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 309 YIYAGLQCTGMISklSLFLSLVTY-VFT---GDIVTSQKVFIVASYYDHLNDSlLHSWPLAINMWVETFVVANRV 379
Cdd:cd18596 238 LLDLLLSLLWFLI--PILVTVVTFaTYTlvmGQELTASVAFTSLALFNMLRGP-LNVLPELITQLLQAKVSLDRI 309
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1012-1264 |
2.30e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.69 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1012 ERVMEYVNIPSEPAYETEESVNLPKHWpsggQLDFRDLRLrYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAL 1091
Cdd:PRK11174 322 ESLVTFLETPLAHPQQGEKELASNDPV----TIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1092 FRLAHINGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVSNLKDG 1168
Cdd:PRK11174 397 LGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1169 INCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVM 1248
Cdd:PRK11174 475 LDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIW 554
|
250
....*....|....*.
gi 221460257 1249 VVDMGRVVELGHPHEL 1264
Cdd:PRK11174 555 VMQDGQIVQQGDYAEL 570
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
90-379 |
2.74e-38 |
|
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: 145.01 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 90 ASIVYSIMAIAVHTTQPLMLGGLVSFFSESTGKItkHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVY 169
Cdd:cd18592 2 SILLLLISLIFGFIGPTILIRKLLEYLEDSDSSV--WYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 170 RKFLRVSVAADNSgvSGYAISLMATDLPTFNE--SFYCFheLWRGPLEGV-VFVYIIYqLIGWPAVVGLGTIVAFIPLQA 246
Cdd:cd18592 80 KKILRLRSLGDKS--VGELINIFSNDGQRLFDaaVFGPL--VIGGPVVLIlGIVYSTY-LLGPWALLGMLVFLLFYPLQA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 247 WAARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGL-QCTGMISKLSL 325
Cdd:cd18592 155 FIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISiSLAPIVPVIAS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 326 FLSLVTYVFTGDIVTSQKVF-IVASYYDHLndSLLHSWPLAINMWVETFVVANRV 379
Cdd:cd18592 235 VVTFLAHVALGNDLTAAQAFtVIAVFNSMR--FSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
447-638 |
4.52e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 151.92 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 447 VSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIiSGSVEVNGV-------------LSYAPQEPWLLRGSLRDNILFTE 513
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIelreldpeswrkhLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 514 P-YDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKMLLDR 592
Cdd:PRK11174 448 PdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH-SEQLVMQ 526
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221460257 593 CLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDALKK 638
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
444-622 |
5.07e-38 |
|
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: 150.51 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrdqIAWVPQHPFLFAGTIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPY-DEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKML 589
Cdd:TIGR02857 418 LARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
170 180 190
....*....|....*....|....*....|...
gi 221460257 590 LDRcLNEFLSKKIRILVTHRVQLLRHVDHLVLL 622
Cdd:TIGR02857 498 LEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
789-1238 |
6.82e-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: 150.20 E-value: 6.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 789 TLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVStaniWLLIPAt 868
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIA----VLSVPA- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 869 vvvALLYGCRCLYIG---------ASRSLKRIETISRSPIYSHTNATFKGLATIRAlNGTkyMERDFHYYQNENTSALYL 939
Cdd:TIGR02868 156 ---ALILAAGLLLAGfvaplvslrAARAAEQALARLRGELAAQLTDALDGAAELVA-SGA--LPAALAQVEEADRELTRA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 940 HVSINRAFAFWTDLICVLYILAVTFSFLLfdkhRGYYSGDVGLAITQSMKLVLMCQAGMRQT-------VELENMMTSVE 1012
Cdd:TIGR02868 230 ERRAAAATALGAALTLLAAGLAVLGALWA----GGPAVADGRLAPVTLAVLVLLPLAAFEAFaalpaaaQQLTRVRAAAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1013 RVME------YVNIPSEPAYETEEsvnlpkhwPSGGQLDFRDLRLRYSNhGPYILKGLTFTIRGEEKIGIVGHTAAGKSS 1086
Cdd:TIGR02868 306 RIVEvldaagPVAEGSAPAAGAVG--------LGKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKST 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1087 IVHALFR-LAHINGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLD-PFEEKTDEELWLALEAVKLKEFVSN 1164
Cdd:TIGR02868 377 LLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1165 LKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRL 1238
Cdd:TIGR02868 457 LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
106-354 |
1.27e-37 |
|
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: 143.91 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 106 PLMLGGLVSFFSEST----GKITKHSAYL----------YAMGVV--LCSLISGLFFHPFMKYLFRVGSRVRLACAGLVY 169
Cdd:cd18591 17 PLCISGIVDYVEENTysssNSTDKLSVSYvtveeffsngYVLAVIlfLALLLQATFSQASYHIVIREGIRLKTALQAMIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 170 RKFLRVSVAADNSG--VSGYAISLMATDlpTFN--ESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQ 245
Cdd:cd18591 97 EKALRLSSWNLSSGsmTIGQITNHMSED--ANNimFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 246 AWAARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGLQCTGMISklSL 325
Cdd:cd18591 175 YLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQAS--PI 252
|
250 260 270
....*....|....*....|....*....|...
gi 221460257 326 FLSLVTYV----FTGDIVTSQKVFIVASYYDHL 354
Cdd:cd18591 253 LVTLVTFGlypyLEGEPLTAAKAFSSLALFNQL 285
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
444-638 |
2.53e-37 |
|
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: 140.44 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPY-DEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKmL 589
Cdd:cd03254 99 LGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK-L 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221460257 590 LDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQG-HYDALKK 638
Cdd:cd03254 178 IQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGtHDELLAK 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1008-1278 |
1.00e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 147.66 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1008 MTSVERVMEYVNIPSEPAYETEESVNLPKhwpsgGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSI 1087
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQ-----VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1088 VHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVS 1163
Cdd:PRK11160 383 LQLLTRAWDPQqGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1164 NlKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMD 1243
Cdd:PRK11160 461 D-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
|
250 260 270
....*....|....*....|....*....|....*
gi 221460257 1244 NDRVMVVDMGRVVELGHPHELLhNRHGYLHRFVEK 1278
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELL-AQQGRYYQLKQR 573
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1042-1255 |
2.72e-36 |
|
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: 137.22 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHGPY-ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRR 1119
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPqGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSGSLRFNLD-PFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQN 1198
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1199 KILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRV 1255
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
701-1018 |
4.74e-36 |
|
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: 139.94 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 701 TYKEYF---KVLGHPLVVVLILLMFVVARSSEATMDIFLSKWA--TWEETEPNQHEPIPEYHRTRLRMMILYTFLILCTL 775
Cdd:cd18600 5 TYLRYItshKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRvnTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 776 IFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAV 855
Cdd:cd18600 85 AMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 856 VSTANIWLLIPATVVVALLYGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTS 935
Cdd:cd18600 165 VSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 936 ALYLHVSINRAFAFWTDLICVLYILAVTFSFLLFdkhRGYYSGDVGLAITQSMKLVLMCQAGMRQTVELENMMTSVERVM 1015
Cdd:cd18600 245 NWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGT---TGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIF 321
|
...
gi 221460257 1016 EYV 1018
Cdd:cd18600 322 KFI 324
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1044-1255 |
1.31e-35 |
|
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: 133.50 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDLRRRISI 1122
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLFSGSLRFNLdpfeektdeelwlaleavklkefvsnlkdgincrlhdcganFSMGQRQLVCLARALLRQNKILI 1202
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1203 MDEATANVDPETDNLIQEAI-HTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRV 1255
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1044-1268 |
1.37e-35 |
|
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: 135.54 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRlaHIN-------GHISIDGFETSQLGLHDL 1116
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKST----LLR--LLNgllkptsGEVLVDGKDITKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDP------------VLFsGSLRFNLDPFE--EKTDEelwlALEAVKLKEF----VSNLkdgincrlhdcga 1178
Cdd:COG1122 74 RRKVGLVFQNPddqlfaptveedVAF-GPENLGLPREEirERVEE----ALELVGLEHLadrpPHEL------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1179 nfSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMDN-DRVMVVDMGRVV 1256
Cdd:COG1122 136 --SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIV 213
|
250
....*....|..
gi 221460257 1257 ELGHPHELLHNR 1268
Cdd:COG1122 214 ADGTPREVFSDY 225
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1003-1270 |
2.05e-35 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 145.09 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1003 ELENMMTSVERVMEYvniPSEPAYETEESV--NLPKHWPSGGQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHT 1080
Cdd:TIGR03796 438 ELEGDLNRLDDVLRN---PVDPLLEEPEGSaaTSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGS 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1081 AAGKSSI---VHALFRlaHINGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL---DPfeEKTDEELWLALE 1154
Cdd:TIGR03796 515 GSGKSTIaklVAGLYQ--PWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1155 AVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKfaHCTVLTI 1234
Cdd:TIGR03796 591 DAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIV 668
|
250 260 270
....*....|....*....|....*....|....*.
gi 221460257 1235 AHRLHTVMDNDRVMVVDMGRVVELGhPHELLHNRHG 1270
Cdd:TIGR03796 669 AHRLSTIRDCDEIIVLERGKVVQRG-THEELWAVGG 703
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1042-1275 |
2.39e-35 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 143.62 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRI 1120
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDeGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLFSGSLRFNLD-PFEEK-TDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQN 1198
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAyARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1199 KILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHNRHGY--LHRF 1275
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYaqLHKM 578
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
446-639 |
3.20e-35 |
|
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: 134.59 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNILFT 512
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 513 EPY--DEQRyLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKMLL 590
Cdd:cd03249 101 KPDatDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE-SEKLV 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221460257 591 DRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDALKKL 639
Cdd:cd03249 179 QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
763-1274 |
1.15e-34 |
|
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: 142.96 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 763 MMILYTFLILCTLIFYVL-------RTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSsDVLAIDVNL 835
Cdd:TIGR01193 191 MMGTLGIISIGLIIAYIIqqilsyiQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 836 PQAMMdSIEFAVNALAVLA---VVSTANIWLL----IPATVVVALLYgcRCLYIGASRSLKRIETISRSPIYSHTNatfk 908
Cdd:TIGR01193 270 ASTIL-SLFLDMWILVIVGlflVRQNMLLFLLsllsIPVYAVIIILF--KRTFNKLNHDAMQANAVLNSSIIEDLN---- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 909 GLATIRALNGtkymeRDFHYYQNENTSALYLHVS--------INRAFAFWTDLICVLYIL----------------AVTF 964
Cdd:TIGR01193 343 GIETIKSLTS-----EAERYSKIDSEFGDYLNKSfkyqkadqGQQAIKAVTKLILNVVILwtgaylvmrgkltlgqLITF 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 965 SFLLfdkhrGYYSGDVGLAITQSMKLvlmcqagmrQTVELENmmtsvERVMEYVNIPSE--PAYETEESVNLpkhwpsGG 1042
Cdd:TIGR01193 418 NALL-----SYFLTPLENIINLQPKL---------QAARVAN-----NRLNEVYLVDSEfiNKKKRTELNNL------NG 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1043 QLDFRDLRLRYSnHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAL---FRLAHinGHISIDGFETSQLGLHDLRRR 1119
Cdd:TIGR01193 473 DIVINDVSYSYG-YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgfFQARS--GEILLNGFSLKDIDRHTLRQF 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSGSLRFNL--DPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQ 1197
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1198 NKILIMDEATANVDPETDNLIQEAIhTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLhNRHGYLHR 1274
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYAS 704
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
444-636 |
2.02e-34 |
|
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: 132.35 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTVLFNDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEP--YDEQRYlEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKM 588
Cdd:cd03253 97 YGRPdaTDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTH-TER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221460257 589 LLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:cd03253 175 EIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
444-632 |
4.04e-34 |
|
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: 131.08 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiglhdlrsrISIIPQDPVLFSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKMLL 590
Cdd:cd03244 100 PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE-TDALI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221460257 591 DRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGH 632
Cdd:cd03244 179 QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
444-636 |
8.50e-34 |
|
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: 130.43 E-value: 8.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEP-YDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDShVSKML 589
Cdd:cd03251 98 YGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 590 LDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:cd03251 177 VQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1042-1278 |
1.23e-33 |
|
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: 139.32 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRL-----AHINGHISIDGFETSQLGLHDL 1116
Cdd:TIGR03797 450 GAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST----LLRLllgfeTPESGSVFYDGQDLAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLR 1196
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVR 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1197 QNKILIMDEATANVDPETDNLIQEAIHTKFAhcTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLhNRHGYLHRFV 1276
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLERLKV--TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM-AREGLFAQLA 682
|
..
gi 221460257 1277 EK 1278
Cdd:TIGR03797 683 RR 684
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1044-1267 |
6.24e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.03 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL----AHINGHISIDGFETSQLGLHDLRRR 1119
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphgGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDP------------VLFsgSLRFNLDPFEEKTDEELWLaLEAVKLKEfvsnlkdgincRLHDCGANFSMGQRQL 1187
Cdd:COG1123 85 IGMVFQDPmtqlnpvtvgdqIAE--ALENLGLSRAEARARVLEL-LEAVGLER-----------RLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1188 VCLARALLRQNKILIMDEATANVDPETDNLIQEAIH--TKFAHCTVLTIAHRLHTVMDN-DRVMVVDMGRVVELGHPHEL 1264
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
...
gi 221460257 1265 LHN 1267
Cdd:COG1123 231 LAA 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1046-1254 |
6.51e-32 |
|
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: 124.12 E-value: 6.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDLRRRISIIP 1124
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QDP------------VLFsgSLRFNLDPfEEKTDEELWLALEAVKLKEFvsnlkdgincRLHDCgANFSMGQRQLVCLAR 1192
Cdd:cd03225 82 QNPddqffgptveeeVAF--GLENLGLP-EEEIEERVEEALELVGLEGL----------RDRSP-FTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1193 ALLRQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMDN-DRVMVVDMGR 1254
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
446-641 |
1.72e-31 |
|
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: 131.41 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNI-LF 511
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIAENIaRF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 TEPyDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLd 591
Cdd:COG4618 430 GDA-DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA- 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 592 RCLNEF-LSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDA-LKKLIR 641
Cdd:COG4618 508 AAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEvLARLAR 559
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
419-1277 |
1.81e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 134.77 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 419 EVKSITVHKLSASWDQKKQEKRHRhieDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVN---------- 488
Cdd:PTZ00265 379 DIKKIQFKNVRFHYDTRKDVEIYK---DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinl 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 489 -------GVLSyapQEPWLLRGSLRDNILFT----------------EPYDEQRYLEVLRVCHL---------------- 529
Cdd:PTZ00265 456 kwwrskiGVVS---QDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQENKNKRNSCRAkcagdlndmsnttdsn 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 530 -------------DRDV-------------EQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDS 583
Cdd:PTZ00265 533 eliemrknyqtikDSEVvdvskkvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 584 HvSKMLLDRCLNEFL--SKKIRILVTHRVQLLRHVDHLVLL--------------------------------------- 622
Cdd:PTZ00265 613 K-SEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnn 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 623 --------EGGRISVQGHYDAL---KKLIRFRMsvANDVEVAKLRAMRTD---------SVYEE------PEPRKSLSQE 676
Cdd:PTZ00265 692 nnnnkinnAGSYIIEQGTHDALmknKNGIYYTM--INNQKVSSKKSSNNDndkdsdmksSAYKDsergydPDEMNGNSKH 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 677 EHMD----RHEIEQQFKEQQQIGSVKLQTYKEYFK---------------VLGHPLVVVLILLMFVVARSSEATMDIFLS 737
Cdd:PTZ00265 770 ENESasnkKSCKMSDENASENNAGGKLPFLRNLFKrkpkapnnlrivyreIFSYKKDVTIIALSILVAGGLYPVFALLYA 849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 738 KWATWEETEPNQhepipEYHRTRLRMMILytFLILCTLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFT--LA 815
Cdd:PTZ00265 850 KYVSTLFDFANL-----EANSNKYSLYIL--VIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKH 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 816 TSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVnalavLAVVSTANIWLLIPatVVVALLYGCRCLY---------IGASR 886
Cdd:PTZ00265 923 APGLLSAHINRDVHLLKTGLVNNIVIFTHFIV-----LFLVSMVMSFYFCP--IVAAVLTGTYFIFmrvfairarLTANK 995
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 887 SL--KRIETISRSPIYSHTNATFK-----------GLATIRALNGTKY----MERDFHYY---QNENT---SALY----- 938
Cdd:PTZ00265 996 DVekKEINQPGTVFAYNSDDEIFKdpsfliqeafyNMNTVIIYGLEDYfcnlIEKAIDYSnkgQKRKTlvnSMLWgfsqs 1075
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 939 LHVSINrAFAFW-------TDLICVLYILAVTFSFLLfdkhRGYYSGDvglaitqsmklvLMCQAGmrqtvELENMMTSV 1011
Cdd:PTZ00265 1076 AQLFIN-SFAYWfgsflirRGTILVDDFMKSLFTFLF----TGSYAGK------------LMSLKG-----DSENAKLSF 1133
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1012 ERVMEYVNIPSEPAYETEESVNLPKHWPSGGQLDFRDLRLRY-SNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHA 1090
Cdd:PTZ00265 1134 EKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSL 1213
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1091 LFRL------AHI-------------------------------------------------NGHISIDGFETSQLGLHD 1115
Cdd:PTZ00265 1214 LMRFydlkndHHIvfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKD 1293
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1116 LRRRISIIPQDPVLFSGSLRFNLDpF--EEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARA 1193
Cdd:PTZ00265 1294 LRNLFSIVSQEPMLFNMSIYENIK-FgkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1194 LLRQNKILIMDEATANVDPETDNLIQEAIH--TKFAHCTVLTIAHRLHTVMDNDRVMVVD----MGRVVELGHPH-ELLH 1266
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNnpdrTGSFVQAHGTHeELLS 1452
|
1130
....*....|.
gi 221460257 1267 NRHGYLHRFVE 1277
Cdd:PTZ00265 1453 VQDGVYKKYVK 1463
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1027-1265 |
1.34e-30 |
|
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: 128.71 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1027 ETEESVNLPKhwPSGgQLDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAL---FRLAHinGHISI 1103
Cdd:COG4618 317 AEPERMPLPR--PKG-RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvWPPTA--GSVRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1104 DGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMG 1183
Cdd:COG4618 392 DGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1184 QRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAI-HTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPH 1262
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIrALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
|
...
gi 221460257 1263 ELL 1265
Cdd:COG4618 552 EVL 554
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
106-379 |
2.06e-30 |
|
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: 122.32 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 106 PLMLGGLVSFFSEstGKITKHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVYRKFLRVSVAADNSGVS 185
Cdd:cd18559 17 PSNLWLLLWFDDP--VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 186 GYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWPAVVGLGTIVAFIPLQAWAARAIARYKRSSADVGDE 265
Cdd:cd18559 95 GELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 266 RVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAG---LQCTGMIskLSLFLSLVTYVFTG--DIVT 340
Cdd:cd18559 175 RYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALavrLWCVGPC--IVLFASFFAYVSRHslAGLV 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 221460257 341 SQKVFIVASYYDHLNdsllhsWPLAINMWVETFVVANRV 379
Cdd:cd18559 253 ALKVFYSLALTTYLN------WPLNMSPEVITNIVAAEV 285
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1061-1208 |
5.79e-30 |
|
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: 116.59 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGS-----L 1134
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1135 RFNL---DPFEEKTDEELWLALEAVKLKEFVSNlkdgincRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATA 1208
Cdd:pfam00005 81 RLGLllkGLSKREKDARAEEALEKLGLGDLADR-------PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
444-636 |
5.94e-30 |
|
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: 119.51 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlrrqVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEP-YDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKML 589
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 590 LDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
410-636 |
6.21e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.86 E-value: 6.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 410 FGRTHKPKAEVKSITVHKLSASWDQKKQEKrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG 489
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYPDQPQPV----LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 490 V-------------LSYAPQEPWLLRGSLRDNILFTEPY-DEQRYLEVLRVCHLDRDVEQlPLGDSTRVGEGGASLSGGQ 555
Cdd:PRK11160 402 QpiadyseaalrqaISVVSQRVHLFSATLRDNLLLAAPNaSDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 556 KARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLdRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDA 635
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
.
gi 221460257 636 L 636
Cdd:PRK11160 560 L 560
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1044-1259 |
2.70e-29 |
|
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: 117.22 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHG--PYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDL---R 1117
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTsGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 RRISIIPQDPvlFSgslrfNLDP-------FEE-----KTDEELWLALEAVKLKEFVSNLKDGI-NCRLHDcganFSMGQ 1184
Cdd:cd03257 82 KEIQMVFQDP--MS-----SLNPrmtigeqIAEplrihGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHE----LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1185 RQLVCLARALLRQNKILIMDEATANVDPETD----NLIQEaIHTKFAhCTVLTIAHRLHTV-MDNDRVMVVDMGRVVELG 1259
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLKK-LQEELG-LTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
422-609 |
3.85e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 123.62 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQKKqekrhRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----------- 490
Cdd:TIGR02868 334 TLELRDLSAGYPGAP-----PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 --LSYAPQEPWLLRGSLRDNILFTEP-YDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYR 567
Cdd:TIGR02868 409 rrVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221460257 568 KADIYLLDDPLSAVDSHVSKMLLdRCLNEFLSKKIRILVTHR 609
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELL-EDLLAALSGRTVVLITHH 529
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
423-641 |
4.05e-29 |
|
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: 117.27 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSaswdqkKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:COG4555 2 IEVENLS------KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprearrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 LSYAPQEPWL-LRGSLRDNILFTEP-YDEQRYLEVLRVchlDRDVEQLPLGDS--TRVGEggasLSGGQKARVSLARAVY 566
Cdd:COG4555 76 IGVLPDERGLyDRLTVRENIRYFAElYGLFDEELKKRI---EELIELLGLEEFldRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 567 RKADIYLLDDPLSAVDShVSKMLLDRCLNEFL-SKKIRILVTHRVQLLRHV-DHLVLLEGGRISVQGHYDALKKLIR 641
Cdd:COG4555 149 HDPKVLLLDEPTNGLDV-MARRLLREILRALKkEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1044-1259 |
7.40e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 111.25 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFR-LAHINGHISIDGFETSQLGlHDLRRRISI 1122
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLFSGSLRFNLdpfeektdeelwlaleavklkefvsnlkdgincrlhdcGANFSMGQRQLVCLARALLRQNKILI 1202
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1203 MDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELG 1259
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
444-627 |
1.21e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 110.77 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 ftepydeqrylevlrvchldrdveqlplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLL 590
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 221460257 591 DRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRI 627
Cdd:cd03246 137 QAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
444-636 |
1.60e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.43 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqldswrsrLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPYDEQRYLE-VLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKML 589
Cdd:PRK10789 411 LGRPDATQQEIEhVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 590 LdRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:PRK10789 491 L-HNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1046-1254 |
2.64e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 109.26 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYsnHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRRISIIP 1124
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTsGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QdpvlfsgslrfnldpfeektdeelwlaleavklkefvsnlkdgincrlhdcganFSMGQRQLVCLARALLRQNKILIMD 1204
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 1205 EATANVDPETDNLIQEAIHTKFAH-CTVLTIAHRLHTVMD-NDRVMVVDMGR 1254
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1044-1271 |
4.00e-27 |
|
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: 117.31 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGP---YILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLG---LHDL 1116
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTsGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDPvlfSGSL---------------RFNLDPFEEKTD--EELwlaLEAVKLKEfvsnlkDGINCRLHDcgan 1179
Cdd:COG1123 341 RRRVQMVFQDP---YSSLnprmtvgdiiaeplrLHGLLSRAERRErvAEL---LERVGLPP------DLADRYPHE---- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1180 FSMGQRQLVCLARALLRQNKILIMDEATANVDPETD----NLIQEaIHTKFaHCTVLTIAHRLHtVMDN--DRVMVVDMG 1253
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRD-LQREL-GLTYLFISHDLA-VVRYiaDRVAVMYDG 481
|
250
....*....|....*....
gi 221460257 1254 RVVELGHPHELLHN-RHGY 1271
Cdd:COG1123 482 RIVEDGPTEEVFANpQHPY 500
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
444-579 |
4.11e-27 |
|
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: 108.12 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRG-SLRDNI 509
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 510 LFtePYDEQRYLEVLRVCHLDRDVEQLPLGD--STRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLS 579
Cdd:pfam00005 81 RL--GLLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
444-627 |
5.97e-27 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 110.64 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG-------------VLSYAPQEPWLLRGSLRDNI- 509
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNIa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 510 --LFTEPYDeqRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSK 587
Cdd:cd03248 110 ygLQSCSFE--CVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 221460257 588 MLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRI 627
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1060-1265 |
1.04e-26 |
|
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: 110.33 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHdLRRRISIIPQDPVLFSG-SLRFN 1137
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1138 LDPFEE---KTDEELWLALEAVkLKEFvsNLKDGINCRLHDcganFSMGQRQLVCLARALLRQNKILIMDEATANVDPET 1214
Cdd:COG4555 95 IRYFAElygLFDEELKKRIEEL-IELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1215 DNLIQEAI--HTKFAHCTVLTiAHRLHTVMD-NDRVMVVDMGRVVELGHPHELL 1265
Cdd:COG4555 168 RRLLREILraLKKEGKTVLFS-SHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
423-627 |
3.00e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.02 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDqkkqekRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------LSYA 494
Cdd:COG1121 7 IELENLTVSYG------GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 495 PQE---PWLLRGSLRDNIL--------FTEPYDEQRYLEVLRVchLDRdVEQLPLGDsTRVGEggasLSGGQKARVSLAR 563
Cdd:COG1121 81 PQRaevDWDFPITVRDVVLmgrygrrgLFRRPSRADREAVDEA--LER-VGLEDLAD-RPIGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 564 AVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIRIL-VTHRV-QLLRHVDHLVLLEGGRI 627
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILvVTHDLgAVREYFDRVLLLNRGLV 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
444-632 |
3.88e-26 |
|
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: 107.50 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIl 510
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistipledlrssLTIIPQDPTLFSGTIRSNL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 ftEPYDEQrylevlrvchldRDVEqlpLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKMLL 590
Cdd:cd03369 103 --DPFDEY------------SDEE---IYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221460257 591 DRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGH 632
Cdd:cd03369 165 QKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1044-1264 |
9.77e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 106.88 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL------AHINGHISIDGFETSQLGLHD-- 1115
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgAPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1116 LRRRISIIPQDPVLFSGSLRFNLD----PFEEKTDEELWL----ALEAVKLKEFVSNlkdgincRLHdcGANFSMGQRQL 1187
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELDErveeALRKAALWDEVKD-------RLH--ALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1188 VCLARALLRQNKILIMDEATANVDPETDNLIQEAIHtKFAH-CTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHEL 1264
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIA-ELKKeYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
440-625 |
1.10e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 106.46 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 440 RHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------LSYAPQE---PWLLRGSLRDN 508
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRrsiDRDFPISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 509 IL--------FTEPYDEQRYLEVLRVchLDRdVEQLPLGDStRVGEggasLSGGQKARVSLARAVYRKADIYLLDDPLSA 580
Cdd:cd03235 91 VLmglyghkgLFRRLSKADKAKVDEA--LER-VGLSELADR-QIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 581 VDSHVSKMLLdRCLNEFLSKKIRIL-VTHRV-QLLRHVDHLVLLEGG 625
Cdd:cd03235 163 VDPKTQEDIY-ELLRELRREGMTILvVTHDLgLVLEYFDRVLLLNRT 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
423-631 |
3.28e-25 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 106.28 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG------------- 489
Cdd:COG1120 2 LEAENLSVGYGGRPV------LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 490 VLSYAPQE---PWLLrgSLRDNIL---------FTEPYDE-----QRYLEVLRVCHL-DRDVEQLplgdstrvgeggasl 551
Cdd:COG1120 76 RIAYVPQEppaPFGL--TVRELVAlgryphlglFGRPSAEdreavEEALERTGLEHLaDRPVDEL--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 552 SGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEFLSKKIrILVTHRVQL-LRHVDHLVLLEGGRIS 628
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLEllRRLARERGRTV-VMVLHDLNLaARYADRLVLLKDGRIV 217
|
...
gi 221460257 629 VQG 631
Cdd:COG1120 218 AQG 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1046-1267 |
3.44e-25 |
|
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: 105.36 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHGPYI--LKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahIN-------GHISIDGFETSQL---GL 1113
Cdd:cd03258 4 LKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKST----LIRC--INglerptsGSVLVDGTDLTLLsgkEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1114 HDLRRRISIIPQdpvlfsgslRFNLdpFEEKT-DEELWLALE------------AVKLKEFVsNLKDgincRLHDCGANF 1180
Cdd:cd03258 78 RKARRRIGMIFQ---------HFNL--LSSRTvFENVALPLEiagvpkaeieerVLELLELV-GLED----KADAYPAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1181 SMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQE---AIHTKFAhCTVLTIAHRLHTVMD-NDRVMVVDMGRVV 1256
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILAllrDINRELG-LTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
250
....*....|.
gi 221460257 1257 ELGHPHELLHN 1267
Cdd:cd03258 221 EEGTVEEVFAN 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
423-627 |
4.36e-25 |
|
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: 104.88 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWdqKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:cd03255 1 IELKNLSKTY--GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 -----LSYAPQEPWLLRG-SLRDNILFTEPY-------DEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKA 557
Cdd:cd03255 79 frrrhIGFVFQSFNLLPDlTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYP-----------SELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 558 RVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEFLSKKIrILVTHRVQLLRHVDHLVLLEGGRI 627
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMEllRELNKEAGTTI-VVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
444-631 |
4.52e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 103.28 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEPWLLRGslrdnilftepYDEQrYL 521
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdLASLSPKELARKIA-----------YVPQ-AL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 522 EVLRVCHL-DRDVEqlplgdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEFL 598
Cdd:cd03214 83 ELLGLAHLaDRPFN---------------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLEllRRLARER 147
|
170 180 190
....*....|....*....|....*....|....
gi 221460257 599 SKKIrILVTHRVQL-LRHVDHLVLLEGGRISVQG 631
Cdd:cd03214 148 GKTV-VMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
715-988 |
7.10e-25 |
|
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: 105.80 E-value: 7.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 715 VVLILLMFVVARSSEATMDIFLSKWATWEeTEPNQHEPIPEyhrtrLRMMILYTFLILCTLIFYVLRTFGFFMMTLRISL 794
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQAL-----NVYSLALLLLGLAQFILSFLQSYLLNHTGERLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 795 RIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAMMDSIEFAVNALAVLAVVSTANIWLLIPATVVVALL 874
Cdd:pfam00664 75 RLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 875 YGCRCLYIGASRSLKRIETISRSPIYSHTNATFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWTDLI 954
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270
....*....|....*....|....*....|....*
gi 221460257 955 -CVLYILAVTFSFLLFDKHRgYYSGDVGLAITQSM 988
Cdd:pfam00664 235 gYLSYALALWFGAYLVISGE-LSVGDLVAFLSLFA 268
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
423-627 |
8.11e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 103.74 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKqekrhrHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGeLDII-SGSVEVNGV----------- 490
Cdd:COG4619 1 LELEGLSFRVGGKP------ILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD-LDPPtSGEIYLDGKplsampppewr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 --LSYAPQEPWLLRGSLRDNILFTEPYDEQRYLEVlrvcHLDRDVEQLPLGDS---TRVGEggasLSGGQKARVSLARAV 565
Cdd:COG4619 74 rqVAYVPQEPALWGGTVRDNLPFPFQLRERKFDRE----RALELLERLGLPPDildKPVER----LSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 566 YRKADIYLLDDPLSAVDSHvSKMLLDRCLNEFLSKKIR--ILVTH-RVQLLRHVDHLVLLEGGRI 627
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPE-NTRRVEELLREYLAEEGRavLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
444-626 |
9.84e-25 |
|
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: 101.55 E-value: 9.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQEPWllrgslRDNILFtepydeqryle 522
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdIAKLPLEEL------RRRIGY----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 523 vlrvchldrdVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvSKMLLDRCLNEFLSKKI 602
Cdd:cd00267 78 ----------VPQL---------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLRELAEEGR 131
|
170 180
....*....|....*....|....*.
gi 221460257 603 RIL-VTHRVQLL-RHVDHLVLLEGGR 626
Cdd:cd00267 132 TVIiVTHDPELAeLAADRVIVLKDGK 157
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
446-636 |
4.00e-24 |
|
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: 109.14 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV---------LSYA----PQEPWLLRGSLRDNILFT 512
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtqasLRAAigivPQDTVLFNDTIAYNIAYG 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 513 EP-YDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD 591
Cdd:COG5265 456 RPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA 535
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 592 rCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:COG5265 536 -ALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAEL 579
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
423-631 |
5.31e-24 |
|
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: 100.47 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEKrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:cd03247 1 LSINNVSFSYPEQEQQV----LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalssl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 LSYAPQEPWLLRGSLRDNIlftepydeqrylevlrvchldrdveqlplgdstrvgegGASLSGGQKARVSLARAVYRKAD 570
Cdd:cd03247 77 ISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 571 IYLLDDPLSAVDSHVSKMLLdRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQG 631
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1047-1259 |
5.34e-24 |
|
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: 100.20 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1047 RDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-AHINGHISIDGFETSQLGLHDLRRRISIIPQ 1125
Cdd:cd03214 3 ENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLlKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1126 dpvlfsgslrfnldpfeektdeelwlALEAVKLKEF----VSNLkdgincrlhdcganfSMGQRQLVCLARALLRQNKIL 1201
Cdd:cd03214 81 --------------------------ALELLGLAHLadrpFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 1202 IMDEATANVDP----ETDNLIQEaiHTKFAHCTVLTIAHRL-HTVMDNDRVMVVDMGRVVELG 1259
Cdd:cd03214 120 LLDEPTSHLDIahqiELLELLRR--LARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
423-638 |
6.78e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 101.68 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSaswdqkKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:COG1131 1 IEVRGLT------KRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 LSYAPQEPWLLRG-SLRDNILF-------TEPYDEQRYLEVLRVCHLDRDVEQlplgdstRVGeggaSLSGGQKARVSLA 562
Cdd:COG1131 75 IGYVPQEPALYPDlTVRENLRFfarlyglPRKEARERIDELLELFGLTDAADR-------KVG----TLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 563 RAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIRILV-THrvqLLRHV----DHLVLLEGGRISVQGHYDALK 637
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWEL-LRELAAEGKTVLLsTH---YLEEAerlcDRVAIIDKGRIVADGTPDELK 219
|
.
gi 221460257 638 K 638
Cdd:COG1131 220 A 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1044-1265 |
1.18e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 101.32 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-AHINGHISIDGFEtsqlgLHDLRRRISI 1122
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLlPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQ----DP--------VLFSGSL-RFNLDPFEEKTDEELWL-ALEAVKLKEF----VSNLkdgincrlhdcganfSMGQ 1184
Cdd:COG1121 80 VPQraevDWdfpitvrdVVLMGRYgRRGLFRRPSRADREAVDeALERVGLEDLadrpIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1185 RQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMDN-DRVMVVDmGRVVELGHPH 1262
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLN-RGLVAHGPPE 223
|
...
gi 221460257 1263 ELL 1265
Cdd:COG1121 224 EVL 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1044-1275 |
1.94e-23 |
|
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: 100.65 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIvhalfrLAHI-------NGHISIDG---FETSQLGL 1113
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTL------LRLIvgllrpdSGEVLIDGediSGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1114 HDLRRRISIIPQDPVLFSG-SLRFNLD-PFEEKTDEELWLALEAVKLK-EFVsNLKDGINCRlhdcGANFSMGQRQLVCL 1190
Cdd:cd03261 73 YRLRRRMGMLFQSGALFDSlTVFENVAfPLREHTRLSEEEIREIVLEKlEAV-GLRGAEDLY----PAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1191 ARALLRQNKILIMDEATANVDPETDNLIQEAIHT--KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
....*...
gi 221460257 1268 RHGYLHRF 1275
Cdd:cd03261 228 DDPLVRQF 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
442-627 |
2.02e-23 |
|
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: 99.90 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 442 RHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQE-------------PWLlrgSLR 506
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdVTGVPPERrnigmvfqdyalfPHL---TVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 507 DNILF-------TEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLS 579
Cdd:cd03259 91 ENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 580 AVDSHVS---KMLLDRCLNEFlsKKIRILVTH-RVQLLRHVDHLVLLEGGRI 627
Cdd:cd03259 160 ALDAKLReelREELKELQREL--GITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
372-636 |
3.60e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.81 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 372 TFVVANRVKDFlFQHENpadgGVHNFKEAEDNPEHGNFFGRthkpkaevksITVHKLSASWDQKKQEkrhrhIEDVSFQA 451
Cdd:PRK13657 299 VFMAAPKLEEF-FEVED----AVPDVRDPPGAIDLGRVKGA----------VEFDDVSFSYDNSRQG-----VEDVSFEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 452 QDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNILFTEP--YD 516
Cdd:PRK13657 359 KPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIRVGRPdaTD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 517 EQRYLEVLRVCHLDRdVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDShVSKMLLDRCLNE 596
Cdd:PRK13657 439 EEMRAAAERAQAHDF-IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV-ETEAKVKAALDE 516
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221460257 597 FLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:PRK13657 517 LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1044-1265 |
5.27e-23 |
|
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: 99.73 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFR-LAHINGHISIDGFETSQLGLHDLRRRISI 1122
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVL-FSGSLR----------FNLDPFEEKTDEEL-WLALEAVKLKEF----VSNLkdgincrlhdcganfSMGQRQ 1186
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryphLGLFGRPSAEDREAvEEALERTGLEHLadrpVDEL---------------SGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1187 LVCLARALLRQNKILIMDEATANVDP----ETDNLIQEaiHTKFAHCTVLTIAHRL-HTVMDNDRVMVVDMGRVVELGHP 1261
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 221460257 1262 HELL 1265
Cdd:COG1120 223 EEVL 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1044-1280 |
8.37e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.60 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQlGLHDLRRRISI 1122
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTsGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVL-----------FSGSLR-FNLDPFEEKTDEelwlALEAVKLKEFvsnlkdgincrLHDCGANFSMGQRQLVCL 1190
Cdd:COG1131 78 VPQEPALypdltvrenlrFFARLYgLPRKEARERIDE----LLELFGLTDA-----------ADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1191 ARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAH-CTVLTIAHRLHTVMDN-DRVMVVDMGRVVELGHPHELlhnR 1268
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDEL---K 219
|
250
....*....|...
gi 221460257 1269 HGYL-HRFVEKTG 1280
Cdd:COG1131 220 ARLLeDVFLELTG 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1048-1259 |
1.16e-22 |
|
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: 97.60 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1048 DLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFEtsqlgLHDLRRRISIIPQ- 1125
Cdd:cd03235 4 DLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKP-----LEKERKRIGYVPQr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1126 ------------DPVLFSGSLRFNLDPFEEKTDEELWL-ALEAVKLKEFvsnlkdgincrLHDCGANFSMGQRQLVCLAR 1192
Cdd:cd03235 77 rsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDeALERVGLSEL-----------ADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1193 ALLRQNKILIMDEATANVDPETDNLIQEAI-HTKFAHCTVLTIAHRLHTVMDN-DRVMVVDmGRVVELG 1259
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLrELRREGMTILVVTHDLGLVLEYfDRVLLLN-RTVVASG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1046-1260 |
3.15e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.66 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQL---GLHDLRRRIS 1121
Cdd:COG2884 4 FENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTsGQVLVNGQDLSRLkrrEIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDpvlfsgslrFNLdpFEEKTDEE-LWLALEAV-----KLKEFVS------NLKDGINCRLHdcgaNFSMGQRQLVC 1189
Cdd:COG2884 83 VVFQD---------FRL--LPDRTVYEnVALPLRVTgksrkEIRRRVRevldlvGLSDKAKALPH----ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1190 LARALLRQNKILIMDEATANVDPET-DNLIQ--EAIHTkfAHCTVLtIA-HRLHTVMD-NDRVMVVDMGRVVELGH 1260
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsWEIMEllEEINR--RGTTVL-IAtHDLELVDRmPKRVLELEDGRLVRDEA 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
423-627 |
3.80e-22 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 96.39 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEkrHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------LSYA 494
Cdd:cd03293 1 LEVRNVSKTYGGGGGA--VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 495 PQE----PWLlrgSLRDNILF-----TEPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLAR 563
Cdd:cd03293 79 FQQdallPWL---TVLDNVALglelqGVPKAEarERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 564 AVYRKADIYLLDDPLSAVDSHvSKMLLDRCLNEFLSKKIR--ILVTHRVQ---LLrhVDHLVLLEG--GRI 627
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAL-TREQLQEELLDIWRETGKtvLLVTHDIDeavFL--ADRVVVLSArpGRI 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1044-1254 |
4.19e-22 |
|
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: 95.61 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRY---SNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALF-RLAHINGHISIDGfetsqlglhdlrrR 1119
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSGSLRFNL---DPFEEktdEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLR 1196
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1197 QNKILIMDEATANVDPETDNLIqeaihtkFAHC---------TVLTIAHRLHTVMDNDRVMVVDMGR 1254
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1044-1264 |
4.31e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.78 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-AHINGHISIDGFETSQLGLHDLRRRISI 1122
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDP-VLFSGS-----LRFNLD----PFEEKTDEELWlALEAVKLKEFvsnlkdgincrLHDCGANFSMGQRQLVCLAR 1192
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddVAFGLEnigvPREEMVERVDQ-ALRQVGMEDF-----------LNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1193 ALLRQNKILIMDEATANVDPETDNLIQEAIHT--KFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHEL 1264
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1046-1267 |
5.98e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSS---IVHALFRLAHinGHISIDGFETSQLGLHDLRRRISI 1122
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQS--GEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDP-VLFSGS-----LRFNLdpfEEKTdeelwlaLEAVKLKEFVSNL--KDGINCRLHDCGANFSMGQRQLVCLARAL 1194
Cdd:PRK13632 88 IFQNPdNQFIGAtveddIAFGL---ENKK-------VPPKKMKDIIDDLakKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1195 LRQNKILIMDEATANVDPETDNLIQEAIHT--KFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
444-636 |
7.81e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.11 E-value: 7.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 F-TEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKML 589
Cdd:TIGR00958 577 YgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 590 LDrcLNEFLSKKIrILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:TIGR00958 657 QE--SRSRASRTV-LLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
423-627 |
2.40e-21 |
|
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: 94.87 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKqeKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQepwllR 502
Cdd:COG1124 2 LEVRNLSVSYGQGG--RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 503 GSLRDNI--LFTEPYD--------EQRYLEVLRVCHL---DRDVEQLplgdSTRVGEGGA-------SLSGGQKARVSLA 562
Cdd:COG1124 75 KAFRRRVqmVFQDPYAslhprhtvDRILAEPLRIHGLpdrEERIAEL----LEQVGLPPSfldryphQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 563 RAVYRKADIYLLDDPLSAVDSHVSKMLLDrclnefLSKKIR-------ILVTHRVQLLRHV-DHLVLLEGGRI 627
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILN------LLKDLReergltyLFVSHDLAVVAHLcDRVAVMQNGRI 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1044-1277 |
2.80e-21 |
|
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: 94.48 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRY--SNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLA-HINGHISIDGFETSQLGLHDLRRRI 1120
Cdd:COG1124 2 LEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPvlfSGSL--RFNLD-----PF----EEKTDEELWLALEAVKLKEfvsNLKDginCRLHDcganFSMGQRQLVC 1189
Cdd:COG1124 82 QMVFQDP---YASLhpRHTVDrilaePLrihgLPDREERIAELLEQVGLPP---SFLD---RYPHQ----LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1190 LARALLRQNKILIMDEATANVDP----ETDNLIQEAIHTKfaHCTVLTIAHRLHtVMDN--DRVMVVDMGRVVELGHPHE 1263
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREER--GLTYLFVSHDLA-VVAHlcDRVAVMQNGRIVEELTVAD 225
|
250
....*....|....*
gi 221460257 1264 LL-HNRHGYLHRFVE 1277
Cdd:COG1124 226 LLaGPKHPYTRELLA 240
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
444-608 |
2.86e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.77 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------LSYAPQE----PWLlrgSLRDNILF 511
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEpallPWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 -------TEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSh 584
Cdd:COG1116 104 glelrgvPKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDA- 171
|
170 180
....*....|....*....|....*..
gi 221460257 585 VSKMLLDRCLNEfLSKKIR---ILVTH 608
Cdd:COG1116 172 LTRERLQDELLR-LWQETGktvLFVTH 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
423-677 |
3.87e-21 |
|
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: 94.92 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSAswdqKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIiSGSVEVNGV------------ 490
Cdd:cd03289 3 MTVKDLTA----KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVswnsvplqkwrk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 -LSYAPQEPWLLRGSLRDNIlftEPYDEQRYLEVLRVCH---LDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVY 566
Cdd:cd03289 78 aFGVIPQKVFIFSGTFRKNL---DPYGKWSDEEIWKVAEevgLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 567 RKADIYLLDDPLSAVDShVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISvqgHYDALKKLIR----F 642
Cdd:cd03289 155 SKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVR---QYDSIQKLLNekshF 230
|
250 260 270
....*....|....*....|....*....|....*
gi 221460257 643 RMSVANDVEVAKLRAMRTDSVYEEPEPRKSLSQEE 677
Cdd:cd03289 231 KQAISPSDRLKLFPRRNSSKSKRKPRPQIQALQEE 265
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
425-626 |
1.00e-20 |
|
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: 91.76 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 425 VHKLSASWDQKKQEKrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQEPW---- 499
Cdd:cd03225 2 LKNLSFSYPDGARPA----LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdLTKLSLKELrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 500 ----------LLRGSLRDNILFT-----EPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLA 562
Cdd:cd03225 78 glvfqnpddqFFGPTVEEEVAFGlenlgLPEEEieERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 563 RAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIRIL-VTHRVQLLR-HVDHLVLLEGGR 626
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLEL-LKKLKAEGKTIIiVTHDLDLLLeLADRVIVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1044-1255 |
1.13e-20 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 90.53 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahIN-------GHISIDGFETSQLGlHDL 1116
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTT----LIKI--ILgllkpdsGEIKVLGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDPVLFSgslrfNLDPFEektdeelwlaleavklkefvsNLKdgincrlhdcganFSMGQRQLVCLARALLR 1196
Cdd:cd03230 72 KRRIGYLPEEPSLYE-----NLTVRE---------------------NLK-------------LSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1197 QNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRV 1255
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
444-677 |
1.14e-20 |
|
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: 99.21 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILgELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVswnsvtlqtwrkaFGVIPQKVFIFSGTFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDShVSKMLL 590
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQII 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 591 DRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISvqgHYDALKKLIR----FRMSVANDVEVAKLRAMRTDSVYEE 666
Cdd:TIGR01271 1393 RKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVK---QYDSIQKLLNetslFKQAMSAADRLKLFPLHRRNSSKRK 1469
|
250
....*....|.
gi 221460257 667 PEPRKSLSQEE 677
Cdd:TIGR01271 1470 PQPKITALREE 1480
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1043-1276 |
1.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.67 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1043 QLDFRDLRLRYSNhgPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL------AHINGHISIDGFETSQLGLHDL 1116
Cdd:PRK14247 3 KIEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDPVLFSgslrfNLDPFEE-----------KTDEEL-----WlALEAVKLKEFVSNlkdgincRLHDCGANF 1180
Cdd:PRK14247 81 RRRVQMVFQIPNPIP-----NLSIFENvalglklnrlvKSKKELqervrW-ALEKAQLWDEVKD-------RLDAPAGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1181 SMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAH-RLHTVMDNDRVMVVDMGRVVELG 1259
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
250
....*....|....*...
gi 221460257 1260 HPHELLHN-RHGYLHRFV 1276
Cdd:PRK14247 228 PTREVFTNpRHELTEKYV 245
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1039-1237 |
1.63e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1039 PSGGQLDFRDLRLRYSNHGPyILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFR-LA----HINGHISidgfetsqlgL 1113
Cdd:COG4178 358 SEDGALALEDLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKST----LLRaIAglwpYGSGRIA----------R 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1114 HDLRRrISIIPQDPVLFSGSLRFNL---DPFEEKTDEELWLALEAVKLKEFVSNLKDGincrlHDCGANFSMGQRQLVCL 1190
Cdd:COG4178 423 PAGAR-VLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAERLDEE-----ADWDQVLSLGEQQRLAF 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 1191 ARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHR 1237
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
427-631 |
1.88e-20 |
|
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: 91.44 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 427 KLSASWDQKKQEKRHRHI-EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSyapqepWLL---- 501
Cdd:cd03220 20 LKKLGILGRKGEVGEFWAlKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLglgg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 --RGSL--RDNILF-------TEPYDEQRYLEVLRVCHLDRDVEqLPLGdstrvgeggaSLSGGQKARVSLARAVYRKAD 570
Cdd:cd03220 94 gfNPELtgRENIYLngrllglSRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 571 IYLLDDPLSAVDSHVSKMLLDRcLNEFLSK-KIRILVTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRR-LRELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1044-1254 |
2.26e-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: 89.94 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLH--DLRRRI 1120
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPdSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLFSgslrfNLDPFEektdeelwlaleavklkefvsnlkdgiNCRLhdcgaNFSMGQRQLVCLARALLRQNKI 1200
Cdd:cd03229 79 GMVFQDFALFP-----HLTVLE---------------------------NIAL-----GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1201 LIMDEATANVDPETDNLIQEAIHTKFAH--CTVLTIAHRLHTVMD-NDRVMVVDMGR 1254
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
423-627 |
6.26e-20 |
|
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: 90.32 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEkrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVlSYAPQEPWLLR 502
Cdd:cd03256 1 IEVENLSKTYPNGKKA-----LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT-DINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 503 gSLRDNI-----------------------------------LFTePYDEQRYLEVLrvchldrdvEQLPLGD--STRVG 545
Cdd:cd03256 75 -QLRRQIgmifqqfnlierlsvlenvlsgrlgrrstwrslfgLFP-KEEKQRALAAL---------ERVGLLDkaYQRAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 546 EggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEflSKKIRILVT-HRVQL-LRHVDHLVL 621
Cdd:cd03256 144 Q----LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDllKRINR--EEGITVIVSlHQVDLaREYADRIVG 217
|
....*.
gi 221460257 622 LEGGRI 627
Cdd:cd03256 218 LKDGRI 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1052-1271 |
7.69e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 95.16 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1052 RYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRRISIIPQDPVLF 1130
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVsEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1131 SGSLRFNL---DPfeEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEAT 1207
Cdd:PRK10789 402 SDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1208 ANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGhPHELLHNRHGY 1271
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG-NHDQLAQQSGW 542
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
438-631 |
1.55e-19 |
|
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: 88.51 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 438 EKRHR-HIEDVSFQAqDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVL-----------------SYAPQE-- 497
Cdd:cd03297 7 EKRLPdFTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 498 --PWLlrgSLRDNILFTEPY-----DEQRYLEVLRVCHLDRDVEQLPLGdstrvgeggasLSGGQKARVSLARAVYRKAD 570
Cdd:cd03297 86 lfPHL---NVRENLAFGLKRkrnreDRISVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 571 IYLLDDPLSAVDSHVSKMLLDRcLNEFLS--KKIRILVTHR-VQLLRHVDHLVLLEGGRISVQG 631
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPE-LKQIKKnlNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
444-627 |
1.72e-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: 88.78 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDII-----SGSVEVNGVLSYAP---------------QEPWLLRG 503
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLdvdvlelrrrvgmvfQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 504 SLRDNILF---------TEPYDEqRYLEVLRVCHLDRDVeqlplGDSTrvgeGGASLSGGQKARVSLARAVYRKADIYLL 574
Cdd:cd03260 96 SIYDNVAYglrlhgiklKEELDE-RVEEALRKAALWDEV-----KDRL----HALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 575 DDPLSAVDShVSKMLLDRCLNEfLSKKIRIL-VTHRV-QLLRHVDHLVLLEGGRI 627
Cdd:cd03260 166 DEPTSALDP-ISTAKIEELIAE-LKKEYTIViVTHNMqQAARVADRTAFLLNGRL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
423-627 |
2.22e-19 |
|
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: 88.72 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKqeKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:cd03257 2 LEVKNLSVSFPTGG--GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 ----LSYAPQEPwllRGSLrdNILFT------EPY-----------DEQRYLEVLRVCHLDRDV-EQLPlgdstrvgegg 548
Cdd:cd03257 80 rrkeIQMVFQDP---MSSL--NPRMTigeqiaEPLrihgklskkeaRKEAVLLLLVGVGLPEEVlNRYP----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 549 ASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrclnefLSKKIR-------ILVTHRVQLLRHV-DHLV 620
Cdd:cd03257 144 HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILD------LLKKLQeelgltlLFITHDLGVVAKIaDRVA 217
|
....*..
gi 221460257 621 LLEGGRI 627
Cdd:cd03257 218 VMYAGKI 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1044-1264 |
2.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.79 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRY-SNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRRIS 1121
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAeSGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDP-VLFSGS-----LRFNLD----PFEEKTdEELWLALEAVKLKEFvsnlKDGINCRLhdcganfSMGQRQLVCLA 1191
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLEnkgiPHEEMK-ERVNEALELVGMQDF----KEREPARL-------SGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1192 RALLRQNKILIMDEATANVDPETD-NLIQ--EAIHTKFaHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHEL 1264
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRlELIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
446-626 |
2.66e-19 |
|
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: 86.86 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSyapQEPWLLRGSLRDNI--LFtepydeQRY--- 520
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL---TDLEDELPPLRRRIgmVF------QDFalf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 --LEVLrvchldrdvEQLPLGdstrvgeggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNE 596
Cdd:cd03229 89 phLTVL---------ENIALG-----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRAllKSLQA 148
|
170 180 190
....*....|....*....|....*....|.
gi 221460257 597 FLSKKIrILVTHRVQLLRHV-DHLVLLEGGR 626
Cdd:cd03229 149 QLGITV-VLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1045-1319 |
2.80e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.02 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1045 DFRDLRLRYSNHGPYI--LKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahIN-------GHISIDGFETSQL---G 1112
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKST----LIRC--INllerptsGRVLVDGQDLTALsekE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1113 LHDLRRRISIIPQdpvlfsgslRFNLdpFEEKT-DEELWLALEAV-----KLKEFVSNLKD--GINCRLHDCGANFSMGQ 1184
Cdd:PRK11153 77 LRKARRQIGMIFQ---------HFNL--LSSRTvFDNVALPLELAgtpkaEIKARVTELLElvGLSDKADRYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1185 RQLVCLARALLRQNKILIMDEATANVDPETDNLIQE---AIHTKFaHCTVLTIAHRlhtvMD-----NDRVMVVDMGRVV 1256
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILEllkDINREL-GLTIVLITHE----MDvvkriCDRVAVIDAGRLV 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1257 ELGHPHEL-LHNRHGYLHRFVEKTgvgTAQHLrhlaEQSYRKRVLGRKSEDQGSVLDLGYKGTT 1319
Cdd:PRK11153 221 EQGTVSEVfSHPKHPLTREFIQST---LHLDL----PEDYLARLQAEPTTGSGPLLRLEFTGES 277
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
444-627 |
3.24e-19 |
|
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: 86.30 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGvlsyapQEPWLLRGSLRDNILFtePYDEQRYLEV 523
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGY--LPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 524 LRVChldrdvEQLplgdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIR 603
Cdd:cd03230 88 LTVR------ENL-------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL-LRELKKEGKT 147
|
170 180
....*....|....*....|....*.
gi 221460257 604 ILV-THRVQLLRHV-DHLVLLEGGRI 627
Cdd:cd03230 148 ILLsSHILEEAERLcDRVAILNNGRI 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1046-1319 |
4.02e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRY-SNHGPYI-LKGLTFTI-RGEekI-GIVGHTAAGKSSivhaLFRLahIN-------GHISIDGFETSQL--- 1111
Cdd:COG1135 4 LENLSKTFpTKGGPVTaLDDVSLTIeKGE--IfGIIGYSGAGKST----LIRC--INllerptsGSVLVDGVDLTALser 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1112 GLHDLRRRISIIPQDpvlfsgslrFNLdpFEEKTDEE-LWLALEAVKLK------------EFVsNLKDgincRLHDCGA 1178
Cdd:COG1135 76 ELRAARRKIGMIFQH---------FNL--LSSRTVAEnVALPLEIAGVPkaeirkrvaellELV-GLSD----KADAYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1179 NFSMGQRQLVCLARALLRQNKILIMDEATANVDPETD----NLIQEaIHTKFaHCTVLTIAHRLHTVMD-NDRVMVVDMG 1253
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENG 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1254 RVVELGHPHELLHN-RHGYLHRFVEKTgvgtaqhLRHLAEQSYRKRVlgRKSEDQGSVLDLGYKGTT 1319
Cdd:COG1135 218 RIVEQGPVLDVFANpQSELTRRFLPTV-------LNDELPEELLARL--REAAGGGRLVRLTFVGES 275
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
423-627 |
6.95e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.02 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEkrhRHI-EDVSFQAQDQQFVGIVGTVGAGKSTLLQvILGELDII-SGSVEVNGV---------- 490
Cdd:COG1136 5 LELRNLTKSYGTGEGE---VTAlRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGQdisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 -------LSYAPQEPWLLRG-SLRDNILF-------TEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQ 555
Cdd:COG1136 81 arlrrrhIGFVFQFFNLLPElTALENVALplllagvSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 556 KARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrCLNEfLSKKIR---ILVTHRVQLLRHVDHLVLLEGGRI 627
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE-LLRE-LNRELGttiVMVTHDPELAARADRVIRLRDGRI 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
423-627 |
9.26e-19 |
|
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: 91.50 E-value: 9.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEKRHRhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRA-VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 ----LSYAPQEP-----------WLLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDV-EQLPlgdstrvgeggASLSGG 554
Cdd:COG1123 340 lrrrVQMVFQDPysslnprmtvgDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLaDRYP-----------HELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 555 QKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrclnefLSKKIR-------ILVTHRVQLLRHV-DHLVLLEGGR 626
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILN------LLRDLQrelgltyLFISHDLAVVRYIaDRVAVMYDGR 482
|
.
gi 221460257 627 I 627
Cdd:COG1123 483 I 483
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1044-1271 |
9.56e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 88.96 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYI--LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL----AHINGHISIDGFETSQLGLHDLR 1117
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpppGITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 ----RRISIIPQDPvlfSGSlrfnLDP-------FEE-------KTDEELWlaLEAVKLKEFVsnlkdGINC---RL--- 1173
Cdd:COG0444 82 kirgREIQMIFQDP---MTS----LNPvmtvgdqIAEplrihggLSKAEAR--ERAIELLERV-----GLPDperRLdry 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1174 -HdcgaNFSMGQRQLVCLARALLRQNKILIMDEATANVDPETD----NLIQEaIHTKFaHCTVLTIAHRLHTVMDN-DRV 1247
Cdd:COG0444 148 pH----ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQaqilNLLKD-LQREL-GLAILFITHDLGVVAEIaDRV 221
|
250 260
....*....|....*....|....*..
gi 221460257 1248 MVvdM--GRVVELGHPHELLHN-RHGY 1271
Cdd:COG0444 222 AV--MyaGRIVEEGPVEELFENpRHPY 246
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
444-638 |
1.00e-18 |
|
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: 86.62 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGvLSYAPQEPWLLR---GslrdnILFTEP------ 514
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG-KDITKKNLRELRrkvG-----LVFQNPddqlfa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 515 ---YDE----------------QRYLEVLRVCHL----DRDVeqlplgdstrvgeggASLSGGQKARVSLARAVYRKADI 571
Cdd:COG1122 91 ptvEEDvafgpenlglpreeirERVEEALELVGLehlaDRPP---------------HELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 572 YLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIR-ILVTHRVQLL-RHVDHLVLLEGGRISVQG-------HYDALKK 638
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLEL-LKRLNKEGKTvIIVTHDLDLVaELADRVIVLDDGRIVADGtprevfsDYELLEE 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
445-621 |
1.01e-18 |
|
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: 85.99 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------LSYAPQEPWLLRG-SLRDNILF 511
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHADGLKPElTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 -----TEPYDEQRYLEVLRVCHLdRDVEQLPLGdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHvS 586
Cdd:COG4133 99 waalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-G 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 221460257 587 KMLLDRCLNEFLSK-KIRILVTHRVQLLRHVDHLVL 621
Cdd:COG4133 167 VALLAELIAAHLARgGAVLLTTHQPLELAAARVLDL 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
422-582 |
2.33e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.21 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQkkqekrHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEpw 499
Cdd:COG3839 3 SLELENVSKSYGG------VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 500 llRG--------------SLRDNILF-----TEPYDE--QRYLEVLRVCHLDrdveqlPLGDStRVGEggasLSGGQKAR 558
Cdd:COG3839 75 --RNiamvfqsyalyphmTVYENIAFplklrKVPKAEidRRVREAAELLGLE------DLLDR-KPKQ----LSGGQRQR 141
|
170 180
....*....|....*....|....
gi 221460257 559 VSLARAVYRKADIYLLDDPLSAVD 582
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1044-1264 |
2.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.73 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRRISI 1122
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPV-LFSGSL-----RFNLDPFE---EKTDEELWLALEAVklkefvsnlkDGINCRLHDCGAnFSMGQRQLVCLARA 1193
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAvpyDEMHRRVSEALKQV----------DMLERADYEPNA-LSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1194 LLRQNKILIMDEATANVDPETD----NLIQEAIHTKfaHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHEL 1264
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARqnllDLVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
455-631 |
2.60e-18 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 84.85 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 455 QFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQEPWLLRGSLRDNILFTEPYDEQRY-LEVLRVCHLDRD 532
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdVTAAPPADRPVSMLFQENNLFAHLTVEQNVgLGLSPGLKLTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 533 VEQLPLGDSTRVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRIL- 605
Cdd:cd03298 105 DRQAIEVALARVGLAGlekrlpGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLm 184
|
170 180
....*....|....*....|....*..
gi 221460257 606 VTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:cd03298 185 VTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
448-636 |
3.17e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.19 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 448 SFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAP---------QE----PWLlrgSLRDNILF- 511
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdLTALPPaerpvsmlfQEnnlfPHL---TVAQNIGLg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 -------TEPyDEQRYLEVLRvchldrdveqlplgdstRVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDPL 578
Cdd:COG3840 96 lrpglklTAE-QRAQVEQALE-----------------RVGLAGlldrlpGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 579 SAVDSHVSKMLLDrclnefLSKKIR-------ILVTHRVQLLRHV-DHLVLLEGGRISVQGHYDAL 636
Cdd:COG3840 158 SALDPALRQEMLD------LVDELCrergltvLMVTHDPEDAARIaDRVLLVADGRIAADGPTAAL 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
444-636 |
4.29e-18 |
|
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: 89.19 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDI---ISGSVEVNGV-------------LSYAPQEPW--LLRGSL 505
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRdllelsealrgrrIGMVFQDPMtqLNPVTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 506 RDNILFT-----EPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPL 578
Cdd:COG1123 102 GDQIAEAlenlgLSRAEarARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 579 SAVDSHVSKMLLD--RCLNEFLSKKIrILVTHRV-QLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:COG1123 171 TALDVTTQAEILDllRELQRERGTTV-LLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
446-631 |
4.83e-18 |
|
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: 87.46 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-----------------LSYAPQE----PWLlrgS 504
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYVFQEarlfPHL---S 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 505 LRDNILftepYDEQRYLEVLRVCHLDRDVEQLPLGD--STRVgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:COG4148 94 VRGNLL----YGRKRAPRAERRISFDEVVELLGIGHllDRRP----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 583 sHVSKM----LLDRCLNEFlskKIRIL-VTHRVQ-LLRHVDHLVLLEGGRISVQG 631
Cdd:COG4148 166 -LARKAeilpYLERLRDEL---DIPILyVSHSLDeVARLADHVVLLEQGRVVASG 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1033-1264 |
5.75e-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: 84.93 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1033 NLPKHWPSGGQldfrdlrlrysnhgpyILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQL 1111
Cdd:cd03256 5 NLSKTYPNGKK----------------ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1112 G---LHDLRRRISIIPQDP-----------VLfSGSLR--------FNLDPFEEKtdEELWLALEAVKLKEFVSNLKDgi 1169
Cdd:cd03256 69 KgkaLRQLRRQIGMIFQQFnlierlsvlenVL-SGRLGrrstwrslFGLFPKEEK--QRALAALERVGLLDKAYQRAD-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1170 ncrlhdcgaNFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQE---AIHTKFAHCTVLTIaHRLHTVMDN-D 1245
Cdd:cd03256 144 ---------QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDllkRINREEGITVIVSL-HQVDLAREYaD 213
|
250
....*....|....*....
gi 221460257 1246 RVMVVDMGRVVELGHPHEL 1264
Cdd:cd03256 214 RIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1061-1267 |
6.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.87 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHalfrlaHIN-------GHISIDGFETS--QLGLHDLRRRISIIPQDP--VL 1129
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQ------HLNgllkptsGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1130 FSGSLR----F---NLDPFEEKTDEELWLALEAVKLKefVSNLKDGINCRLhdcganfSMGQRQLVCLARALLRQNKILI 1202
Cdd:PRK13637 97 FEETIEkdiaFgpiNLGLSEEEIENRVKRAMNIVGLD--YEDYKDKSPFEL-------SGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1203 MDEATANVDP----ETDNLIQEaIHTKFaHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK13637 168 LDEPTAGLDPkgrdEILNKIKE-LHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
422-631 |
7.36e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.74 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQKKQEKrhrhieDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSY---APQEp 498
Cdd:COG1118 2 SIEVRNISKRFGSFTLLD------DVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlPPRE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 499 wllRG--------------SLRDNILFTepydeqrylevLRVCHLDRD-----VEQLpLGdstRVGEGG------ASLSG 553
Cdd:COG1118 75 ---RRvgfvfqhyalfphmTVAENIAFG-----------LRVRPPSKAeirarVEEL-LE---LVQLEGladrypSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 554 GQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKML---LDRCLNEFlsKKIRILVTH-RVQLLRHVDHLVLLEGGRISV 629
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELrrwLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQ 214
|
..
gi 221460257 630 QG 631
Cdd:COG1118 215 VG 216
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
90-358 |
8.81e-18 |
|
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: 85.00 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 90 ASIVYSIMAIAVHTTQPLMLGGLVSFFSESTGKITKHSAyLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVY 169
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALN-VYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 170 RKFLRVSVAA-DNSGVsGYAISLMATDLPTFNESFYCFHELWRGPLEGVVFVYIIYQLIGWP-AVVGLGTIVAFIPLQAW 247
Cdd:pfam00664 82 KKILRQPMSFfDTNSV-GELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 248 AARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKSFAKLIGKVRKEEMDSIRGSTYIYAGLQ-CTGMISKLSLF 326
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFgITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 221460257 327 LSL---VTYVFTGDIvTSQKVFIVASYYDHLNDSL 358
Cdd:pfam00664 241 LALwfgAYLVISGEL-SVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
424-627 |
9.36e-18 |
|
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: 83.08 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 424 TVHKLSASwdqkkQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG----------VLSY 493
Cdd:cd03226 1 RIENISFS-----YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 494 APQEP--WLLRGSLRDNILFTE---PYDEQRYLEVLRVCHLDRDVEQLPLgdstrvgeggaSLSGGQKARVSLARAVYRK 568
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLkelDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 569 ADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRVQLL-RHVDHLVLLEGGRI 627
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
444-627 |
9.36e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 83.46 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEpwllRG--------------SLRD 507
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdVTDLPPKD----RDiamvfqnyalyphmTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 508 NILF-----TEPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSA 580
Cdd:cd03301 92 NIAFglklrKVPKDEidERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221460257 581 VDSHVS-KMLLD-RCLNEFLSKKIrILVTH-RVQLLRHVDHLVLLEGGRI 627
Cdd:cd03301 161 LDAKLRvQMRAElKRLQQRLGTTT-IYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
442-638 |
9.87e-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: 84.09 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 442 RHI-EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----LSYAPQEPWLLR-G------------ 503
Cdd:cd03261 13 RTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisgLSEAELYRLRRRmGmlfqsgalfdsl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 504 SLRDNILF--------TEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLD 575
Cdd:cd03261 93 TVFENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 576 DPLSAVDSHVSKMLLD--RCLNEFLSKKIrILVTHRVQ-LLRHVDHLVLLEGGRISVQGHYDALKK 638
Cdd:cd03261 162 EPTAGLDPIASGVIDDliRSLKKELGLTS-IMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
435-632 |
1.08e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.56 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----------------LSYAPQEP 498
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 499 WLLRG-SLRDNILFtepydeqryleVLRVCHLDRD-----VEQLpLgdsTRVGEGG------ASLSGGQKARVSLARAVY 566
Cdd:COG2884 89 RLLPDrTVYENVAL-----------PLRVTGKSRKeirrrVREV-L---DLVGLSDkakalpHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 567 RKADIYLLDDPLSAVDSHVSKMLLdRCLNEFLSKKIRILV-THRVQLLRHVDHLVL-LEGGRISVQGH 632
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIM-ELLEEINRRGTTVLIaTHDLELVDRMPKRVLeLEDGRLVRDEA 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1044-1264 |
1.15e-17 |
|
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: 83.32 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALfrlAHI----NGHISIDGFETSQlGLHDLRRR 1119
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML---TGElrptSGTAYINGYSIRT-DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSG-----SLRFnldpF-------EEKTDEELWLALEAVKLKEFvsnlkdgINCRLHDCganfSMGQRQL 1187
Cdd:cd03263 77 LGYCPQFDALFDEltvreHLRF----YarlkglpKSEIKEEVELLLRVLGLTDK-------ANKRARTL----SGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1188 VCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHtVMDN--DRVMVVDMGRVVELGHPHEL 1264
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMD-EAEAlcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1044-1259 |
1.84e-17 |
|
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: 82.57 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYsnHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHdlRRRISI 1122
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDsGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLF----------SGsLRFNLDPFEEKTDEELWLaLEAVKLKEFVSNLKDGIncrlhdcganfSMGQRQLVCLAR 1192
Cdd:cd03259 77 VFQDYALFphltvaeniaFG-LKLRGVPKAEIRARVREL-LELVGLEGLLNRYPHEL-----------SGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1193 ALLRQNKILIMDEATANVDPET-DNLIQE--AIHTKFaHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELG 1259
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLrEELREElkELQREL-GITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
444-649 |
2.23e-17 |
|
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: 88.46 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLniakiglhdlrfkITIIPQDPVLFSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLL 590
Cdd:TIGR00957 1382 PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 591 DRCLNEFLSKKIrILVTHRVQLLRHVDHLVLLEGGRISvqgHYDALKKLIRFR---MSVAND 649
Cdd:TIGR00957 1462 STIRTQFEDCTV-LTIAHRLNTIMDYTRVIVLDKGEVA---EFGAPSNLLQQRgifYSMAKD 1519
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
422-636 |
2.29e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.47 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQKKqekrhRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG----VLSYA--- 494
Cdd:PRK10790 340 RIDIDNVSFAYRDDN-----LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsSLSHSvlr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 495 ------PQEPWLLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRK 568
Cdd:PRK10790 415 qgvamvQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 569 ADIYLLDDPLSAVDSHvSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:PRK10790 495 PQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1044-1258 |
2.95e-17 |
|
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: 82.15 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGP--YILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDL---- 1116
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQD---------------PVLFSGSLRFNLdpfEEKTDEelwlALEAVKLKE----FVSNLkdgincrlhdcg 1177
Cdd:cd03255 81 RRHIGFVFQSfnllpdltalenvelPLLLAGVPKKER---RERAEE----LLERVGLGDrlnhYPSEL------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1178 anfSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIH--TKFAHCTVLTIAHrlhtvmdnDRVMVVDMGRV 1255
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTH--------DPELAEYADRI 210
|
...
gi 221460257 1256 VEL 1258
Cdd:cd03255 211 IEL 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1044-1281 |
3.04e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.97 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDGfETSQLGLH--------- 1114
Cdd:PRK14267 5 IETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEG-EVRLFGRNiyspdvdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1115 DLRRRISIIPQDPVLF---------SGSLRFN-LDPFEEKTDEELWLALEAVKLKEFVSNlkdgincRLHDCGANFSMGQ 1184
Cdd:PRK14267 82 EVRREVGMVFQYPNPFphltiydnvAIGVKLNgLVKSKKELDERVEWALKKAALWDEVKD-------RLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1185 RQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHR-LHTVMDNDRVMVVDMGRVVELGHPHE 1263
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
250
....*....|....*....
gi 221460257 1264 LLHN-RHGYLHRFVekTGV 1281
Cdd:PRK14267 235 VFENpEHELTEKYV--TGA 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1044-1256 |
4.09e-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: 80.17 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHD-LRRRIS 1121
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDsGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQdpvlfsgslrfnldpfeektdeelwlaleavklkefvsnlkdgincrlhdcganFSMGQRQLVCLARALLRQNKIL 1201
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 1202 IMDEATANVDP-ETDNLIqEAIHT-KFAHCTVLTIAHRLHTVMDN-DRVMVVDMGRVV 1256
Cdd:cd03216 105 ILDEPTAALTPaEVERLF-KVIRRlRAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
444-625 |
5.80e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEV--NGVLSYAPQEPWLLRGSLRDNILF---TEPYDEQ 518
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDA 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 519 RYLEVLRVCHLDRDVEQLplgdsTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFL 598
Cdd:COG4178 459 ELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREEL 532
|
170 180
....*....|....*....|....*..
gi 221460257 599 SKKIRILVTHRVQLLRHVDHLVLLEGG 625
Cdd:COG4178 533 PGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
437-638 |
6.00e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.23 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 437 QEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRG 503
Cdd:PRK11176 352 PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlaslrnqVALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 504 SLRDNILF--TEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAV 581
Cdd:PRK11176 432 TIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 582 DSHvSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQG-HYDALKK 638
Cdd:PRK11176 512 DTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGtHAELLAQ 568
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
423-638 |
8.29e-17 |
|
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: 81.18 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKqekrhrHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----LSYAPQEP 498
Cdd:COG1127 6 IEVRNLTKSFGDRV------VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditgLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 499 WLLR-----------GSL--RDNILFtePYDE----------QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQ 555
Cdd:COG1127 80 LRRRigmlfqggalfDSLtvFENVAF--PLREhtdlseaeirELVLEKLELVGLPGAADKMP-----------SELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 556 KARVSLARAVYRKADIYLLDDPLSAVDShVSKMLLDRCLNEfLSKKIR---ILVTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIRE-LRDELGltsVVVTHDLDSAFAIaDRVAVLADGKIIAEG 224
|
....*..
gi 221460257 632 HYDALKK 638
Cdd:COG1127 225 TPEELLA 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1061-1265 |
8.33e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSS---IVHALFRlaHINGHISIDGFETSQLGLHDLRRRISIIPQDP-VLFSGS--- 1133
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGAtve 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1134 --LRFNLD----PFEE---KTDEelwlALEAVKLKEFVSNLKdgincrlhdcgANFSMGQRQLVCLARALLRQNKILIMD 1204
Cdd:PRK13642 101 ddVAFGMEnqgiPREEmikRVDE----ALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1205 EATANVDPETDNLIQEAIHT---KFaHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEikeKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1044-1267 |
1.02e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 80.56 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYsnhGPY-ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQLGLHDLRRR-I 1120
Cdd:cd03224 1 LEVENLNAGY---GKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRFDGRDITGLPPHERARAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLFSG-SLRFNLD----PFEEKTDEElwlALEAV-----KLKEfvsnlkdgincRLHDCGANFSMGQRQLVCL 1190
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLlgayARRRAKRKA---RLERVyelfpRLKE-----------RRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1191 ARALLRQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
423-626 |
1.09e-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: 78.26 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNgvlsyapqepwllr 502
Cdd:cd03221 1 IELENLSKTYGGKLL------LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 503 gslrdnilftepydeqrylEVLRVCHLdrdvEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:cd03221 61 -------------------STVKIGYF----EQL---------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 583 SHvSKMLLDRCLNEFlsKKIRILVTHRVQLLRHV-DHLVLLEGGR 626
Cdd:cd03221 103 LE-SIEALEEALKEY--PGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
423-627 |
1.68e-16 |
|
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: 80.72 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQK-KQEKRHrhiedVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----------- 490
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKH-----VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 --LSYAPQEPWLLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVGEGGASLSGGQKARVSLARAVYRK 568
Cdd:cd03288 95 srLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 569 ADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIrILVTHRVQLLRHVDHLVLLEGGRI 627
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTV-VTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1060-1269 |
2.01e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDG----FETS----QLGLHDLRRRISIIPQDPVLFS 1131
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrvefFNQNiyerRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1132 GSL---------------RFNLDPFEEKT--DEELWlaleavklkefvsnlkDGINCRLHDCGANFSMGQRQLVCLARAL 1194
Cdd:PRK14258 102 MSVydnvaygvkivgwrpKLEIDDIVESAlkDADLW----------------DEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1195 LRQNKILIMDEATANVDPETDNLIQEAIHTKF--AHCTVLTIAHRLHTVM-----------DNDRVmvvdmGRVVELGHP 1261
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----GQLVEFGLT 240
|
....*...
gi 221460257 1262 HELLHNRH 1269
Cdd:PRK14258 241 KKIFNSPH 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1036-1250 |
2.13e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1036 KHWPSGGQLDFRDLRLRYSNHGPY-ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISI-DGFETSQLG 1112
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIInDSHNLKDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1113 LHDLRRRISIIPQDPVLFSGSLRFNL--------------DPFEEKT--------------------------------- 1145
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsNYYNEDGndsqenknkrnscrakcagdlndmsnttdsnel 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1146 -----------DEELWLALEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPET 1214
Cdd:PTZ00265 535 iemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|....*...
gi 221460257 1215 DNLIQEAIHTKFAHCTVLT--IAHRLHTVMDNDRVMVV 1250
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITiiIAHRLSTIRYANTIFVL 652
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1044-1271 |
2.42e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.69 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYI--LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHIS----IDGFETSQLGLHDLR 1117
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGgsatFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 R----RISIIPQDPVLfsgslrfNLDPF---EEKTDEELWL---------------ALEAVKLKEfvsnLKDGINCRLHD 1175
Cdd:PRK09473 93 KlraeQISMIFQDPMT-------SLNPYmrvGEQLMEVLMLhkgmskaeafeesvrMLDAVKMPE----ARKRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1176 cganFSMGQRQLVCLARALLRQNKILIMDEATANVDPEtdnlIQEAIHT-------KFaHCTVLTIAHRLHTVMDN-DRV 1247
Cdd:PRK09473 162 ----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTllnelkrEF-NTAIIMITHDLGVVAGIcDKV 232
|
250 260
....*....|....*....|....*
gi 221460257 1248 MVVDMGRVVELGHPHELL-HNRHGY 1271
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFyQPSHPY 257
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
432-631 |
2.65e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 432 WDQKKQEKRHRHI-EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSyapqepWLL------RGS 504
Cdd:COG1134 29 LRRRRTRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgagfHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 505 L--RDNILF-------TEPYDEQRYLEVLRVC----HLDrdveqLPLGdstrvgeggaSLSGGQKARVSLARAVYRKADI 571
Cdd:COG1134 103 LtgRENIYLngrllglSRKEIDEKFDEIVEFAelgdFID-----QPVK----------TYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 572 YLLDDPLSAVDSHVSKMLLDRcLNEFLSK-KIRILVTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLAR-IRELRESgRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
433-631 |
2.67e-16 |
|
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: 79.62 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 433 DQKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELD---IISGSVEVNGV----------LSYAPQEPW 499
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQprkpdqfqkcVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 500 LLRG-SLRDNILFTEPYDEQR-----YLEVLRVCHLDRDVEQLPLGDSTRVGeggasLSGGQKARVSLARAVYRKADIYL 573
Cdd:cd03234 92 LLPGlTVRETLTYTAILRLPRkssdaIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 574 LDDPLSAVDSHVSKMLLdrclnEFLSK-----KIRILVTH--RVQLLRHVDHLVLLEGGRISVQG 631
Cdd:cd03234 167 LDEPTSGLDSFTALNLV-----STLSQlarrnRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
435-636 |
2.80e-16 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 80.04 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLL 501
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdpvelrrkIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 -RGSLRDNIL-------FTEPYDEQRYLEVLRVCHLDrdveqlplgDSTRVGEGGASLSGGQKARVSLARAVYRKADIYL 573
Cdd:cd03295 88 pHMTVEENIAlvpkllkWPKEKIRERADELLALVGLD---------PAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 574 LDDPLSAVDSHVSKMLLD--RCLNEFLSKKIrILVTHRVQ-LLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:cd03295 159 MDEPFGALDPITRDQLQEefKRLQQELGKTI-VFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
445-635 |
2.94e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEPWLLRG-SLRDNIL--FTEPYDEQR 519
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 520 YLEVLRVCHLDRDVEQLPLGD-STRVGEGGA--------------------------SLSGGQKARVSLARAVYRKADIY 572
Cdd:COG0488 95 ELEELEAKLAEPDEDLERLAElQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 573 LLDDP-----LSAVdshvskmlldRCLNEFLsKKIR---ILVTHRVQLLRHV-DHLVLLEGGRISV-QGHYDA 635
Cdd:COG0488 175 LLDEPtnhldLESI----------EWLEEFL-KNYPgtvLVVSHDRYFLDRVaTRILELDRGKLTLyPGNYSA 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1044-1265 |
3.52e-16 |
|
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: 79.30 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNhgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVH--ALFrLAHINGHISIDGFETSqlGLHDLRRRIS 1121
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLEtiAGF-IKPDSGKILLNGKDIT--NLPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDPVLFSgslrfNLDPFEektDEELWLALEAVKLKEFVSNLKD-----GINCRLHDCGANFSMGQRQLVCLARALLR 1196
Cdd:cd03299 75 YVPQNYALFP-----HMTVYK---NIAYGLKKRKVDKKEIERKVLEiaemlGIDHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 1197 QNKILIMDEATANVDPET-DNLIQE--AIHTKFAhCTVLTIAHRLHTV-MDNDRVMVVDMGRVVELGHPHELL 1265
Cdd:cd03299 147 NPKILLLDEPFSALDVRTkEKLREElkKIRKEFG-VTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
444-631 |
4.97e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEPWLLRGSLRD--NILF-------- 511
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpLADWSPAELARRRAVLPQhsSLSFpftveevv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 -------TEPYDE-----QRYLEVLRVCHL-DRDVEQlplgdstrvgeggasLSGGQKARVSLARA---VYRKAD---IY 572
Cdd:PRK13548 98 amgraphGLSRAEddalvAAALAQVDLAHLaGRDYPQ---------------LSGGEQQRVQLARVlaqLWEPDGpprWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 573 LLDDPLSAVD----SHVSKMLLDRCLNEFLSKkirILVTHRVQL-LRHVDHLVLLEGGRISVQG 631
Cdd:PRK13548 163 LLDEPTSALDlahqHHVLRLARQLAHERGLAV---IVVLHDLNLaARYADRIVLLHQGRLVADG 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1058-1267 |
5.32e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.75 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1058 PYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHalfrlaHIN-------GHISIDGFETSQLG-LHDLRRRISIIPQDP-- 1127
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAK------HMNallipseGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1128 ----------VLFsGSLRFNLDPFE--EKTDEelwlALEAVKLKEFvsnlkdgincRLHDCGAnFSMGQRQLVCLARALL 1195
Cdd:PRK13633 97 qivativeedVAF-GPENLGIPPEEirERVDE----SLKKVGMYEY----------RRHAPHL-LSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1196 RQNKILIMDEATANVDP----ETDNLIQEaIHTKFaHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPsgrrEVVNTIKE-LNKKY-GITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1043-1229 |
6.33e-16 |
|
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: 77.90 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1043 QLDFRDLRLRYsnHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFR-LAHIN----GHISIDGFETSQLGlHDLR 1117
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRiLAGLLppsaGEVLWNGEPIRDAR-EDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 RRISIIPQDPVLFSG-SLRFNLDpF------EEKTDEELWLALEAVKLKEFvsnlkdgincrLHDCGANFSMGQRQLVCL 1190
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-----------ADLPVRQLSAGQKRRVAL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 221460257 1191 ARALLRQNKILIMDEATANVDPETDNLIQEAIHtkfAHC 1229
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIA---AHL 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
444-631 |
8.04e-16 |
|
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: 78.39 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEpwlLRgSLRDNI--------LFTE 513
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdLTLLSGKE---LR-KARRRIgmifqhfnLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 514 P--YDEQRY-LEVLRV--CHLDRDVEQLP--LGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVS 586
Cdd:cd03258 97 RtvFENVALpLEIAGVpkAEIEERVLELLelVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221460257 587 KMLLDRCLNefLSKKIRI---LVTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:cd03258 177 QSILALLRD--INRELGLtivLITHEMEVVKRIcDRVAVMEKGEVVEEG 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
435-631 |
9.78e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 77.97 E-value: 9.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------------LSYAPQEPWL 500
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 LRG-SLRDNIL-----FTEPYDEQRYL--EVLRVCHLDRDVEQLplgdstrvgegGASLSGGQKARVSLARAVYRKADIY 572
Cdd:cd03218 87 FRKlTVEENILavleiRGLSKKEREEKleELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 573 LLDDPLSAVDShVSKMLLDRCLNEFLSKKIRILVT-HRV-QLLRHVDHLVLLEGGRISVQG 631
Cdd:cd03218 156 LLDEPFAGVDP-IAVQDIQKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEG 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1044-1255 |
9.82e-16 |
|
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: 77.45 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSqlGLHD-----LR 1117
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 RRISIIPQDPVLFSgslrfNLDPFEEktdeeLWLALEAVKLK-----EFVSNLKD--GINCRLHDCGANFSMGQRQLVCL 1190
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVYEN-----VAFALEVTGVPpreirKRVPAALElvGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 1191 ARALLRQNKILIMDEATANVDPETDNLIQ---EAIHTKFAHCTVLTIAHRLHTVMDNdRVMVVDMGRV 1255
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMnllKKINKAGTTVVVATHAKELVDTTRH-RVIALERGKL 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
444-632 |
1.05e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 78.62 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG----------------VLsyaPQ----------- 496
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrraVL---PQhsslafpftve 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 497 -------EPWLLRGSLRDNILftepydeQRYLEVLRVCHL-DRDVEQlplgdstrvgeggasLSGGQKARVSLARA---- 564
Cdd:COG4559 94 evvalgrAPHGSSAAQDRQIV-------REALALVGLAHLaGRSYQT---------------LSGGEQQRVQLARVlaql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 565 ---VYRKADIYLLDDPLSAVD-SHVSKMLldRCLNEFLSKKIRIL-VTHRVQL-LRHVDHLVLLEGGRISVQGH 632
Cdd:COG4559 152 wepVDGGPRWLFLDEPTSALDlAHQHAVL--RLARQLARRGGGVVaVLHDLNLaAQYADRILLLHQGRLVAQGT 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
423-634 |
1.37e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEV--NGVLSYAPQEPWL 500
Cdd:COG0488 316 LELEGLSKSYGDKTL------LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 LRGSLRdnilftePYDE-QRYLEVLRvchlDRDVEQLpLGD--------STRVGeggaSLSGGQKARVSLARAVYRKADI 571
Cdd:COG0488 390 LDPDKT-------VLDElRDGAPGGT----EQEVRGY-LGRflfsgddaFKPVG----VLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 572 YLLDDP---LSaVDshvSKMLLDRCLNEF---LskkirILVTHRVQLL-RHVDHLVLLEGGRISV-QGHYD 634
Cdd:COG0488 454 LLLDEPtnhLD-IE---TLEALEEALDDFpgtV-----LLVSHDRYFLdRVATRILEFEDGGVREyPGGYD 515
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
440-622 |
1.43e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 440 RHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQ---EPWLL------------- 501
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQrseVPDSLpltvrdlvamgrw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 --RGSLRdnilftepydeqrylevlRVCHLDRDVeqlpLGDS-TRVGEGG------ASLSGGQKARVSLARAVYRKADIY 572
Cdd:NF040873 84 arRGLWR------------------RLTRDDRAA----VDDAlERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 573 LLDDPLSAVDSHvSKMLLDRCLNEFLSKKIRIL-VTHRVQLLRHVDHLVLL 622
Cdd:NF040873 142 LLDEPTTGLDAE-SRERIIALLAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1044-1268 |
1.55e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFR-LAHINGHISIDG--FETSQLGLHDLRRRI 1120
Cdd:PRK13636 6 LKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDP--VLFSGSLrfnldpFEEKTDEELWLALEAVKLKEFVSNL--KDGINCRLHDCGANFSMGQRQLVCLARALLR 1196
Cdd:PRK13636 85 GMVFQDPdnQLFSASV------YQDVSFGAVNLKLPEDEVRKRVDNAlkRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1197 QNKILIMDEATANVDPETDNLIQEAIHT--KFAHCTVLTIAHRLHTV-MDNDRVMVVDMGRVVELGHPHELLHNR 1268
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
423-583 |
2.49e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.59 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAP------- 495
Cdd:COG4525 4 LTVRHVSVRYPGGGQ--PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPgadrgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 496 -QE----PWLlrgSLRDNILF-------TEPYDEQRYLEVLRVCHLDrDVEQLPLgdstrvgeggASLSGGQKARVSLAR 563
Cdd:COG4525 82 fQKdallPWL---NVLDNVAFglrlrgvPKAERRARAEELLALVGLA-DFARRRI----------WQLSGGMRQRVGIAR 147
|
170 180
....*....|....*....|
gi 221460257 564 AVYRKADIYLLDDPLSAVDS 583
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDA 167
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1061-1264 |
2.53e-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: 76.64 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-------AHINGHisiDGFETSQlglhDLRRRISIIPQDPVLFSG- 1132
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlkptsgrATVAGH---DVVREPR----EVRRRIGIVFQDLSVDDEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1133 SLRFNL-----------DPFEEKTDEelwlALEAVKLKEFvsnlKDGINCrlhdcgaNFSMGQRQLVCLARALLRQNKIL 1201
Cdd:cd03265 89 TGWENLyiharlygvpgAERRERIDE----LLDFVGLLEA----ADRLVK-------TYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1202 IMDEATANVDPETDNLIQEAIHT---KFAhCTVLTIAHrlhtVMDN-----DRVMVVDMGRVVELGHPHEL 1264
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKlkeEFG-MTILLTTH----YMEEaeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1061-1269 |
2.79e-15 |
|
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: 76.71 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahIN-------GHISIDGFETSQLGLHDLRRR--------ISIIPQ 1125
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTT----LFNL--ISgflrptsGSVLFDGEDITGLPPHEIARLgigrtfqiPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1126 DPVL--------FSGSLRFNLDPF---EEKTDEELWLALEAVKLKEfvsnlkdgincRLHDCGANFSMGQRQLVCLARAL 1194
Cdd:cd03219 90 LTVLenvmvaaqARTGSGLLLARArreEREARERAEELLERVGLAD-----------LADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1195 LRQNKILIMDEATANVDP-ETDNLIQEAIHTKFAHCTVLTIAHRLHTVMDN-DRVMVVDMGRVVELGHPHELLHNRH 1269
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1044-1270 |
3.44e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGfETSQLGLHDLRRRISI 1122
Cdd:PRK13537 8 IDFRNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCG-EPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQ----DPVLfsgSLRFNLDPFEEktdeelWLALEAVKLKEFV------SNLKDGINCRLHDcganFSMGQRQLVCLAR 1192
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGR------YFGLSAAAARALVppllefAKLENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1193 ALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHC-TVLTIAHrlhtVMDN-----DRVMVVDMGRVVELGHPHELLH 1266
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTH----FMEEaerlcDRLCVIEEGRKIAEGAPHALIE 227
|
....
gi 221460257 1267 NRHG 1270
Cdd:PRK13537 228 SEIG 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
444-631 |
4.42e-15 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 75.93 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------------LSYAPQEPWLLRG-SLRDN 508
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 509 ILFTEpydeqrylEVLRVCHLDRDVEQL----P-LGDstRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDP---LS- 579
Cdd:cd03224 96 LLLGA--------YARRRAKRKARLERVyelfPrLKE--RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAp 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 580 AVDSHVSKMLldrclneflsKKIR------ILVTHRVQL-LRHVDHLVLLEGGRISVQG 631
Cdd:cd03224 166 KIVEEIFEAI----------RELRdegvtiLLVEQNARFaLEIADRAYVLERGRVVLEG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1044-1259 |
5.45e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRgEEKI-GIVGHTAAGKSSIVHALFRL------AHINGHISIDGFE--TSQLGLH 1114
Cdd:COG1117 12 IEVRNLNVYYGDK--QALKDINLDIP-ENKVtALIGPSGCGKSTLLRCLNRMndlipgARVEGEILLDGEDiyDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1115 DLRRRISIIPQDPVLFSGS--------LRFNLDPFEEKTDEELWLALEAVKLKEFVsnlKDgincRLHDCGANFSMGQRQ 1186
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALWDEV---KD----RLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 1187 LVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRlhtvMD-----NDRVMVVDMGRVVELG 1259
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELVEFG 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
446-635 |
6.02e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.15 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVL----------------SYApQEPWLlrgSLRDNI 509
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaergvgmvfqSYA-LYPHL---SVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 510 LF-------TEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:PRK11000 97 SFglklagaKKEEINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 583 S--------HVSKmlldrclnefLSKKIR---ILVTH-RVQLLRHVDHLVLLEGGRISVQG------HYDA 635
Cdd:PRK11000 166 AalrvqmriEISR----------LHKRLGrtmIYVTHdQVEAMTLADKIVVLDAGRVAQVGkplelyHYPA 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
422-627 |
6.05e-15 |
|
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: 75.84 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSaswdqkKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEpw 499
Cdd:cd03296 2 SIEVRNVS------KRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 500 llRG--------------SLRDNILF---------TEPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGG 554
Cdd:cd03296 74 --RNvgfvfqhyalfrhmTVFDNVAFglrvkprseRPPEAEirAKVHELLKLVQLDWLADRYP-----------AQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 555 QKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMlLDRCLNEfLSKKIRI---LVTH-RVQLLRHVDHLVLLEGGRI 627
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRKE-LRRWLRR-LHDELHVttvFVTHdQEEALEVADRVVVMNKGRI 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1044-1269 |
6.26e-15 |
|
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: 75.80 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYsNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-AHINGHISIDGFETSQLGLHDLRRRISI 1122
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLFSG-SLRFN--LDPFEEKTDEElwlaleavKLKEFVSNLkdgincrLHDCG---ANF--------SMGQRQLV 1188
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKWPKE--------KIRERADEL-------LALVGldpAEFadryphelSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1189 CLARALLRQNKILIMDEATANVDPET-DNLIQEAIHTKFA-HCTVLTIAHRlhtvMDN-----DRVMVVDMGRVVELGHP 1261
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITrDQLQEEFKRLQQElGKTIVFVTHD----IDEafrlaDRIAIMKNGEIVQVGTP 220
|
....*...
gi 221460257 1262 HELLHNRH 1269
Cdd:cd03295 221 DEILRSPA 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1047-1259 |
7.13e-15 |
|
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: 75.10 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1047 RDLRLRYSNHGPYI--LKGLTFTIRGEEKIGIVGHTAAGKSS---IVHALFRLAhiNGHISIDGFETSQLGLhDLRRRIS 1121
Cdd:cd03266 5 DALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTtlrMLAGLLEPD--AGFATVDGFDVVKEPA-EARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDPVLFSG-SLRFNLDPFEektdeelwlALEAVKLKEFVSNLKD-----GINCRLHDCGANFSMGQRQLVCLARALL 1195
Cdd:cd03266 82 FVSDSTGLYDRlTARENLEYFA---------GLYGLKGDELTARLEEladrlGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1196 RQNKILIMDEATANVDPETDNLIQEAI-HTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELG 1259
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIrQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1059-1259 |
7.74e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1059 YILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDGFETSQLG---LHDLRRRISIIPQDPvlfSGSL- 1134
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1135 -RFN-LDPFEE------------KTDEELWLALEAVKLKEFVSnlkdgincrlHDCGANFSMGQRQLVCLARALLRQNKI 1200
Cdd:PRK15134 377 pRLNvLQIIEEglrvhqptlsaaQREQQVIAVMEEVGLDPETR----------HRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1201 LIMDEATANVDPETDNLIQEAIHT-----KFAHctvLTIAHRLHTVMD-NDRVMVVDMGRVVELG 1259
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSlqqkhQLAY---LFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1044-1265 |
8.38e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 75.18 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYsnhGPYILKgLTFTIRGEEKIGIVGHTAAGKSSIVHAL--FrLAHINGHISIDGfeTSQLGLHDLRRRIS 1121
Cdd:COG3840 2 LRLDDLTYRY---GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIagF-LPPDSGRILWNG--QDLTALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDPVLFS----------G---SLRfnLDPFEEKTDEElwlALEAVKLKEFVSnlkdgincRLhdCGAnFSMGQRQLV 1188
Cdd:COG3840 75 MLFQENNLFPhltvaqniglGlrpGLK--LTAEQRAQVEQ---ALERVGLAGLLD--------RL--PGQ-LSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1189 CLARALLRQNKILIMDEATANVDP----ETDNLIQEaIHTKFaHCTVLTIAHRLHTVMDN-DRVMVVDMGRVVELGHPHE 1263
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDE-LCRER-GLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAA 216
|
..
gi 221460257 1264 LL 1265
Cdd:COG3840 217 LL 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
444-622 |
1.82e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------LSYAPQEPWLLRGSLRDNIL 510
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FtePY-------DEQRYLevlrvchldRDVEQLPLGDSTrVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDS 583
Cdd:PRK10247 103 F--PWqirnqqpDPAIFL---------DDLERFALPDTI-LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 584 HvSKmlldRCLNEFL-----SKKIRIL-VTHRVQLLRHVDHLVLL 622
Cdd:PRK10247 171 S-NK----HNVNEIIhryvrEQNIAVLwVTHDKDEINHADKVITL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
443-582 |
1.82e-14 |
|
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: 74.29 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 443 HIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-----------LSYAPQEPWLL-RGSLRDNIL 510
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 511 F-------TEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:cd03299 94 YglkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
435-631 |
1.87e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.85 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG---------VLSYAPQEpwllRGSL 505
Cdd:cd03269 7 TKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEE----RGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 506 RDnilfTEPYDEQRYLEVLR-------VCHLDRDVEQLPLGD--STRVGEggasLSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:cd03269 83 PK----MKVIDQLVYLAQLKglkkeeaRRRIDEWLERLELSEyaNKRVEE----LSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 577 PLSAVDShVSKMLLDRCLNEFLSK-KIRILVTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:cd03269 155 PFSGLDP-VNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
422-631 |
2.53e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQKkqekrhRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG------------ 489
Cdd:PRK11231 2 TLRTENLTVGYGTK------RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 490 -VLSYAPQE------------------PWL-LRGSLRDNilftepyDEQRYLEVLRVCHLDRDVEQlPLGDstrvgegga 549
Cdd:PRK11231 76 rRLALLPQHhltpegitvrelvaygrsPWLsLWGRLSAE-------DNARVNQAMEQTRINHLADR-RLTD--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 550 sLSGGQKARVSLARAVYRKADIYLLDDPLSAVD-SH-VSKMLLDRCLNEflSKKIRILVTHRV-QLLRHVDHLVLLEGGR 626
Cdd:PRK11231 139 -LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHqVELMRLMRELNT--QGKTVVTVLHDLnQASRYCDHLVVLANGH 215
|
....*
gi 221460257 627 ISVQG 631
Cdd:PRK11231 216 VMAQG 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
423-631 |
3.98e-14 |
|
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: 72.61 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekrhrhIEDVSFQAQDQQFvGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------ 490
Cdd:cd03264 1 LQLENLTKRYGKKRA------LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 LSYAPQEPwllrgSLRDNilFTEpYDEQRYLEVLRVCH-------LDRDVEQLPLGD--STRVGeggaSLSGGQKARVSL 561
Cdd:cd03264 74 IGYLPQEF-----GVYPN--FTV-REFLDYIAWLKGIPskevkarVDEVLELVNLGDraKKKIG----SLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 562 ARAVYRKADIYLLDDPLSAVDShVSKMLLDRCLNEFLSKKIRILVTHRVQ-LLRHVDHLVLLEGGRISVQG 631
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1044-1271 |
4.02e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.13 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHG--------PYILK---GLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGFETSQL 1111
Cdd:PRK15079 9 LEVADLKVHFDIKDgkqwfwqpPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAtDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1112 G---LHDLRRRISIIPQDPvLFSGSLRFNL-----DPFE----EKTDEELWLALEAVKLKefVSNLKDGINCRLHDcgan 1179
Cdd:PRK15079 89 KddeWRAVRSDIQMIFQDP-LASLNPRMTIgeiiaEPLRtyhpKLSRQEVKDRVKAMMLK--VGLLPNLINRYPHE---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1180 FSMGQRQLVCLARALLRQNKILIMDEATANVD----PETDNLIQEAihTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGR 1254
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQL--QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGH 239
|
250
....*....|....*...
gi 221460257 1255 VVELGHPHELLHN-RHGY 1271
Cdd:PRK15079 240 AVELGTYDEVYHNpLHPY 257
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
444-631 |
4.33e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEPWLLRGSLRDNILFTEPYDEQRYL 521
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddVEALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 522 EVLRVCHL----------DRDVEQ-LPLGDSTR-VGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSH--VSK 587
Cdd:PRK09536 99 EMGRTPHRsrfdtwtetdRAAVERaMERTGVAQfADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhqVRT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 588 MLLDRCLNEflSKKIRILVTHRVQL-LRHVDHLVLLEGGRISVQG 631
Cdd:PRK09536 179 LELVRRLVD--DGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1041-1259 |
4.62e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 72.20 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1041 GGQLDFRDLRL----RYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAL---FRLAHINGHISIDGFetsQLGL 1113
Cdd:cd03213 1 GVTLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEVLINGR---PLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1114 HDLRRRISIIPQDPVLFSgslrfNLDPFEektdeelwlALeavklkEFVSNLKdGIncrlhdcganfSMGQRQLVCLARA 1193
Cdd:cd03213 78 RSFRKIIGYVPQDDILHP-----TLTVRE---------TL------MFAAKLR-GL-----------SGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1194 LLRQNKILIMDEATANVDPETDNLIQEAIhTKFA--HCTVLTIAHRLHTVMDN--DRVMVVDMGRVVELG 1259
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLL-RRLAdtGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1061-1271 |
5.18e-14 |
|
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: 76.65 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDGFETSQLG---LHDLRRRISIIPQDPvlFsGSL--R 1135
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLspR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1136 FN---------------LDPfeEKTDEELWLALEAVKLKEfvsnlkdgiNCRL---HDcganFSMGQRQLVCLARALLRQ 1197
Cdd:COG4172 379 MTvgqiiaeglrvhgpgLSA--AERRARVAEALEEVGLDP---------AARHrypHE----FSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1198 NKILIMDEATANVdpetDNLIQEAIHTKFA------HCTVLTIAHRLHTV--MdNDRVMVVDMGRVVELGHPHELLHN-R 1268
Cdd:COG4172 444 PKLLVLDEPTSAL----DVSVQAQILDLLRdlqrehGLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDApQ 518
|
...
gi 221460257 1269 HGY 1271
Cdd:COG4172 519 HPY 521
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1055-1222 |
6.43e-14 |
|
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: 71.90 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1055 NHGPYILKGLTFTIRGEEKIGIVGHTAAGKSS---IVHALFRLAHinGHISIDGfetSQLGLHDLRRRISIIPQDP--VL 1129
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTlakILAGLIKESS--GSILLNG---KPIKAKERRKSIGYVMQDVdyQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1130 FSGSLRFNLDPFEEKTDEELWLAlEAVkLKEF-VSNLKDgincRL-HDCganfSMGQRQLVCLARALLRQNKILIMDEAT 1207
Cdd:cd03226 85 FTDSVREELLLGLKELDAGNEQA-ETV-LKDLdLYALKE----RHpLSL----SGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170
....*....|....*
gi 221460257 1208 ANVDPETDNLIQEAI 1222
Cdd:cd03226 155 SGLDYKNMERVGELI 169
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1044-1265 |
6.52e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSnhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFrlahinGHISIDGFETSQLGL------HDLR 1117
Cdd:PRK13536 42 IDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL------GMTSPDAGKITVLGVpvparaRLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 RRISIIPQ-DPVLFSGSLRFNL----DPFEEKTDEelwlaLEAV--KLKEFvSNLKDGINCRLhdcgANFSMGQRQLVCL 1190
Cdd:PRK13536 114 ARIGVVPQfDNLDLEFTVRENLlvfgRYFGMSTRE-----IEAVipSLLEF-ARLESKADARV----SDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1191 ARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHC-TVLTIAHrlhtVMDN-----DRVMVVDMGRVVELGHPHEL 1264
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTH----FMEEaerlcDRLCVLEAGRKIAEGRPHAL 259
|
.
gi 221460257 1265 L 1265
Cdd:PRK13536 260 I 260
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1061-1265 |
7.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.48 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLG-LHDLRRRISIIPQDP-VLFSG----- 1132
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQFVGrtvee 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1133 SLRFN-----LDPFEEKtdEELWLALEAVKLKEFvsnlkdgincrLHDCGANFSMGQRQLVCLARALLRQNKILIMDEAT 1207
Cdd:PRK13644 98 DLAFGpenlcLPPIEIR--KRVDRALAEIGLEKY-----------RHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1208 ANVDPETDNLIQEAI---HTKFAhcTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK13644 165 SMLDPDSGIAVLERIkklHEKGK--TIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1046-1237 |
1.16e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 70.26 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHGPyILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFR-LAHI----NGHISIDGfetsqlglhdlRRRI 1120
Cdd:cd03223 3 LENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSS----LFRaLAGLwpwgSGRIGMPE-----------GEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLFSGSLRfnldpfeektdEELWLALEAVklkefvsnlkdgincrlhdcganFSMGQRQLVCLARALLRQNKI 1200
Cdd:cd03223 67 LFLPQRPYLPLGTLR-----------EQLIYPWDDV-----------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 221460257 1201 LIMDEATANVDPETDNLIQEAIHTKFAhcTVLTIAHR 1237
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1044-1267 |
1.21e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.91 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL----AHINGHISIDGFETSQLGLHDLRRR 1119
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDP-VLFSGSlrfnldpfeeKTDEELWLALE--AVKLKEFVSNLKDGINcrlhDCG---------ANFSMGQRQL 1187
Cdd:PRK13640 86 VGIVFQNPdNQFVGA----------TVGDDVAFGLEnrAVPRPEMIKIVRDVLA----DVGmldyidsepANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1188 VCLARALLRQNKILIMDEATANVDPETDNLIQEAIH--TKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
..
gi 221460257 1266 HN 1267
Cdd:PRK13640 232 SK 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
423-631 |
1.44e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.57 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEkrHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVI--LGELDiiSGSVEVNGV----LSyaPQ 496
Cdd:COG1135 2 IELENLSKTFPTKGGP--VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInlLERPT--SGSVLVDGVdltaLS--ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 497 EpwlLRGsLR-------------------DNILFtePydeqryLEVLRVCHLDRD--VEQLpLgdsTRVGEGG------A 549
Cdd:COG1135 76 E---LRA-ARrkigmifqhfnllssrtvaENVAL--P------LEIAGVPKAEIRkrVAEL-L---ELVGLSDkadaypS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 550 SLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrclnefLSKKIR-------ILVTHRVQLLRHV-DHLVL 621
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILD------LLKDINrelgltiVLITHEMDVVRRIcDRVAV 213
|
250
....*....|
gi 221460257 622 LEGGRISVQG 631
Cdd:COG1135 214 LENGRIVEQG 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1044-1267 |
1.97e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPyiLKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDG--------FETSQLGLHD 1115
Cdd:PRK14239 6 LQVSDLSVYYNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGsivynghnIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1116 LRRRISIIPQDPVLFSGS--------LRFNLDPFEEKTDEELWLALEAVKLKEFVsnlKDgincRLHDCGANFSMGQRQL 1187
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEV---KD----RLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1188 VCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLH 1266
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFM 236
|
.
gi 221460257 1267 N 1267
Cdd:PRK14239 237 N 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
423-631 |
1.99e-13 |
|
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: 70.86 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKqeKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQEPWLL 501
Cdd:cd03266 2 ITADALTKRFRDVK--KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 RGSLRDNilfTEPYDEQRYLEVL----RVCHLDRD---------VEQLPLGD--STRVGEggasLSGGQKARVSLARAVY 566
Cdd:cd03266 80 LGFVSDS---TGLYDRLTARENLeyfaGLYGLKGDeltarleelADRLGMEEllDRRVGG----FSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 567 RKADIYLLDDPLSAVDSHVSKMLLD--RCLNEfLSKKIrILVTHRVQ-LLRHVDHLVLLEGGRISVQG 631
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREfiRQLRA-LGKCI-LFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
455-627 |
2.48e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 455 QFVGIVGTVGAGKSTLLQVILGeLDIISGSVEVNGV--LSYAPQE-----------PWL---------LRGSLRDNILft 512
Cdd:PRK11247 39 QFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTapLAEAREDtrlmfqdarllPWKkvidnvglgLKGQWRDAAL-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 513 epydeqRYLEVLrvchldrdveqlplGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDShvskmlLDR 592
Cdd:PRK11247 116 ------QALAAV--------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA------LTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 221460257 593 C----LNEFLSKK---IRILVTHRV-QLLRHVDHLVLLEGGRI 627
Cdd:PRK11247 170 IemqdLIESLWQQhgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1044-1257 |
2.56e-13 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 70.58 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPY--ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFEtsqlgLHDLRRRI 1120
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDPVLF---------SGSLRFNLDPFEEKTD--EELwlaLEAVKLKEFvsnlkdgincrlhdcgANF-----SMGQ 1184
Cdd:cd03293 76 GYVFQQDALLpwltvldnvALGLELQGVPKAEAREraEEL---LELVGLSGF----------------ENAyphqlSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1185 RQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAI-----HTKFahcTVLTIAHRLH-TVMDNDRVMVVDM--GRVV 1256
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVLSArpGRIV 213
|
.
gi 221460257 1257 E 1257
Cdd:cd03293 214 A 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1044-1265 |
2.63e-13 |
|
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: 71.27 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI--NGHISIDGFETSQLGLHDLRRRIS 1121
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtyGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 II---------PQDPVL------FSGSLrfnlDPFEEKTDEELWLALEAvkLKEF-VSNLKDginCRLHDCganfSMGQR 1185
Cdd:COG1119 82 LVspalqlrfpRDETVLdvvlsgFFDSI----GLYREPTDEQRERAREL--LELLgLAHLAD---RPFGTL----SQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1186 QLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHtKFAH---CTVLTIAHRLHTVMDN-DRVMVVDMGRVVELGHP 1261
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLD-KLAAegaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227
|
....
gi 221460257 1262 HELL 1265
Cdd:COG1119 228 EEVL 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1044-1267 |
2.74e-13 |
|
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: 71.22 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSnhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahINGH-------ISIDGFETSQLGLHDL 1116
Cdd:COG0411 5 LEVRGLTKRFG--GLVAVDDVSLEVERGEIVGLIGPNGAGKTT----LFNL--ITGFyrptsgrILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRR--------ISIIPQDPVL---------------FSGSLRFNLDPFEEK-TDEELWLALEAVKLKEfvsnlkdgincR 1172
Cdd:COG0411 77 ARLgiartfqnPRLFPELTVLenvlvaaharlgrglLAALLRLPRARREEReARERAEELLERVGLAD-----------R 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1173 LHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDP-ETDNLIQ--EAIHTKFAhCTVLTIAHRLHTVMDN-DRVM 1248
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPeETEELAEliRRLRDERG-ITILLIEHDMDLVMGLaDRIV 224
|
250
....*....|....*....
gi 221460257 1249 VVDMGRVVELGHPHELLHN 1267
Cdd:COG0411 225 VLDFGRVIAEGTPAEVRAD 243
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
444-624 |
2.98e-13 |
|
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: 74.40 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQvILGELDIISG---SVEVNGVLSYAPQEPWLLRGSLRDNILFTEP------ 514
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSsedmkr 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 515 --YDEQRYLEVLRVCHLDRDVEQlplgdstrvgEGGAS--------LSGGQKARVSLARAVYRKADIYLLDDPLSAVDSH 584
Cdd:TIGR00954 547 rgLSDKDLEQILDNVQLTHILER----------EGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 221460257 585 VSKMLLDRClneflsKKIRIL---VTHRVQLLRHVDHLVLLEG 624
Cdd:TIGR00954 617 VEGYMYRLC------REFGITlfsVSHRKSLWKYHEYLLYMDG 653
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
445-627 |
2.99e-13 |
|
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: 70.25 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLrgsLRDNI--LFtepydeQRY-- 520
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINE---LRQKVgmVF------QQFnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 ---LEVL--------RVCHLDRD-VEQLPLGDSTRVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:cd03262 88 fphLTVLenitlapiKVKGMSKAeAEERALELLEKVGLADkadaypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221460257 583 SHVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHV-DHLVLLEGGRI 627
Cdd:cd03262 168 PELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
444-630 |
3.37e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.44 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEpwllRG--------------SLRD 507
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdVTGLPPEK----RNvgmvfqdyalfphlTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 508 NILF-------TEPYDEQRYLEVLRVCHL----DRDVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:COG3842 97 NVAFglrmrgvPKAEIRARVAELLELVGLeglaDRYPHQL---------------SGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 577 PLSAvdshvskmlLDRCLNEFLSKKIR----------ILVTHRvQL--LRHVDHLVLLEGGRIsVQ 630
Cdd:COG3842 162 PLSA---------LDAKLREEMREELRrlqrelgitfIYVTHD-QEeaLALADRIAVMNDGRI-EQ 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
444-624 |
3.82e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.72 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSV---EVNGVLsYAPQEPWLLRGSLRDNILFtePYDEQry 520
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmpEGEDLL-FLPQRPYLPLGTLREQLIY--PWDDV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 levlrvchldrdveqlplgdstrvgeggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDshvsKMLLDRCLNEFLSK 600
Cdd:cd03223 92 ------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLYQLLKEL 137
|
170 180
....*....|....*....|....*
gi 221460257 601 KIRIL-VTHRVQLLRHVDHLVLLEG 624
Cdd:cd03223 138 GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1039-1257 |
4.21e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 70.89 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1039 PSGGQLDFRDLRLRY-SNHGPY-ILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLA-----HINGHISIDGFETSQL 1111
Cdd:COG1116 3 AAAPALELRGVSKRFpTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIaglekPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1112 GlhdlrRRISIIPQDPVLF-----SGSLRFNLD----PFEEKTD--EELwlaLEAVKLKEFV----SNLkdgincrlhdc 1176
Cdd:COG1116 79 G-----PDRGVVFQEPALLpwltvLDNVALGLElrgvPKAERREraREL---LELVGLAGFEdaypHQL----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1177 ganfSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQE---AIHTKFaHCTVLTIAH------RLhtvmdNDRV 1247
Cdd:COG1116 140 ----SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDellRLWQET-GKTVLFVTHdvdeavFL-----ADRV 209
|
250
....*....|....
gi 221460257 1248 MVvdM----GRVVE 1257
Cdd:COG1116 210 VV--LsarpGRIVE 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
427-636 |
4.84e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 427 KLSASwDQKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVN-----------GVLSYAP 495
Cdd:PRK10619 5 KLNVI-DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkdGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 496 QEPW-LLRGSLrdNILFtEPYDEQRYLEVLRVChLDRDVEQLPLGDS----------TRVGEGGAS-------LSGGQKA 557
Cdd:PRK10619 84 KNQLrLLRTRL--TMVF-QHFNLWSHMTVLENV-MEAPIQVLGLSKQeareravkylAKVGIDERAqgkypvhLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 558 RVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLdRCLNEFLSK-KIRILVTHRVQLLRHV-DHLVLLEGGRISVQGHYDA 635
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVL-RIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQ 238
|
.
gi 221460257 636 L 636
Cdd:PRK10619 239 L 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1047-1297 |
5.18e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1047 RDLRLRYSNhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIvhalfrLAHIN-------GHISIDGFETSQLGLHDLRRR 1119
Cdd:PRK13647 8 EDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTL------LLHLNgiylpqrGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDP--VLFSGS-----------LRFNLDPFEEKTDEelwlALEAVKLKEFVsnlkdgincrlHDCGANFSMGQRQ 1186
Cdd:PRK13647 81 VGLVFQDPddQVFSSTvwddvafgpvnMGLDKDEVERRVEE----ALKAVRMWDFR-----------DKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1187 LVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIA-HRLHTVMD-NDRVMVVDMGRVVELGHPhEL 1264
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDK-SL 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 221460257 1265 LHNRhgylhRFVEKTGVG---TAQHLRHLAEQSYRK 1297
Cdd:PRK13647 225 LTDE-----DIVEQAGLRlplVAQIFEDLPELGQSK 255
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
444-631 |
5.61e-13 |
|
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: 70.11 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISG-SVEV--------N--------GVLSYAPQEPWLLRGSLR 506
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrggeDvwelrkriGLVSPALQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 507 DNIL---------FTEPYDEQR-----YLEVLRVCHL-DRdveqlPLGdstrvgeggaSLSGGQKARVSLARAVYRKADI 571
Cdd:COG1119 99 DVVLsgffdsiglYREPTDEQRerareLLELLGLAHLaDR-----PFG----------TLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 572 YLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIR--ILVTHRVQ-LLRHVDHLVLLEGGRISVQG 631
Cdd:COG1119 164 LILDEPTAGLDLGARELLLAL-LDKLAAEGAPtlVLVTHHVEeIPPGITHVLLLKDGRVVAAG 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1061-1294 |
8.15e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.99 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLG---LHDLRRR--------ISIIPQDPV 1128
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1129 LFSGSLRFNLD--PFEEKTDEELwLALEAVKLKEFVSNLKDgincrlhdcgaNFSMGQRQLVCLARALLRQNKILIMDEA 1206
Cdd:PRK10070 124 LDNTAFGMELAgiNAEERREKAL-DALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1207 TANVDPETDNLIQ-EAIHTKFAHC-TVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN-RHGYLHRFVEKTGVG 1282
Cdd:PRK10070 192 FSALDPLIRTEMQdELVKLQAKHQrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNpANDYVRTFFRGVDIS 271
|
250
....*....|..
gi 221460257 1283 TAQHLRHLAEQS 1294
Cdd:PRK10070 272 QVFSAKDIARRT 283
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
446-630 |
8.32e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 70.37 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEPWLLRG----------------SLRD 507
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdIAAMSRKELRELRRkkismvfqsfallphrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 508 NILFTepydeqryLEVLRVCHLDRD---VEQLplgdsTRVGEGGAS------LSGGQKARVSLARAVYRKADIYLLDDPL 578
Cdd:cd03294 122 NVAFG--------LEVQGVPRAEREeraAEAL-----ELVGLEGWEhkypdeLSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 579 SAVDSHVSKMLLDRCLNefLSKKIR---ILVTHRV-QLLRHVDHLVLLEGGRIsVQ 630
Cdd:cd03294 189 SALDPLIRREMQDELLR--LQAELQktiVFITHDLdEALRLGDRIAIMKDGRL-VQ 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1044-1257 |
9.82e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.92 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYS--NHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLG---LHDLR 1117
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTsGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 RR-ISIIPQDpvlfsgslrFNLDPF---------------------EEKTDEelwlALEAVKLKEfvsnlkdgincRLHD 1175
Cdd:COG1136 85 RRhIGFVFQF---------FNLLPEltalenvalplllagvsrkerRERARE----LLERVGLGD-----------RLDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1176 CGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETD----NLIQEAIHTKfaHCTVLTIAHRLHTVMDNDRVMVVD 1251
Cdd:COG1136 141 RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHDPELAARADRVIRLR 218
|
....*.
gi 221460257 1252 MGRVVE 1257
Cdd:COG1136 219 DGRIVS 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
444-636 |
1.24e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV------------LSYAPQEPWL-LRGSLRDNIL 510
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDNLdLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 FTEPYDEQRYLEVLRVCHLDRDVEQLPLGDSTRVgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLL 590
Cdd:PRK13536 137 VFGRYFGMSTREIEAVIPSLLEFARLESKADARV----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221460257 591 DRcLNEFLSK-KIRILVTHRVQLL-RHVDHLVLLEGGRISVQGHYDAL 636
Cdd:PRK13536 213 ER-LRSLLARgKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1057-1276 |
1.27e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1057 GPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLA------HINGHISIDGFET-SQLGLHDLRRRISIIPQDPvl 1129
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgyRYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRP-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1130 fsgslrfnlDPFEEKTDEELWLALEAVKL---KEFVS---------NLKDGINCRLHDCGANFSMGQRQLVCLARALLRQ 1197
Cdd:PRK14271 111 ---------NPFPMSIMDNVLAGVRAHKLvprKEFRGvaqarltevGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1198 NKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRL-HTVMDNDRVMVVDMGRVVELGHPHELLHN-RHGYLHRF 1275
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSpKHAETARY 261
|
.
gi 221460257 1276 V 1276
Cdd:PRK14271 262 V 262
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
444-627 |
1.35e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAP------------QEPwlLRG-----SL 505
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPeykrakyigrvfQDP--MMGtapsmTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 506 RDNILFTEPYDEQRYLeVLRVCHLDRD-----VEQLPLG--D--STRVGeggaSLSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:COG1101 100 EENLALAYRRGKRRGL-RRGLTKKRRElfrelLATLGLGleNrlDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 577 PLSAVDSHVSKMLLDrclnefLSKKI-------RILVTHRV-QLLRHVDHLVLLEGGRI 627
Cdd:COG1101 175 HTAALDPKTAALVLE------LTEKIveennltTLMVTHNMeQALDYGNRLIMMHEGRI 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
435-637 |
1.42e-12 |
|
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: 68.30 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRH-IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG------------VLSYAPQepwll 501
Cdd:cd03263 8 KTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 rgslrDNILFTE--PYDEQRYLEVLR-VCHLDRDVE------QLPLGDS--TRVGEggasLSGGQKARVSLARAVYRKAD 570
Cdd:cd03263 83 -----FDALFDEltVREHLRFYARLKgLPKSEIKEEvelllrVLGLTDKanKRART----LSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 571 IYLLDDPLSAVDsHVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHV-DHLVLLEGGRISVQGHYDALK 637
Cdd:cd03263 154 VLLLDEPTSGLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQELK 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
435-631 |
1.51e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------------LSYAPQEPWL 500
Cdd:COG1137 10 VKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 LRG-SLRDNIL----FTEPYDEQRY------LEVLRVCHLdRDVEqlplgdstrvgegGASLSGGQKARVSLARAVYRKA 569
Cdd:COG1137 90 FRKlTVEDNILavleLRKLSKKEREerleelLEEFGITHL-RKSK-------------AYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 570 DIYLLDDPLSAVD----SHVSKMLLDrclnefLSKK-IRILVT-HRVQ-LLRHVDHLVLLEGGRISVQG 631
Cdd:COG1137 156 KFILLDEPFAGVDpiavADIQKIIRH------LKERgIGVLITdHNVReTLGICDRAYIISEGKVLAEG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1065-1285 |
1.56e-12 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 69.21 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1065 TFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLG---LHDLRR-RISII-------PQDPVLFSG 1132
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTsGKVLIDGQDIAAMSrkeLRELRRkKISMVfqsfallPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1133 SLRFNLDPFEEKTDEELWL-ALEAVKLKEFVSNLKDgincrlhdcgaNFSMGQRQLVCLARALLRQNKILIMDEATANVD 1211
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1212 PETDNLIQE---AIHTKFaHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN-RHGYLHRFVEktGVGTAQ 1285
Cdd:cd03294 193 PLIRREMQDellRLQAEL-QKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR--GVDRAK 268
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1044-1268 |
2.05e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.47 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLT---FTIRGEEKIGIVGHTAAGKSSIV-HALFRLAHINGHISIDGF----ETSQLGLHD 1115
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDnisFELEEGSFVALVGHTGSGKSTLMqHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1116 LRRRISIIPQDP------------VLFsGSLRFNLDPFEEKTDEELWlaLEAVKLKEFVSNlkdgincrlhDCGANFSMG 1183
Cdd:PRK13641 83 LRKKVSLVFQFPeaqlfentvlkdVEF-GPKNFGFSEDEAKEKALKW--LKKVGLSEDLIS----------KSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1184 QRQLVCLARALLRQNKILIMDEATANVDPET-DNLIQEAIHTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHP 1261
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
....*..
gi 221460257 1262 HELLHNR 1268
Cdd:PRK13641 230 KEIFSDK 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
423-611 |
2.37e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.65 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVI--LGELD---IISGSVEVNGVLSYAPQE 497
Cdd:PRK14239 6 LQVSDLSVYYNKKKA------LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 498 PWLlrgSLRDNI--LFTEP-------YDEQRYleVLRV------CHLDRDVEQLPLGDST------RVGEGGASLSGGQK 556
Cdd:PRK14239 80 DTV---DLRKEIgmVFQQPnpfpmsiYENVVY--GLRLkgikdkQVLDEAVEKSLKGASIwdevkdRLHDSALGLSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 557 ARVSLARAVYRKADIYLLDDPLSAVDShVSKMLLDRCLNEFLSKKIRILVTHRVQ 611
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
444-631 |
2.39e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.89 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG-VLSyaPQEPWLLR----------------GSLR 506
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmVLS--EETVWDVRrqvgmvfqnpdnqfvgATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 507 DNILFT-E----PYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLS 579
Cdd:PRK13635 101 DDVAFGlEnigvPREEmvERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 580 AVDSHVSKMLLD--RCLNEflSKKIRIL-VTHRVQLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK13635 170 MLDPRGRREVLEtvRQLKE--QKGITVLsITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
444-631 |
2.47e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.36 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQE--------------PWLlrgSLRDN 508
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdITHVPAEnrhvntvfqsyalfPHM---TVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 509 ILF-----TEPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAV 581
Cdd:PRK09452 107 VAFglrmqKTPAAEitPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 582 DSHVSKML------LDRCLN-EFlskkirILVTH-RVQLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK09452 176 DYKLRKQMqnelkaLQRKLGiTF------VFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
444-631 |
2.74e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVlsyapqEPWLLRGSLRD-----NILFTEPyDEQ 518
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGV------DITDKKVKLSDirkkvGLVFQYP-EYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 519 RYLEVlrvchLDRDVE----QLPLGDS---TRVGEG----GAS-----------LSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:PRK13637 96 LFEET-----IEKDIAfgpiNLGLSEEeieNRVKRAmnivGLDyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 577 PLSAVDSHVSkmllDRCLNEF--LSKK---IRILVTHRVQ-LLRHVDHLVLLEGGRISVQG 631
Cdd:PRK13637 171 PTAGLDPKGR----DEILNKIkeLHKEynmTIILVSHSMEdVAKLADRIIVMNKGKCELQG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1044-1220 |
2.83e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 67.55 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLG--LHDLRRRI 1120
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKLTDDKknINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1121 SIIPQDpvlfsgslrFNLdpFEEKTD-EELWLAL---------EAVKLKEfvSNLKD-GINCRLHDCGANFSMGQRQLVC 1189
Cdd:cd03262 79 GMVFQQ---------FNL--FPHLTVlENITLAPikvkgmskaEAEERAL--ELLEKvGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190
....*....|....*....|....*....|.
gi 221460257 1190 LARALLRQNKILIMDEATANVDPEtdnLIQE 1220
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPE---LVGE 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
448-636 |
2.83e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 448 SFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-----------LSYAPQE----PWLlrgSLRDNI-LF 511
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQEnnlfSHL---TVAQNIgLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 TEP----YDEQRYL--EVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHV 585
Cdd:PRK10771 96 LNPglklNAAQREKlhAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 586 -SKM--LLDRCLNEflsKKIRIL-VTHRVQ-LLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:PRK10771 165 rQEMltLVSQVCQE---RQLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
422-631 |
3.34e-12 |
|
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: 66.81 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELD--IISGSVEVNGVlsyaPQEPW 499
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGR----PLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 500 LLRGSL----RDNILFtePYDEQRylEVLRVCHLDRdveqlplgdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLD 575
Cdd:cd03213 79 SFRKIIgyvpQDDILH--PTLTVR--ETLMFAAKLR------------------GLSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 576 DPLSAVDS----HVSKMLLDrclnefLSKKIR--ILVTH--RVQLLRHVDHLVLLEGGRISVQG 631
Cdd:cd03213 137 EPTSGLDSssalQVMSLLRR------LADTGRtiICSIHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1058-1276 |
4.39e-12 |
|
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: 71.13 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1058 PYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALF-RLAHINGHISIDGfetsqlglhdlrrRISIIPQDPVLFSGSLRF 1136
Cdd:TIGR00957 651 PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1137 NL---DPFEEKTDEELwlaLEAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPE 1213
Cdd:TIGR00957 718 NIlfgKALNEKYYQQV---LEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1214 TDNLIQEAI---HTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELLhNRHGYLHRFV 1276
Cdd:TIGR00957 795 VGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL-QRDGAFAEFL 859
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1057-1269 |
4.73e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1057 GPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRR-ISIIPQDPVLFSGSL 1134
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1135 RFN-----LDPFEEKTDEELWLALEAVkLKEF-VSNLKDGIncrlhdcGANFSMGQRQLVCLARALLRQNKILIMDEATA 1208
Cdd:PRK10895 95 VYDnlmavLQIRDDLSAEQREDRANEL-MEEFhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 1209 NVDPETDNLIQEAI-HTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHNRH 1269
Cdd:PRK10895 167 GVDPISVIDIKRIIeHLRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
423-634 |
4.77e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQkkqekrHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGEL--DIISGS-VEVngvLSYAPQEPW 499
Cdd:PRK09984 5 IRVEKLAKTFNQ------HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIEL---LGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 500 LLRGSLRDNILFT----EPYDEQRYLEVL--------------RVC--HLDRDVEQLPLGDSTRVG------EGGASLSG 553
Cdd:PRK09984 76 RLARDIRKSRANTgyifQQFNLVNRLSVLenvligalgstpfwRTCfsWFTREQKQRALQALTRVGmvhfahQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 554 GQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEflSKKIRILVT-HRVQL-LRHVDHLVLLEGGRISV 629
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDtlRDINQ--NDGITVVVTlHQVDYaLRYCERIVALRQGHVFY 233
|
....*...
gi 221460257 630 QG---HYD 634
Cdd:PRK09984 234 DGssqQFD 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
453-632 |
4.85e-12 |
|
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: 67.43 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 453 DQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQE-----PWLLRGSLRD--NILFTEPYDEQrylEVL 524
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYikadyEGTVRDLLSSitKDFYTHPYFKT---EIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 525 RVCHLDRDVEQlplgdstRVGEggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDS----HVSKMLLDRCLNEflsK 600
Cdd:cd03237 101 KPLQIEQILDR-------EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAENN---E 166
|
170 180 190
....*....|....*....|....*....|...
gi 221460257 601 KIRILVTHRVQLLRHV-DHLVLLEgGRISVQGH 632
Cdd:cd03237 167 KTAFVVEHDIIMIDYLaDRLIVFE-GEPSVNGV 198
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
422-694 |
5.16e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.21 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSaswdqkKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG---------VLS 492
Cdd:COG4152 1 MLELKGLT------KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepldpedrrRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 493 YAPQEpwllRG-----SLRDNILF-------TEPYDEQRYLEVLrvchldrdvEQLPLGD--STRVGEggasLSGGQKAR 558
Cdd:COG4152 75 YLPEE----RGlypkmKVGEQLVYlarlkglSKAEAKRRADEWL---------ERLGLGDraNKKVEE----LSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 559 VSLARAVYRKADIYLLDDPLSAVDShvskmlldrcLN-EFLSKKIR---------ILVTHRVQLL-RHVDHLVLLEGGRI 627
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDP----------VNvELLKDVIRelaakgttvIFSSHQMELVeELCDRIVIINKGRK 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 628 SVQGHYDALKKLI-RFRMSVANDVEVAKLRAMRTDSVYEEPEPRKSLSQEEHMDRHEIEQQFKEQQQI 694
Cdd:COG4152 208 VLSGSVDEIRRQFgRNTLRLEADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARGPV 275
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
446-631 |
6.17e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVI-------LGELDIISGSVEvngvLSYAPQEPWLLrgSLRDNI--LF----- 511
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFD----FSKTPSDKAIR--ELRRNVgmVFqqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 --------------------TEPYDEQRYLEVLRVCHLDRDVEQLPLgdstrvgeggaSLSGGQKARVSLARAVYRKADI 571
Cdd:PRK11124 94 wphltvqqnlieapcrvlglSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 572 YLLDDPLSAVDSHVSKMLLDrCLNEFLSKKI-RILVTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVS-IIRELAETGItQVIVTHEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
446-627 |
8.50e-12 |
|
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: 64.76 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGvlsyAPQEPWLLRGSLRDNILFtepydeqrylevlr 525
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----KEVSFASPRDARRAGIAM-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 526 vchldrdVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEFLSKKIRIL 605
Cdd:cd03216 80 -------VYQL---------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV-IRRLRAQGVAVI 136
|
170 180
....*....|....*....|....
gi 221460257 606 -VTHRVQ-LLRHVDHLVLLEGGRI 627
Cdd:cd03216 137 fISHRLDeVFEIADRVTVLRDGRV 160
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
436-632 |
1.12e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 436 KQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------------LSYAPQEPWLL 501
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 RG-SLRDNIL--------FTEPYDEQRYLEVLRVCHLDRdveqlpLGDSTrvgegGASLSGGQKARVSLARAVYRKADIY 572
Cdd:PRK10895 91 RRlSVYDNLMavlqirddLSAEQREDRANELMEEFHIEH------LRDSM-----GQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 573 LLDDPLSAVDShVSKMLLDRCLNEFLSKKIRILVT-HRVQllrhvDHLVLLEGGRISVQGH 632
Cdd:PRK10895 160 LLDEPFAGVDP-ISVIDIKRIIEHLRDSGLGVLITdHNVR-----ETLAVCERAYIVSQGH 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1065-1265 |
1.41e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1065 TFTIRGEEKIGIVGHTAAGKSSIVH--ALFrLAHINGHISIDGFEtsqlglHDL----RRRISIIPQDPVLFSG-SLRFN 1137
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1138 ----LDPfEEKTDEELWLALEAVKLKEFVSNLKDgincRLhdcGANFSMGQRQLVCLARALLRQNKILIMDEATANVDP- 1212
Cdd:PRK10771 92 iglgLNP-GLKLNAAQREKLHAIARQMGIEDLLA----RL---PGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1213 ---ETDNLIQEAIHTKfaHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK10771 164 lrqEMLTLVSQVCQER--QLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1044-1272 |
1.46e-11 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 65.64 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSS---IVHALFRLAHinGHISIDGFETSQLGLHDLRRR- 1119
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTtfyMIVGLVKPDS--GKILLDGQDITKLPMHKRARLg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSG-SLRFNLDPFEE---KTDEELWLALEAVkLKEFvsnlkdGINCRLHDCGANFSMGQRQLVCLARALL 1195
Cdd:cd03218 77 IGYLPQEASIFRKlTVEENILAVLEirgLSKKEREEKLEEL-LEEF------HITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1196 RQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN---RHG 1270
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANelvRKV 229
|
..
gi 221460257 1271 YL 1272
Cdd:cd03218 230 YL 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
446-627 |
1.66e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.53 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGeLDII-SGSVEVNGV-LSYAPQEPwllRGSLR-DNILFtepydeqryle 522
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAG-LDRPtSGTVRLAGQdLFALDEDA---RARLRaRHVGF----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 523 VLRVCHL------------------DRDVEQLPLGDSTRVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDPL 578
Cdd:COG4181 95 VFQSFQLlptltalenvmlplelagRRDARARARALLERVGLGHrldhypAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 579 SAVDS----HVSKMLLDrcLNE----FLskkirILVTHRVQLLRHVDHLVLLEGGRI 627
Cdd:COG4181 175 GNLDAatgeQIIDLLFE--LNRergtTL-----VLVTHDPALAARCDRVLRLRAGRL 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
422-627 |
1.76e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDqkkqekRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----------- 490
Cdd:PRK10851 2 SIEIANIKKSFG------RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 491 LSYAPQEPWLLRG-SLRDNILF-----------TEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKAR 558
Cdd:PRK10851 76 VGFVFQHYALFRHmTVFDNIAFgltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 559 VSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEFLsKKIRILVTHRVQLLRHV-DHLVLLEGGRI 627
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRwlRQLHEEL-KFTSVFVTHDQEEAMEVaDRVVVMSQGNI 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1066-1267 |
1.95e-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: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1066 FTIRGEEKIGIVGHTAAGKSSIVHA---LFRLAHinGHISIDG---FETSQ---LGLHdlRRRISIIPQDPVLFS----- 1131
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAiagLERPDS--GRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFPhlsvr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1132 GSLRFNL---------DPFEEKTDeelWLALEAVkLKEFVSNLkdgincrlhdcganfSMGQRQLVCLARALLRQNKILI 1202
Cdd:COG4148 96 GNLLYGRkrapraerrISFDEVVE---LLGIGHL-LDRRPATL---------------SGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1203 MDEATANVDPETDNLIQ---EAIHTKFAhCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:COG4148 157 MDEPLAALDLARKAEILpylERLRDELD-IPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1067-1259 |
2.00e-11 |
|
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: 64.82 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1067 TIRGEEKIGIVGHTAAGKSSIVH--ALFRLAHiNGHISIDGFETSQLGLHDlrRRISIIPQDPVLF-------------S 1131
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNliAGFETPQ-SGRVLINGVDVTAAPPAD--RPVSMLFQENNLFahltveqnvglglS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1132 GSLRFNldpfeEKTDEELWLALEAVKLKEFVSNLKDGIncrlhdcganfSMGQRQLVCLARALLRQNKILIMDEATANVD 1211
Cdd:cd03298 97 PGLKLT-----AEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 1212 PETDNLIQEAIHTKFAHcTVLTIAHRLHTVMD----NDRVMVVDMGRVVELG 1259
Cdd:cd03298 161 PALRAEMLDLVLDLHAE-TKMTVLMVTHQPEDakrlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1060-1281 |
2.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.80 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVhalfrlAHING--------------HISIDGFETSQLGLHD---------L 1116
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLV------THFNGlikskygtiqvgdiYIGDKKNNHELITNPYskkiknfkeL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDP--VLFSGSLRFNL--DPFEEKTDEElwlalEAVKLKEFVSN---LKDGIncrLHDCGANFSMGQRQLVC 1189
Cdd:PRK13631 115 RRRVSMVFQFPeyQLFKDTIEKDImfGPVALGVKKS-----EAKKLAKFYLNkmgLDDSY---LERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1190 LARALLRQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTD 266
|
250
....*....|....
gi 221460257 1268 RHGYLHRFVEKTGV 1281
Cdd:PRK13631 267 QHIINSTSIQVPRV 280
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
422-624 |
2.53e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWdqkkqEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG----------VL 491
Cdd:PRK15056 6 GIVVNDVTVTW-----RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptrqalqknLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 492 SYAPQEP---WLLRGSLRDNILF-----------TEPYDEQRYLEVL-RVCHLDRDVEQlplgdstrVGEggasLSGGQK 556
Cdd:PRK15056 81 AYVPQSEevdWSFPVLVEDVVMMgryghmgwlrrAKKRDRQIVTAALaRVDMVEFRHRQ--------IGE----LSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 557 ARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrCLNEFLSKKIRILV-THRV-QLLRHVDHLVLLEG 624
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS-LLRELRDEGKTMLVsTHNLgSVTEFCDYTVMVKG 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1060-1265 |
2.92e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.17 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAlfrlahINGHIS-------IDGFETSQLGLHDLRRRISIIPQDPVL--- 1129
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRA------INGTLTptagtvlVAGDDVEALSARAASRRVASVPQDTSLsfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1130 FSGSL---------RFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGIncrlhdcganfSMGQRQLVCLARALLRQNKI 1200
Cdd:PRK09536 92 FDVRQvvemgrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSL-----------SGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1201 LIMDEATANVD--------------PETDNLIQEAIHTkfahctvLTIAHRLhtvmdNDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK09536 161 LLLDEPTASLDinhqvrtlelvrrlVDDGKTAVAAIHD-------LDLAARY-----CDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
445-591 |
2.97e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG----VLSYAPQEPWL-----LRGSL--RDNILF-- 511
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdidDPDVAEACHYLghrnaMKPALtvAENLEFwa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 ----TEPYDEQRYLEVLRVchldRDVEQLPLGDstrvgeggasLSGGQKARVSLAR--AVYRKadIYLLDDPLSAVDSHV 585
Cdd:PRK13539 99 aflgGEELDIAAALEAVGL----APLAHLPFGY----------LSAGQKRRVALARllVSNRP--IWILDEPTAALDAAA 162
|
....*.
gi 221460257 586 SKMLLD 591
Cdd:PRK13539 163 VALFAE 168
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1061-1265 |
4.53e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALF-RLAHINGHISIDGFETSQLGLHDLRRRISIIPQDPV----------- 1128
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAgMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1129 LFSGSLRFNLDPFEEKTDEELWLALEAVKLkefvsnLKDGINCRLHdcgaNFSMGQRQLVCLARALLRQNKILIMDEATA 1208
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPDHASYYPH----MLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1209 NVD----PETDNLIQEaIHTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK15112 179 SLDmsmrSQLINLMLE-LQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1044-1238 |
4.81e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL------AHINGHISIDGFE--TSQLGLHD 1115
Cdd:PRK14243 11 LRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVEGKVTFHGKNlyAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1116 LRRRISIIPQDPVLFSGSLRFNL------DPFEEKTDEELWLALEAVKLKEFVsnlKDgincRLHDCGANFSMGQRQLVC 1189
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEV---KD----KLKQSGLSLSGGQQQRLC 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221460257 1190 LARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTIAHRL 1238
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
409-631 |
5.44e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 409 FFGRTHKPKAevKSITVHKLSASWDQKKQEKRHRHieDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELD---IISGSV 485
Cdd:TIGR00955 10 VFGRVAQDGS--WKQLVSRLRGCFCRERPRKHLLK--NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 486 EVNG----------VLSYAPQEPwLLRGSL--RDNILFT--------EPYDEQRylevLRVchlDRDVEQLPLGD--STR 543
Cdd:TIGR00955 86 LLNGmpidakemraISAYVQQDD-LFIPTLtvREHLMFQahlrmprrVTKKEKR----ERV---DEVLQALGLRKcaNTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 544 VGEGGA--SLSGGQKARVSLARAVYRKADIYLLDDPLSAVDS----HVSKMLLDRClnefLSKKIRILVTHR--VQLLRH 615
Cdd:TIGR00955 158 IGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSfmaySVVQVLKGLA----QKGKTIICTIHQpsSELFEL 233
|
250
....*....|....*.
gi 221460257 616 VDHLVLLEGGRISVQG 631
Cdd:TIGR00955 234 FDKIILMAEGRVAYLG 249
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1060-1259 |
5.64e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 63.75 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIrGEEKIGIVGHTAAGKSSivhaLFR-LAHI----NGHISIDGFETSQLGlHDLRRRISIIPQDpvlFSGSL 1134
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTT----LMRiLATLtppsSGTIRIDGQDVLKQP-QKLRRRIGYLPQE---FGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1135 RFNLDPFEE-----------KTDEELWLALEAVklkefvsNLKDgincRLHDCGANFSMGQRQLVCLARALLRQNKILIM 1203
Cdd:cd03264 86 NFTVREFLDyiawlkgipskEVKARVDEVLELV-------NLGD----RAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1204 DEATANVDPET----DNLIQEAIHTKfahcTVLTIAHRLHTVMDN-DRVMVVDMGRVVELG 1259
Cdd:cd03264 155 DEPTAGLDPEErirfRNLLSELGEDR----IVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
444-608 |
6.32e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.27 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELD---IISGSVEVNGV-----------LSYAPQEPWL---LrgSLR 506
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqrrIGILFQDDLLfphL--SVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 507 DNILFTEPYD---EQRYLEVLRVchLDRdveqlplgdstrVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:COG4136 95 ENLAFALPPTigrAQRRARVEQA--LEE------------AGLAGfadrdpATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|..
gi 221460257 578 LSAVDSHVSKMLLDRCLNEFLSKKI-RILVTH 608
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIpALLVTH 192
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
444-635 |
6.70e-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: 64.00 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQE------------PWLLRG-SLRDN 508
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGedITGLPPHEiarlgigrtfqiPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 509 ILFTEPYDEQRYLEVLRVCHLDRDV--------EQLPLGD--STRVGEggasLSGGQKARVSLARAVYRKADIYLLDDP- 577
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREAreraeellERVGLADlaDRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPa 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 578 --LSAVDSHVskmlldrcLNEFLsKKIR------ILVTHRVQL-LRHVDHLVLLEGGRISVQGHYDA 635
Cdd:cd03219 172 agLNPEETEE--------LAELI-RELRergitvLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1042-1267 |
7.65e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.48 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1042 GQLDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFR----LAHIN-GHISIDGfeTSQLGLHDL 1116
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTsGEILIGG--RDVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDPVLF-SGSLRFNL-----------DPFEEKTDEelwlALEAVKLKEF----VSNLkdgincrlhdcganf 1180
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIafplklrkvpkAEIDRRVRE----AAELLGLEDLldrkPKQL--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1181 SMGQRQLVCLARALLRQNKILIMDEATANVDPET-DNLIQE--AIHTKFAHCTV---------LTIAhrlhtvmdnDRVM 1248
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAEikRLHRRLGTTTIyvthdqveaMTLA---------DRIA 205
|
250
....*....|....*....
gi 221460257 1249 VVDMGRVVELGHPHELLHN 1267
Cdd:COG3839 206 VMNDGRIQQVGTPEELYDR 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1071-1259 |
7.78e-11 |
|
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: 63.08 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1071 EEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDG---FETSQ-LGLHDLRRRISIIPQDPVLFSG-SLRFNLDpFEEK 1144
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIVLNGtvlFDSRKkINLPPQQRKIGLVFQQYALFPHlNVRENLA-FGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1145 tdeelwlALEAVKLKEFVSNLKD--GINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQ--- 1219
Cdd:cd03297 102 -------RKRNREDRISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLpel 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 221460257 1220 EAIHTKFaHCTVLTIAHRLHTV-MDNDRVMVVDMGRVVELG 1259
Cdd:cd03297 175 KQIKKNL-NIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
444-627 |
8.44e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 63.20 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAP--QEPWLLRG--------------SLR 506
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdVSDLRgrAIPYLRRKigvvfqdfrllpdrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 507 DNILFT-----EPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLS 579
Cdd:cd03292 97 ENVAFAlevtgVPPREirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221460257 580 AVDSHVSKMLLDrCLNEFLSKKIRILV-THRVQLLRHVDHLVL-LEGGRI 627
Cdd:cd03292 166 NLDPDTTWEIMN-LLKKINKAGTTVVVaTHAKELVDTTRHRVIaLERGKL 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
445-582 |
8.63e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.76 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGvlsyapQEPWLLRGSLRDNILFTEPYD----EQRY 520
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG------TPLAEQRDEPHENILYLGHLPglkpELSA 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 521 LEVLRVCHLDRDVEQLPLGDS-TRVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDAlAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1025-1258 |
1.17e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1025 AYETEESV-NLPKHWPsggQLDFRDLRLRYSNHGpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHIS 1102
Cdd:PRK10522 306 PYKAEFPRpQAFPDWQ---TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQpQSGEIL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1103 IDGFETSQLGLHDLRRRISIIPQDPVLFSGSLrfnlDPFEEKTDEEL---WLalEAVKLKEFVSnLKDGincRLHDcgAN 1179
Cdd:PRK10522 382 LDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL----GPEGKPANPALvekWL--ERLKMAHKLE-LEDG---RISN--LK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1180 FSMGQRQLVCLARALLRQNKILIMDEATANVDP--------ETDNLIQEAIHTKFAhctvltIAHRLHTVMDNDRVMVVD 1251
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDEWAADQDPhfrrefyqVLLPLLQEMGKTIFA------ISHDDHYFIHADRLLEMR 523
|
....*..
gi 221460257 1252 MGRVVEL 1258
Cdd:PRK10522 524 NGQLSEL 530
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1044-1267 |
1.24e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 64.73 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHdlRRRISI 1122
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDsGRILLDGRDVTGLPPE--KRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLFS----------GsLRF-NLDPFE--EKTDEelwlALEAVKLKEF----VSNLkdgincrlhdcganfSMGQR 1185
Cdd:COG3842 82 VFQDYALFPhltvaenvafG-LRMrGVPKAEirARVAE----LLELVGLEGLadryPHQL---------------SGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1186 QLVCLARALLRQNKILIMDEATANVDPET-DNLIQE--AIHTKFAHCTV---------LTIAhrlhtvmdnDRVMVVDMG 1253
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLrEEMREElrRLQRELGITFIyvthdqeeaLALA---------DRIAVMNDG 212
|
250
....*....|....
gi 221460257 1254 RVVELGHPHELLHN 1267
Cdd:COG3842 213 RIEQVGTPEEIYER 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
435-627 |
1.67e-10 |
|
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: 62.23 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLRGSL--------- 505
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALieapgfypn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 506 ---RDNILFTEPY---DEQRYLEVLRVCHldrdveqlpLGDSTRVGEGGASLsgGQKARVSLARAVYRKADIYLLDDPLS 579
Cdd:cd03268 87 ltaRENLRLLARLlgiRKKRIDEVLDVVG---------LKDSAKKKVKGFSL--GMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221460257 580 AVDSHVSKMLLDRCLNefLSKK-IRILVT----HRVQLLrhVDHLVLLEGGRI 627
Cdd:cd03268 156 GLDPDGIKELRELILS--LRDQgITVLISshllSEIQKV--ADRIGIINKGKL 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
423-636 |
1.67e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSaswdqkKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVI--LGELD---IISGSVEVNGVLSYAPQE 497
Cdd:PRK11264 4 IEVKNLV------KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPEagtIRVGDITIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 498 PwLLRgSLRDNILFT----EPYDEQRYLEvlRVCHLDRDVEQLPLGDST--------RVGEGGAS------LSGGQKARV 559
Cdd:PRK11264 78 G-LIR-QLRQHVGFVfqnfNLFPHRTVLE--NIIEGPVIVKGEPKEEATararellaKVGLAGKEtsyprrLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 560 SLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEflSKKIRILVTHRVQLLRHV-DHLVLLEGGRISVQGHYDAL 636
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNtiRQLAQ--EKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
444-627 |
1.84e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLRG-SLRDNI--LFTEP------ 514
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVgmVFQQPnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 515 --YD------------EQRYL-----EVLRVCHLDRDVEQlplgdstRVGEGGASLSGGQKARVSLARAVYRKADIYLLD 575
Cdd:PRK14246 106 siYDniayplkshgikEKREIkkiveECLRKVGLWKEVYD-------RLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221460257 576 DPLSAVDShVSKMLLDRCLNEFLSKKIRILVTHR-VQLLRHVDHLVLLEGGRI 627
Cdd:PRK14246 179 EPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGEL 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1061-1257 |
2.22e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALF-RLAHINGHISIDGFETSQLGLHD-LRRRISIIPQDPVLFSgslrfNL 1138
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSgVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVP-----NL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1139 dpfeekTDEE-LWLALEAVK----------------LKEFvsnlkdGINCRLHDCGANFSMGQRQLVCLARALLRQNKIL 1201
Cdd:COG1129 95 ------SVAEnIFLGREPRRgglidwramrrrarelLARL------GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1202 IMDEATANVDP-ETDNLIqEAIHT-KFAHCTVLTIAHRLHTVMDN-DRVMVvdM--GRVVE 1257
Cdd:COG1129 163 ILDEPTASLTErEVERLF-RIIRRlKAQGVAIIYISHRLDEVFEIaDRVTV--LrdGRLVG 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
440-582 |
3.38e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 60.52 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 440 RHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVlsyaPQEPWLLRGSLRDNILFTePYDEQR 519
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK----PVTRRSPRDAIRAGIAYV-PEDRKR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 520 YLEVLrvchldrdveQLPLGDSTRVgegGASLSGG--QKarVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:cd03215 87 EGLVL----------DLSVAENIAL---SSLLSGGnqQK--VVLARWLARDPRVLILDEPTRGVD 136
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
549-631 |
3.67e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 549 ASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRClnEFLSKKIRI---LVTHRVQ-LLRHVDHLVLLEG 624
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL--ERLAREINIpilYVSHSLDeILRLADRVVVLEQ 204
|
....*..
gi 221460257 625 GRISVQG 631
Cdd:PRK11144 205 GKVKAFG 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1044-1264 |
4.10e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSnhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALfrlAHI----NGHISIDGFETS--------QL 1111
Cdd:PRK15439 12 LCARSISKQYS--GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKII---AGIvppdSGTLEIGGNPCArltpakahQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1112 GLHdlrrrisIIPQDPVLFSG-SLRFNLD---PFEEKTDEelwlaleavKLKEFVSNLkdGINCRLHDCGANFSMGQRQL 1187
Cdd:PRK15439 87 GIY-------LVPQEPLLFPNlSVKENILfglPKRQASMQ---------KMKQLLAAL--GCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1188 VCLARALLRQNKILIMDEATANVDP-ETDNLIQEAIHTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHEL 1264
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
754-1018 |
4.10e-10 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 62.62 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 754 PEYHrTRLRMMILYTFLILCTLIfyvlrTFGFFMM----TLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVL 829
Cdd:cd18559 33 PQEH-GQVYLSVLGALAILQGIT-----VFQYSMAvsigGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 830 AIDVNLPQAMMdsiefaVNALAVLAVVSTANIWLLIPATVVVA-----LLYGCRCLYIGASRSLKRIETISRSPIYSHTN 904
Cdd:cd18559 107 RVDSMAPQVIK------MWMGPLQNVIGLYLLILLAGPMAAVGiplglLYVPVNRVYAASSRQLKRLESVSKDPRYKLFN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 905 ATFKGLATIRALNGTKYMERDFHYYQnENTSALYLHVSINRAFAFWTDLICVLYILAVTFSFLLFdkhRGYYSGDVGLAI 984
Cdd:cd18559 181 ETLLGISVIKAFEWEEAFIRQVDAKR-DNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVS---RHSLAGLVALKV 256
|
250 260 270
....*....|....*....|....*....|....
gi 221460257 985 TQSMKLVLMCQAGMRQTVELENMMTSVERVMEYV 1018
Cdd:cd18559 257 FYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
457-580 |
4.49e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQ--EP-------WLLRGSLRDNilFTEPYDEQRYLEVLRVC 527
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyiSPdydgtveEFLRSANTDD--FGSSYYKTEIIKPLGLE 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 221460257 528 HL-DRDVEqlplgdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLDDPlSA 580
Cdd:COG1245 447 KLlDKNVK---------------DLSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
444-636 |
4.69e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAP--------QE-----------PWLlrgS 504
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvderlirQEagmvfqqfylfPHL---T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 505 LRDNILF--------TEPYDEQRYLEVLRvchldrdveqlPLGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:PRK09493 94 ALENVMFgplrvrgaSKEEAEKQARELLA-----------KVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 577 PLSAVDSHVSKMLLD--RCLNEflSKKIRILVTHRVQLLRHV-DHLVLLEGGRISVQGHYDAL 636
Cdd:PRK09493 163 PTSALDPELRHEVLKvmQDLAE--EGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1040-1267 |
7.17e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1040 SGGQLDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAL-FRLAHINGHISIDG------------- 1105
Cdd:PRK10619 2 SENKLNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInFLEKPSEGSIVVNGqtinlvrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1106 --FETSQLGLhdLRRRISIIPQDPVLFSGSLRfnLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHD-CGANFSM 1182
Cdd:PRK10619 80 kvADKNQLRL--LRTRLTMVFQHFNLWSHMTV--LENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1183 GQRQLVCLARALLRQNKILIMDEATANVDPEtdnLIQEA--IHTKFAH--CTVLTIAHRLHTVMD-NDRVMVVDMGRVVE 1257
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVlrIMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
250
....*....|
gi 221460257 1258 LGHPHELLHN 1267
Cdd:PRK10619 233 EGAPEQLFGN 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
444-639 |
8.18e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 8.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDII-----SGSVEVNGVLSYAP---------------QEPWLLRG 503
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 504 SLRDNILFTEPYDE-QRYLEVLrvchLDRDVEQLPLGDSTR--VGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSA 580
Cdd:PRK14243 106 SIYDNIAYGARINGyKGDMDEL----VERSLRQAALWDEVKdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 581 VDShVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLL-------EGGRISVQGHYDALKKL 639
Cdd:PRK14243 182 LDP-ISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFfnvelteGGGRYGYLVEFDRTEKI 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1060-1265 |
8.79e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.83 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGF------ETSQLGLHDLRRRISIIPQDPVLFS- 1131
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1132 ----GSLRFNLDPFEEKTDEELWLALEAVKLKefvSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEAT 1207
Cdd:PRK14246 105 lsiyDNIAYPLKSHGIKEKREIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1208 ANVDPETDNLIQEAIHTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1061-1256 |
8.95e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIR-GEekI-GIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHD-LRRRISIIPQDPVLFsgslrf 1136
Cdd:COG3845 21 NDDVSLTVRpGE--IhALLGENGAGKSTLMKILYGLYQPDsGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLV------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1137 nlDPFeekTDEE-LWLALEavKLKEFVSNLKDGINcRLHDCGANF-------------SMGQRQLVCLARALLRQNKILI 1202
Cdd:COG3845 93 --PNL---TVAEnIVLGLE--PTKGGRLDRKAARA-RIRELSERYgldvdpdakvedlSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 1203 MDEATANVDP-ETDNLIqeAIHTKFAH--CTVLTIAHRLHTVMDN-DRVMVVDMGRVV 1256
Cdd:COG3845 165 LDEPTAVLTPqEADELF--EILRRLAAegKSIIFITHKLREVMAIaDRVTVLRRGKVV 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
457-580 |
9.70e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQ----------EPWLlrGSLRDNILfTEPYdeqrYLEVLRV 526
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdydgtvEDLL--RSITDDLG-SSYY----KSEIIKP 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 221460257 527 CHLDRDVEQlplgdstRVGEggasLSGGQKARVSLARAVYRKADIYLLDDPlSA 580
Cdd:PRK13409 441 LQLERLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1044-1259 |
1.23e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 59.60 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFR-LAHINGHISIDGfetSQLGLHDlRRRISI 1122
Cdd:cd03269 1 LEVENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDG---KPLDIAA-RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IP-----------QDPVLFSGSLRfNLDPFEEKTDEELWLalEAVKLKEFVsnlkdgiNCRLHDcganFSMGQRQLVCLA 1191
Cdd:cd03269 75 LPeerglypkmkvIDQLVYLAQLK-GLKKEEARRRIDEWL--ERLELSEYA-------NKRVEE----LSKGNQQKVQFI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1192 RALLRQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELG 1259
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
457-658 |
1.38e-09 |
|
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: 62.26 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILG-ELDIISGSVEVNGV-LSYAPQEPWL-----LRGSLRD---------------NILFTEP 514
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGvDKDFNGEARPQPGIkVGYLPQEPQLdptktVRENVEEgvaeikdaldrfneiSAKYAEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 515 YDE-----------QRYLEVLRVCHLDRDVEQ------LPLGDsTRVgeggASLSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:TIGR03719 114 DADfdklaaeqaelQEIIDAADAWDLDSQLEIamdalrCPPWD-ADV----TKLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 578 LSAVDSHvSKMLLDRCLNEFlsKKIRILVTHRVQLLRHVDHLVL-LEGGR-ISVQGHYDALKKLIRFRMSVANDVEVAKL 655
Cdd:TIGR03719 189 TNHLDAE-SVAWLERHLQEY--PGTVVAVTHDRYFLDNVAGWILeLDRGRgIPWEGNYSSWLEQKQKRLEQEEKEESARQ 265
|
...
gi 221460257 656 RAM 658
Cdd:TIGR03719 266 KTL 268
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1048-1265 |
1.39e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1048 DLRLRYSNHGpyILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDG--FETSQLGLHDLRRRISIIP 1124
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QDP---VLFSG-------SLRfNLDPFEEKTDEELWLALEAVKLKEFvsnLKDGINCRLHdcganfsmGQRQLVCLARAL 1194
Cdd:PRK13638 84 QDPeqqIFYTDidsdiafSLR-NLGVPEAEITRRVDEALTLVDAQHF---RHQPIQCLSH--------GQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 1195 LRQNKILIMDEATANVDPETDNLIQEAIHTKFAHCTVLTI-AHRLHTVMD-NDRVMVVDMGRVVELGHPHELL 1265
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1044-1271 |
1.41e-09 |
|
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: 62.39 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPY--ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-----AHINGHISIDGFETSQLGLHDL 1116
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpaAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RR----RISIIPQDP----------------VLfsgSLRFNLDPfEEKTDEELWLaLEAVKLKEFVSnlkdgincRLHDC 1176
Cdd:COG4172 87 RRirgnRIAMIFQEPmtslnplhtigkqiaeVL---RLHRGLSG-AAARARALEL-LERVGIPDPER--------RLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1177 GANFSMGQRQLVCLARALLRQNKILIMDEatanvdPET--DNLIQEAI---------HTKFAhctVLTIAHRLHTVMD-N 1244
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADE------PTTalDVTVQAQIldllkdlqrELGMA---LLLITHDLGVVRRfA 224
|
250 260
....*....|....*....|....*...
gi 221460257 1245 DRVMVVDMGRVVELGHPHELLHN-RHGY 1271
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAApQHPY 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
444-627 |
1.56e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------------LSYAPQEPWLLRGS 504
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetgnknlkklrkkvsLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 505 -LRD------NILFTEPYDEQRYLEVLRVCHLDRDV-EQLPLgdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:PRK13641 103 vLKDvefgpkNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPF-----------ELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 577 PLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRV-QLLRHVDHLVLLEGGRI 627
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
439-631 |
1.62e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 439 KRHRHI-EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELD--------IISGSVEVNG----------------VLSY 493
Cdd:PRK13547 11 RRHRAIlRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGeplaaidaprlarlraVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 494 APQEPWLLrgSLRDNILFTepydeqRYLEVLR---VCHLDRDVEQLPL---GDSTRVGEGGASLSGGQKARVSLARAV-- 565
Cdd:PRK13547 91 AAQPAFAF--SAREIVLLG------RYPHARRagaLTHRDGEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 566 -------YRKADIYLLDDPLSAVDSHVSKMLLDRCLNefLSKKIRILV---THRVQL-LRHVDHLVLLEGGRISVQG 631
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRR--LARDWNLGVlaiVHDPNLaARHADRIAMLADGAIVAHG 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
423-632 |
1.74e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.97 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKqeKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--LSYAPQEpwl 500
Cdd:PRK11153 2 IELKNISKVFPQGG--RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 LRGSLR------------------DNILFT-----EPYDE--QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQ 555
Cdd:PRK11153 77 LRKARRqigmifqhfnllssrtvfDNVALPlelagTPKAEikARVTELLELVGLSDKADRYP-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 556 KARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLD--RCLNEFLSKKIrILVTHRVQLLRHV-DHLVLLEGGRISVQGH 632
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILEllKDINRELGLTI-VLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1051-1265 |
1.84e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1051 LRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALF-RLAHINGHISIDGFETSQLGLHDLRRRISIIPQDPVL 1129
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1130 ---FS---------GSLRFNLDPFEEKTDEelwlALEAVKLKEFVSnlkdgincRLHdcgANFSMGQRQLVCLARALLR- 1196
Cdd:PRK13548 88 sfpFTveevvamgrAPHGLSRAEDDALVAA----ALAQVDLAHLAG--------RDY---PQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1197 -----QNKILIMDEATANVDpetdnlIQEAIHT-----KFAH---CTVLTIAHRLH-TVMDNDRVMVVDMGRVVELGHPH 1262
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALD------LAHQHHVlrlarQLAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
...
gi 221460257 1263 ELL 1265
Cdd:PRK13548 227 EVL 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1076-1253 |
1.85e-09 |
|
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: 59.27 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1076 IVGHTAAGKSSIVHALF-RLAHINGHISIDGFETSQLGLHDLRRR----ISIIPQDPVLFSGSLRFNLdPFEEKTDEELW 1150
Cdd:cd03290 32 IVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENI-TFGSPFNKQRY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1151 LAL-EAVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPE-TDNLIQEAIhTKFAH 1228
Cdd:cd03290 111 KAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGI-LKFLQ 189
|
170 180
....*....|....*....|....*...
gi 221460257 1229 ---CTVLTIAHRLHTVMDNDRVMVVDMG 1253
Cdd:cd03290 190 ddkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
444-631 |
1.97e-09 |
|
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: 59.67 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAP------------QEPWLLRG-SLRDN 508
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrdITGLPPhriarlgiartfQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 509 IL----------------------FTEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVY 566
Cdd:COG0411 100 VLvaaharlgrgllaallrlprarREEREARERAEELLERVGLADRADEPA-----------GNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 567 RKADIYLLDDP---LSAVDSHVskmlldrcLNEFLsKKIR-------ILVTHRVQLL-RHVDHLVLLEGGRISVQG 631
Cdd:COG0411 169 TEPKLLLLDEPaagLNPEETEE--------LAELI-RRLRdergitiLLIEHDMDLVmGLADRIVVLDFGRVIAEG 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
444-650 |
2.09e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.05 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQvILGELD-IISGSVEVNG--VLSYAPQEPWLLRgslRDNILFTEpydeQRY 520
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDkPTSGTYRVAGqdVATLDADALAQLR---REHFGFIF----QRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 -----------LEV-------LRVCHLDRDVEQLP-LGDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAV 581
Cdd:PRK10535 96 hllshltaaqnVEVpavyaglERKQRLLRAQELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 582 DSHVSK--MLLDRCLNEflSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQGHYDALKKLIRFRMSVANDV 650
Cdd:PRK10535 176 DSHSGEevMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTA 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1002-1265 |
2.10e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.74 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1002 VELENMMTSVERVMEYVnipSEPAYETEESVNLPKhwpsggqLDFRDLRLRYSNHGPYILK---GLTFTIRGEEKIGIVG 1078
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGV---SEVEKECEVEVGEPI-------IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1079 HTAAGKSSIVHAL------------FRLahinGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGslRFNLDPFEEKTD 1146
Cdd:TIGR03269 318 TSGAGKTTLSKIIagvleptsgevnVRV----GDEWVDMTKPGPDGRGRAKRYIGILHQEYDLYPH--RTVLDNLTEAIG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1147 EEL------WLALEAVKLKEFVSNLKDGINCRLHDcgaNFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQE 1220
Cdd:TIGR03269 392 LELpdelarMKAVITLKMVGFDEEKAEEILDKYPD---ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTH 468
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 221460257 1221 AIHT--KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELL 1265
Cdd:TIGR03269 469 SILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
421-631 |
2.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 421 KSITVHKLSASWdQKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQV------------ILGELDIISGSVEVN 488
Cdd:PRK13645 5 KDIILDNVSYTY-AKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYAIPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 489 GV--------LSYAPQEPWLLRGSLRDNILF---------TEPYdeQRYLEVLRVCHLDRD-VEQLPLgdstrvgeggaS 550
Cdd:PRK13645 84 EVkrlrkeigLVFQFPEYQLFQETIEKDIAFgpvnlgenkQEAY--KKVPELLKLVQLPEDyVKRSPF-----------E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 551 LSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSK--MLLDRCLNEFLSKKIrILVTHRV-QLLRHVDHLVLLEGGRI 627
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfINLFERLNKEYKKRI-IMVTHNMdQVLRIADEVIVMHEGKV 229
|
....
gi 221460257 628 SVQG 631
Cdd:PRK13645 230 ISIG 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
444-627 |
2.11e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 59.85 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG-VLSYAP------------QEP-----------W 499
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhKLEYGDykyrckhirmifQDPntslnprlnigQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 500 LLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQLPLGDstrvgeggasLSGGQKARVSLARAVYRKADIYLLDDPLS 579
Cdd:COG4167 109 ILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHM----------LSSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 580 AVDSHV-SKMlldrcLNEFLSKKIR-----ILVTHRVQLLRHV-DHLVLLEGGRI 627
Cdd:COG4167 179 ALDMSVrSQI-----INLMLELQEKlgisyIYVSQHLGIVKHIsDKVLVMHQGEV 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
423-631 |
2.22e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 59.71 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG------------- 489
Cdd:COG4604 2 IEIKNVSKRYGGKVV------LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 490 VLSYAPQEPWL-LRGSLRDNILFTE-PY--------DEQ------RYLEV--LRVCHLDrdveqlplgdstrvgeggaSL 551
Cdd:COG4604 76 RLAILRQENHInSRLTVRELVAFGRfPYskgrltaeDREiideaiAYLDLedLADRYLD-------------------EL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 552 SGGQKARVSLARAVYRKADIYLLDDPLSAVD-SH-VSKMLLDRCLNEFLSKKIrILVTHRVQLL-RHVDHLVLLEGGRIS 628
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHsVQMMKLLRRLADELGKTV-VIVLHDINFAsCYADHIVAMKDGRVV 215
|
...
gi 221460257 629 VQG 631
Cdd:COG4604 216 AQG 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1061-1271 |
2.46e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFET---SQLGLHDLRRRISIIPQDPVlfsGSL-- 1134
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETpTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY---GSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1135 RFNL-----DPFEEKTDeelwlaLEAVKLKEFVSNLKDGINCRLHDCGAN---FSMGQRQLVCLARALLRQNKILIMDEA 1206
Cdd:PRK11308 108 RKKVgqileEPLLINTS------LSAAERREKALAMMAKVGLRPEHYDRYphmFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1207 TANVD----PETDNL---IQEAIHTKFahctvLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN-RHGY 1271
Cdd:PRK11308 182 VSALDvsvqAQVLNLmmdLQQELGLSY-----VFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNpRHPY 250
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
447-707 |
2.80e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.71 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 447 VSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG-VLSYAPQEpwLLRGSLRDNILFTEPyDEQrylevLR 525
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYDKKS--LLEVRKTVGIVFQNP-DDQ-----LF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 526 VCHLDRDVEQLPLG-------------DS-TRVG-EGGAS-----LSGGQKARVSLARAVYRKADIYLLDDPLSAVD--- 582
Cdd:PRK13639 93 APTVEEDVAFGPLNlglskeevekrvkEAlKAVGmEGFENkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 583 -SHVSKMLLDrcLNEflsKKIRILV-THRVQLL-RHVDHLVLLEGGRISVQGhydALKKLirfrMSVANDVEVAKLRAMR 659
Cdd:PRK13639 173 aSQIMKLLYD--LNK---EGITIIIsTHDVDLVpVYADKVYVMSDGKIIKEG---TPKEV----FSDIETIRKANLRLPR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 221460257 660 TDSVYEEpeprksLSQEEHMDrheieqqFKEQQQIGSVKlQTYKEYFK 707
Cdd:PRK13639 241 VAHLIEI------LNKEDNLP-------IKMGYTIGEAR-RNIKELLK 274
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
445-582 |
3.22e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.27 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGvlsyapQEPWLLRGSLRDNILFTEPYDEQR----Y 520
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIARGLLYLGHAPGIKttlsV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 521 LEVLRVCHLDRDVEQLpLGDSTRVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:cd03231 91 LENLRFWHADHSDEQV-EEALARVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
423-583 |
3.37e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKkqekrhRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAP------- 495
Cdd:PRK11248 2 LQISHLYADYGGK------PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 496 -QE----PWLlrgSLRDNILFTepydeqryLEVLRVCHLDRdvEQLPLGDSTRVGEGGA------SLSGGQKARVSLARA 564
Cdd:PRK11248 76 fQNegllPWR---NVQDNVAFG--------LQLAGVEKMQR--LEIAHQMLKKVGLEGAekryiwQLSGGQRQRVGIARA 142
|
170
....*....|....*....
gi 221460257 565 VYRKADIYLLDDPLSAVDS 583
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDA 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
435-636 |
3.49e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.82 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQ--------------EP 498
Cdd:PRK13537 14 EKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepVPSRARHarqrvgvvpqfdnlDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 499 WLlrgSLRDNILFTEPY-------DEQRYLEVLRVCHLDRDVEqlplgdsTRVGEggasLSGGQKARVSLARAVYRKADI 571
Cdd:PRK13537 94 DF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 572 YLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRV-QLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMeEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
447-631 |
4.53e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 58.70 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 447 VSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDiISGSVEVNG--VLSYAPQEPWLLRGSLRDNIL-------------- 510
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGrpLSDWSAAELARHRAYLSQQQSppfampvfqylalh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 ----FTEPYDEQRYLEVLR----VCHLDRDVEQlplgdstrvgeggasLSGGQKARVSLARA---VYRKADIY----LLD 575
Cdd:COG4138 94 qpagASSEAVEQLLAQLAEalglEDKLSRPLTQ---------------LSGGEWQRVRLAAVllqVWPTINPEgqllLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 576 DPLSAVDSHvSKMLLDRCLNEFLSKKIRILV-THRVQL-LRHVDHLVLLEGGRISVQG 631
Cdd:COG4138 159 EPMNSLDVA-QQAALDRLLRELCQQGITVVMsSHDLNHtLRHADRVWLLKQGKLVASG 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1056-1278 |
4.99e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.61 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1056 HGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN------GHISIDGFE--TSQLGL-HDLRRRISIIPQD 1126
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDTARslSQQKGLiRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1127 pvlfsgslrFNLDPFE-------------EKTDEElwlalEAVKL-KEFVSnlKDGINCRLHDCGANFSMGQRQLVCLAR 1192
Cdd:PRK11264 94 ---------FNLFPHRtvleniiegpvivKGEPKE-----EATARaRELLA--KVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1193 ALLRQNKILIMDEATANVDPEtdnLIQEAIHTKFAHC----TVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPE---LVGEVLNTIRQLAqekrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
250
....*....|..
gi 221460257 1268 -RHGYLHRFVEK 1278
Cdd:PRK11264 235 pQQPRTRQFLEK 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1060-1264 |
5.46e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.20 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAL--------------FRLAHIN--GHIS--------------------I 1103
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiYHVALCEkcGYVErpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1104 DGFETSQLGLHDLRRRISIIPQDPVLFSGSLRF------NLDPFEEKTDEELWLALEAVKLKEfvsnlkdgINCRLHDCG 1177
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVldnvleALEEIGYEGKEAVGRAVDLIEMVQ--------LSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1178 ANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIH--TKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGR 1254
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|
gi 221460257 1255 VVELGHPHEL 1264
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
423-631 |
6.17e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.11 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQE------------KRHRHIE---DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEV 487
Cdd:cd03267 1 IEVSNLSKSYRVYSKEpgligslkslfkRKYREVEalkGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 488 NGVLSYAPQEPWLLRGSL----RDNILFTEPYDEQRYL--EVLRV------CHLDRDVEQLPLGD----STRvgeggaSL 551
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVvfgqKTQLWWDLPVIDSFYLlaAIYDLpparfkKRLDELSELLDLEElldtPVR------QL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 552 SGGQKARVSLARAVYRKADIYLLDDPLSAVDShVSKmlldRCLNEFLSKKIR------ILVTHRVQ-LLRHVDHLVLLEG 624
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-VAQ----ENIRNFLKEYNRergttvLLTSHYMKdIEALARRVLVIDK 229
|
....*..
gi 221460257 625 GRISVQG 631
Cdd:cd03267 230 GRLLYDG 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
423-627 |
6.40e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEKRHRH---IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----LSYA- 494
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHQHqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplakLNRAq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 495 --------------------PQEP--WLLRGSLRDNILFTEPYDEQRYLEVLRVCHLD-RDVEQLPlgdstrvgeggASL 551
Cdd:PRK10419 84 rkafrrdiqmvfqdsisavnPRKTvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRP-----------PQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 552 SGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrclnefLSKKIR-------ILVTHRVQLLRHVDHLVL-LE 623
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR------LLKKLQqqfgtacLFITHDLRLVERFCQRVMvMD 226
|
....
gi 221460257 624 GGRI 627
Cdd:PRK10419 227 NGQI 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
444-629 |
6.45e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAP--QEPWLL---------RGSLRDNILF 511
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyQRPINMmfqsyalfpHMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 TEPYDE-------QRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDsh 584
Cdd:PRK11607 115 GLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD-- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 585 vsKMLLDRCLNEFLSKKIRILVThrVQLLRHVDHLVLLEGGRISV 629
Cdd:PRK11607 182 --KKLRDRMQLEVVDILERVGVT--CVMVTHDQEEAMTMAGRIAI 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1061-1256 |
6.71e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.11 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALfrlahiNGHISIDGFETSQLGLHDLRRRISIIPQDPVLFS--GSLRFNL 1138
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKIL------SGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGqkTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1139 DPFEEKtdeELWLALEAVKLKEFVSNLkDGInCRLHDCGA-------NFSMGQRQLVCLARALLRQNKILIMDEATANVD 1211
Cdd:cd03267 111 PVIDSF---YLLAAIYDLPPARFKKRL-DEL-SELLDLEElldtpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221460257 1212 PETDNLIQEAIHT--KFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVV 1256
Cdd:cd03267 186 VVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1060-1267 |
6.93e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.80 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFET--SQLGLHDLRRRISIIPQdpvlfsgslRF 1136
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDGLKVndPKVDERLIRQEAGMVFQ---------QF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1137 NLdpFEEKTdeelwlALEAVKL-------------KEFVSNL--KDGINCRLHDCGANFSMGQRQLVCLARALLRQNKIL 1201
Cdd:PRK09493 87 YL--FPHLT------ALENVMFgplrvrgaskeeaEKQARELlaKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 1202 IMDEATANVDPE--------TDNLIQEAIhtkfahcTVLTIAHRL---HTVmdNDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK09493 159 LFDEPTSALDPElrhevlkvMQDLAEEGM-------TMVIVTHEIgfaEKV--ASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1050-1229 |
8.01e-09 |
|
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: 56.98 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1050 RLRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHdlrrrisiiPQDPV 1128
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRpDSGEVRWNGTPLAEQRDE---------PHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1129 LFSG---------SLRFNLD---PFEEKTDEELWLALEAVklkefvsnlkdGINCRLHDCGANFSMGQRQLVCLARALLR 1196
Cdd:TIGR01189 76 LYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAV-----------GLTGFEDLPAAQLSAGQQRRLALARLWLS 144
|
170 180 190
....*....|....*....|....*....|...
gi 221460257 1197 QNKILIMDEATANVDPETDNLIQEAIHtkfAHC 1229
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLR---AHL 174
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
447-631 |
8.18e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 447 VSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----LSYA----------PQEPWLLRG-SLRDNILF 511
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarLTPAkahqlgiylvPQEPLLFPNlSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 ---TEPYDEQRYLEVLRV--CHLDRDVEqlplgdstrvgegGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVS 586
Cdd:PRK15439 110 glpKRQASMQKMKQLLAAlgCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 587 KMLLDRcLNEFLSKKIRIL-VTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:PRK15439 177 ERLFSR-IRELLAQGVGIVfISHKLPEIRQLaDRISVMRDGTIALSG 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
446-631 |
8.25e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 57.70 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGeLDII-SGSVEVNGVLSYAPQEPWLlrgSLRDNI--LFtepydeQRY-- 520
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTITVDGEDLTDSKKDIN---KLRRKVgmVF------QQFnl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 ---LEVL--------RVCHLDRD------VEQLplgdsTRVGEGG------ASLSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:COG1126 89 fphLTVLenvtlapiKVKKMSKAeaeeraMELL-----ERVGLADkadaypAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 578 LSAvdshvskmlLDRCL-NEFLS--KKIR------ILVTHRVQLLRHV-DHLVLLEGGRISVQG 631
Cdd:COG1126 164 TSA---------LDPELvGEVLDvmRDLAkegmtmVVVTHEMGFAREVaDRVVFMDGGRIVEEG 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
444-627 |
9.72e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.77 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELD--IISGSVEVNG--VLSYAPQEpwllRGSLRDNILFTEPYDeqr 519
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGedITDLPPEE----RARLGIFLAFQYPPE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 520 yLEVLRVCHLDRDveqlplgdstrVGEGgasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDshVSKM-LLDRCLNEFL 598
Cdd:cd03217 89 -IPGVKNADFLRY-----------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD--IDALrLVAEVINKLR 151
|
170 180 190
....*....|....*....|....*....|..
gi 221460257 599 SKKIR-ILVTHRVQLLRHV--DHLVLLEGGRI 627
Cdd:cd03217 152 EEGKSvLIITHYQRLLDYIkpDRVHVLYDGRI 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1072-1300 |
1.01e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1072 EKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLG---LHDLRRRISIIPQDP---------VLFS--GSLRF 1136
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldprqtVGDSimEPLRV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1137 -NLDPFEEKTDEELWLaLEAVKLK-EFVSNLKdgincrlHDcganFSMGQRQLVCLARALLRQNKILIMDEATANVD--- 1211
Cdd:PRK10261 431 hGLLPGKAAAARVAWL-LERVGLLpEHAWRYP-------HE----FSGGQRQRICIARALALNPKVIIADEAVSALDvsi 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1212 -PETDNL---IQEAIHTKFahctvLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN-RHGYLHRFVEKTGVGTAQ 1285
Cdd:PRK10261 499 rGQIINLlldLQRDFGIAY-----LFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENpQHPYTRKLMAAVPVADPS 573
|
250
....*....|....*
gi 221460257 1286 HLRhlaeqsyRKRVL 1300
Cdd:PRK10261 574 RQR-------PQRVL 581
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1051-1271 |
1.02e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.77 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1051 LRYSNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALfrLAH-----INGHISIDGFETSQLGLHDLRRR-ISIIP 1124
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHpkyevTEGEILFKGEDITDLPPEERARLgIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QDPVLFSGslrfnldpfeektdeelwlaleaVKLKEFVSNLKDGincrlhdcganFSMGQRQLVCLARALLRQNKILIMD 1204
Cdd:cd03217 84 QYPPEIPG-----------------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 1205 EATANVDPETDNLIQEAIHT-KFAHCTVLTIAH--RLHTVMDNDRVMVVDMGRVVELGhPHELLH--NRHGY 1271
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG-DKELALeiEKKGY 200
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
444-627 |
1.06e-08 |
|
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: 57.25 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV----------------LSYApQEPWLlrgSLRD 507
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpvntvfQNYA-LFPHL---TVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 508 NILF-----TEPYDE--QRYLEVLRVC----HLDRDVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:cd03300 92 NIAFglrlkKLPKAEikERVAEALDLVqlegYANRKPSQL---------------SGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 577 PLSAVDSHVSK-MLLDrcLNEfLSKKIRI---LVTH-RVQLLRHVDHLVLLEGGRI 627
Cdd:cd03300 157 PLGALDLKLRKdMQLE--LKR-LQKELGItfvFVTHdQEEALTMSDRIAVMNKGKI 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
444-631 |
1.12e-08 |
|
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: 57.30 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV--------------LSYAPQEpwllRG-----S 504
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEG----RRifpslT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 505 LRDNIL---FTEPYDEQRylevlrvchlDRDVEQL----P-LGDstRVGEGGASLSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:COG0410 95 VEENLLlgaYARRDRAEV----------RADLERVyelfPrLKE--RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 577 P---LSAVdshVSKMLLDRClneflsKKIR------ILVTHRVQL-LRHVDHLVLLEGGRISVQG 631
Cdd:COG0410 163 PslgLAPL---IVEEIFEII------RRLNregvtiLLVEQNARFaLEIADRAYVLERGRIVLEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
405-577 |
1.17e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 405 EHGNFFGRTHKPKAEVKsITVHKLSaswdqkkqekRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGS 484
Cdd:COG1129 240 ELEDLFPKRAAAPGEVV-LEVEGLS----------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 485 VEVNGV--------------LSYAP----QEPWLLRGSLRDNILFTepydeqRYLEVLRVCHLDRD---------VEQL- 536
Cdd:COG1129 309 IRLDGKpvrirsprdairagIAYVPedrkGEGLVLDLSIRENITLA------SLDRLSRGGLLDRRreralaeeyIKRLr 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 537 --PLGDSTRVGeggaSLSGG--QKarVSLARAVYRKADIYLLDDP 577
Cdd:COG1129 383 ikTPSPEQPVG----NLSGGnqQK--VVLAKWLATDPKVLILDEP 421
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
423-631 |
1.61e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQekrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILG--ELDIISGSVEVNgvLSYAPQEPWL 500
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV------LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH--VALCEKCGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 LRGSL--------------------------------RDNILFTEP---YDEQRYLE-VLRVCH---------LDRDVEQ 535
Cdd:TIGR03269 73 ERPSKvgepcpvcggtlepeevdfwnlsdklrrrirkRIAIMLQRTfalYGDDTVLDnVLEALEeigyegkeaVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 536 LPLGD-STRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVT-HRVQLL 613
Cdd:TIGR03269 153 IEMVQlSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVI 232
|
250
....*....|....*....
gi 221460257 614 RHV-DHLVLLEGGRISVQG 631
Cdd:TIGR03269 233 EDLsDKAIWLENGEIKEEG 251
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1060-1257 |
1.72e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.39 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-AHINGHISIDGFETSQL---GLHDLRRRISIIPQDPV------- 1128
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1129 ----LFSGSLR--FNLDPFE--EKTDEelwlALEAVKLKEFVsnlkdgincrLHDCGANFSMGQRQLVCLARALLRQNKI 1200
Cdd:PRK10419 107 tvreIIREPLRhlLSLDKAErlARASE----MLRAVDLDDSV----------LDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1201 LIMDEATANVDpetdNLIQ-------EAIHTKFAHCTVLtIAHRLHTVMD-NDRVMVVDMGRVVE 1257
Cdd:PRK10419 173 LILDEAVSNLD----LVLQagvirllKKLQQQFGTACLF-ITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1044-1236 |
1.73e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 54.76 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALF-RLAHINGHISIDGfetsqlglhdlRRRISI 1122
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQdpvlfsgslrfnldpfeektdeelwlaleavklkefvsnlkdgincrlhdcganFSMGQRQLVCLARALLRQNKILI 1202
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 221460257 1203 MDEATANVDPETDNLIQEAIHTKfaHCTVLTIAH 1236
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1076-1302 |
1.74e-08 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 57.89 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1076 IVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHdlRRRISIIPQDPVLF---------SGSLRFNLDPFEEKt 1145
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDsGSIMLDGEDVTNVPPH--LRHINMVFQSYALFphmtveenvAFGLKMRKVPRAEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1146 DEELWLALEAVKLKEFVSNlkdgincRLHDcganFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQ---EAI 1222
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADR-------KPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlelKTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1223 HTKFAHCTVLTIAHRLHTVMDNDRVMVVDMGRVVELGHPHELL-HNRHGYLHRFVEKTGVGTAQHLRHLAEQSYRKRVLG 1301
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYeEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEG 226
|
.
gi 221460257 1302 R 1302
Cdd:TIGR01187 227 R 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
760-962 |
1.75e-08 |
|
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: 57.56 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 760 RLRMMILYTFLILCTLIFYVLRTFGFFMMTLRISLRI-HD---QLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDV-- 833
Cdd:cd07346 34 DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVvFDlrrDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 834 --NLPQAMMDSIEFAVnALAVLAVVStaniWLLIPATVVVALLYgcrclYIGASRSLKRIETISR------SPIYSHTNA 905
Cdd:cd07346 114 ssGLLQLLSDVLTLIG-ALVILFYLN----WKLTLVALLLLPLY-----VLILRYFRRRIRKASRevreslAELSAFLQE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 906 TFKGLATIRALNGTKYMERDFHYYQNENTSALYLHVSINRAFAFWTDLICVLYILAV 962
Cdd:cd07346 184 SLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
421-582 |
1.86e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.43 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 421 KSITVHKLSASWDQkkqEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLsYAPQEPWL 500
Cdd:PRK13650 3 NIIEVKNLTFKYKE---DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 LRGSLrdNILFTEPyDEQRY-----------LEVLRVCHLD---RDVEQLPL-GDSTRVGEGGASLSGGQKARVSLARAV 565
Cdd:PRK13650 79 IRHKI--GMVFQNP-DNQFVgatveddvafgLENKGIPHEEmkeRVNEALELvGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170
....*....|....*..
gi 221460257 566 YRKADIYLLDDPLSAVD 582
Cdd:PRK13650 156 AMRPKIIILDEATSMLD 172
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1035-1261 |
1.90e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1035 PKHWPSGGQLDFRDLRLRYsnHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahinghisIDGFETSQLG-- 1112
Cdd:PRK11247 4 TARLNQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRL--------LAGLETPSAGel 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1113 ------LHDLRRRISIIPQDPVLFsgslrfnldPFEEKTD-----------EELWLALEAVKLKEfvsnlkdgincRLHD 1175
Cdd:PRK11247 70 lagtapLAEAREDTRLMFQDARLL---------PWKKVIDnvglglkgqwrDAALQALAAVGLAD-----------RANE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1176 CGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFA--HCTVLTIAHRL-HTVMDNDRVMVVDM 1252
Cdd:PRK11247 130 WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEE 209
|
250
....*....|....
gi 221460257 1253 GRV-----VELGHP 1261
Cdd:PRK11247 210 GKIgldltVDLPRP 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1004-1273 |
3.24e-08 |
|
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: 58.38 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1004 LENMMTSVERVMEYVNIPSEPA----YETEESVNLPKHWPSGgqldfrDLRLRYSN---HGPYILKGLTFTIRGEEKIGI 1076
Cdd:TIGR01271 384 LEYNLTTTEVEMVNVTASWDEGigelFEKIKQNNKARKQPNG------DDGLFFSNfslYVTPVLKNISFKLEKGQLLAV 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1077 VGHTAAGKSSIVHALF-RLAHINGHISIDGfetsqlglhdlrrRISIIPQDPVLFSGSLRFNLdPFEEKTDEELWLA-LE 1154
Cdd:TIGR01271 458 AGSTGSGKSSLLMMIMgELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI-IFGLSYDEYRYTSvIK 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1155 AVKLKEFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKF-AHCTVLT 1233
Cdd:TIGR01271 524 ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLmSNKTRIL 603
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221460257 1234 IAHRLHTVMDNDRVMvvdmgrvvelghpheLLHNRHGYLH 1273
Cdd:TIGR01271 604 VTSKLEHLKKADKIL---------------LLHEGVCYFY 628
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
444-631 |
3.75e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.30 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGvLSYAPQEPWLLRGSLrdNILFTEP--------- 514
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN-QAITDDNFEKLRKHI--GIVFQNPdnqfvgsiv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 515 -YDEQRYLEVLRVCHLD---------RDVEQLPLGDSTRvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSH 584
Cdd:PRK13648 102 kYDVAFGLENHAVPYDEmhrrvsealKQVDMLERADYEP-----NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221460257 585 VSKMLLD--RCLNEflSKKIRIL-VTHRVQLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK13648 177 ARQNLLDlvRKVKS--EHNITIIsITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1046-1207 |
3.78e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.77 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSnhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahINGHISIDGFETSqlglhdLRR--RISII 1123
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKI--LAGELEPDSGEVS------IPKglRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1124 PQDPVLFSG---------------SLRFNLDPFEEKTDE---------ELWLALEAV-------KLKEFVSNLkdGINCR 1172
Cdd:COG0488 67 PQEPPLDDDltvldtvldgdaelrALEAELEELEAKLAEpdedlerlaELQEEFEALggweaeaRAEEILSGL--GFPEE 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 221460257 1173 LHD--CGaNFSMGQRQLVCLARALLRQNKILIMDEAT 1207
Cdd:COG0488 145 DLDrpVS-ELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
447-634 |
4.26e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 447 VSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIiSGSVEVNG--VLSYAPQEPWLLRGSL--RDNILFTEP---YdEQR 519
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGqpLEAWSAAELARHRAYLsqQQTPPFAMPvfqY-LTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 520 YLEVLRV-----CHLDRDVEQLPLGD--STRVGEggasLSGGQKARVSLARA---VYRKADIY----LLDDPLSAVDShV 585
Cdd:PRK03695 93 HQPDKTRteavaSALNEVAEALGLDDklGRSVNQ----LSGGEWQRVRLAAVvlqVWPDINPAgqllLLDEPMNSLDV-A 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 586 SKMLLDRCLNEFLSKKIRILVT-HRV-QLLRHVDHLVLLEGGRISVQGHYD 634
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSsHDLnHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
441-631 |
5.13e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 441 HRHIEDVSFQAQDQQFVGIVGTVGAGKST----LLQVILGEldiisGSVEVNGvlsyAPQEPWLLRGSL----RDNILFT 512
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDG----QPLHNLNRRQLLpvrhRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 513 EPYD--------EQRYLEVLRVCHLD---RDVEQLPLGDSTRVGEGGAS-------LSGGQKARVSLARAVYRKADIYLL 574
Cdd:PRK15134 370 DPNSslnprlnvLQIIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETrhrypaeFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 575 DDPLSAVDSHVSKMLLDrcLNEFLSKKIR---ILVTHRVQLLRHVDH-LVLLEGGRISVQG 631
Cdd:PRK15134 450 DEPTSSLDKTVQAQILA--LLKSLQQKHQlayLFISHDLHVVRALCHqVIVLRQGEVVEQG 508
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
445-631 |
6.23e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEPWLLRGSLRDNIlfTEPYD--EQRY 520
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehIQHYASKEVARRIGLLAQNA--TTPGDitVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 LEVLRVCHL---------DRDVEQLPL---GDSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVD-SHVSK 587
Cdd:PRK10253 102 VARGRYPHQplftrwrkeDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 588 MLldRCLNEFLSKKIRIL--VTHRV-QLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK10253 182 LL--ELLSELNREKGYTLaaVLHDLnQACRYASHLIALREGKIVAQG 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
444-582 |
6.48e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEpwllRG--------------SLRD 507
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPAD----RDiamvfqnyalyphmSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 508 NI---L----FTEPYDEQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSA 580
Cdd:PRK11650 96 NMaygLkirgMPKAEIEERVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
..
gi 221460257 581 VD 582
Cdd:PRK11650 165 LD 166
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
423-617 |
7.11e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKKQEKRHrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQEPwll 501
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSI--LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQpLHQMDEEA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 RGSLR-DNILF---------TEPYDEQRYLEVLRVCHLDRD--------VEQLPLGDstRVGEGGASLSGGQKARVSLAR 563
Cdd:PRK10584 82 RAKLRaKHVGFvfqsfmlipTLNALENVELPALLRGESSRQsrngakalLEQLGLGK--RLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 564 AVYRKADIYLLDDPLSAVDSHVSKMLLDR--CLNEFLSKKIrILVTHRVQL-------LRHVD 617
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLlfSLNREHGTTL-ILVTHDLQLaarcdrrLRLVN 221
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1002-1253 |
7.21e-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: 55.63 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1002 VELENMMTSVERVmeyvniPSEPAYETEESVNLPKHWPSGGQLDFRDLRLrysnHGPYILKGLTFTIRGEEKIGIVGHTA 1081
Cdd:cd03291 4 VIMENVTAFWDEG------FGELLEKAKQENNDRKHSSDDNNLFFSNLCL----VGAPVLKNINLKIEKGEMLAITGSTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1082 AGKSSIVHALF-RLAHINGHISIDGfetsqlglhdlrrRISIIPQDPVLFSGSLRFNLdPFEEKTDEELWLA-LEAVKLK 1159
Cdd:cd03291 74 SGKTSLLMLILgELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1160 EFVSNLKDGINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKF-AHCTVLTIAHRL 1238
Cdd:cd03291 140 EDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLmANKTRILVTSKM 219
|
250
....*....|....*
gi 221460257 1239 HTVMDNDRVMVVDMG 1253
Cdd:cd03291 220 EHLKKADKILILHEG 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1044-1267 |
7.39e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYsNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFrlAHING-------HISIDGFET--SQLGLH 1114
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKST----LF--LHFNGilkptsgEVLIKGEPIkyDKKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1115 DLRRRISIIPQDP--VLFSGSLR-------FNLDPFEEKTDEELWLALEAVKLKEFVSNLKdgincrlHdcgaNFSMGQR 1185
Cdd:PRK13639 75 EVRKTVGIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-------H----HLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1186 QLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHT-KFAHCTVLTIAHRLHTV-MDNDRVMVVDMGRVVELGHPHE 1263
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
....
gi 221460257 1264 LLHN 1267
Cdd:PRK13639 224 VFSD 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
455-614 |
7.88e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 455 QFVGIVGTVGAGKSTLLQVILGELDIISGSVEVngvlsyapqepwllrgsLRDNILFTEPYDEQRYlevlrvchldrdve 534
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------IDGEDILEEVLDQLLL-------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 535 qlplgdsTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIR------ILVTH 608
Cdd:smart00382 52 -------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSeknltvILTTN 124
|
....*.
gi 221460257 609 RVQLLR 614
Cdd:smart00382 125 DEKDLG 130
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
455-582 |
9.37e-08 |
|
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: 54.68 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 455 QFVGIVGTVGAGKSTLLQVILGEL--------------DIIS----------------GSVEVNGVLSYAPQEPWLLRGS 504
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLkpnlgkfddppdwdEILDefrgselqnyftklleGDVKVIVKPQYVDLIPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 505 LRDNILFTEPYDEQRYL-EVLRVCH-LDRDVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:cd03236 107 VGELLKKKDERGKLDELvDQLELRHvLDRNIDQL---------------SGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
412-635 |
9.52e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 412 RTHKPKAEVkSITVHKLSASwdqkkqekrhrHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG-- 489
Cdd:PRK10762 248 RLDKAPGEV-RLKVDNLSGP-----------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhe 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 490 VLSYAPQEPwLLRGSL-------RDNILFTEPYDEQRYLEVLR-----VCHLDRDVEQLPLGDSTR------------VG 545
Cdd:PRK10762 316 VVTRSPQDG-LANGIVyisedrkRDGLVLGMSVKENMSLTALRyfsraGGSLKHADEQQAVSDFIRlfniktpsmeqaIG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 546 EggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrCLNEFLSKKIRI-LVTHRV-QLLRHVDHLVLLE 623
Cdd:PRK10762 395 L----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIiLVSSEMpEVLGMSDRILVMH 469
|
250
....*....|..
gi 221460257 624 GGRISvqGHYDA 635
Cdd:PRK10762 470 EGRIS--GEFTR 479
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1049-1223 |
1.42e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1049 LRLR---YSNHGPYILKGLTFTIR-GEEKIgIVGHTAAGKSS---IVHALfrLAHINGHISIDGFETSQLGLHDLRRRIS 1121
Cdd:PRK10247 8 LQLQnvgYLAGDAKILNNISFSLRaGEFKL-ITGPSGCGKSTllkIVASL--ISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDPVLFSGSLRFNLD-PFE---EKTDEELWLA-LEAVKLKEfvSNLKDGINcrlhdcgaNFSMGQRQLVCLARALLR 1196
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfPWQirnQQPDPAIFLDdLERFALPD--TILTKNIA--------ELSGGEKQRISLIRNLQF 154
|
170 180
....*....|....*....|....*..
gi 221460257 1197 QNKILIMDEATANVDPETDNLIQEAIH 1223
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIH 181
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
435-609 |
1.56e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIE-DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGEL--DIISGSVEVngvlsyaPQEPWLLRGSLRDNILF 511
Cdd:COG2401 36 VELRVVERYVLrDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-------PDNQFGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 TEPYDEQryLEVLRVCHLDrDVeQLPLgdsTRVGEggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKmLLD 591
Cdd:COG2401 109 KGDFKDA--VELLNAVGLS-DA-VLWL---RRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK-RVA 176
|
170 180
....*....|....*....|.
gi 221460257 592 RCLNEfLSKKIRI---LVTHR 609
Cdd:COG2401 177 RNLQK-LARRAGItlvVATHH 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1061-1278 |
1.64e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIvhalfrLAHINGHISIDGFETSQLGL------------HDLRR---------- 1118
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTL------LRHLSGLITGDKSAGSHIELlgrtvqregrlaRDIRKsrantgyifq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1119 ------RISIIPQDPVLFSGSLRF---NLDPFEEKTDEELWLALEAVKLKEFVsnlkdgincrlHDCGANFSMGQRQLVC 1189
Cdd:PRK09984 94 qfnlvnRLSVLENVLIGALGSTPFwrtCFSWFTREQKQRALQALTRVGMVHFA-----------HQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1190 LARALLRQNKILIMDEATANVDPETDNLIQEAIH--TKFAHCTVLTIAHRLHTVMDN-DRVMVVDMGRVVELGHPHELLH 1266
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHVFYDGSSQQFDN 242
|
250
....*....|..
gi 221460257 1267 NRHGYLHRFVEK 1278
Cdd:PRK09984 243 ERFDHLYRSINR 254
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1061-1267 |
1.76e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 54.77 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGfETSQLGLHDLRRRISIIPQDPVLFS-------- 1131
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDsGRIVLNG-RDLFTNLPPRERRVGFVFQHYALFPhmtvaeni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1132 --GsLRfNLDPFEEKTD---EELwlaLEAVKL----KEFVSNLkdgincrlhdcganfSMGQRQLVCLARALLRQNKILI 1202
Cdd:COG1118 97 afG-LR-VRPPSKAEIRarvEEL---LELVQLeglaDRYPSQL---------------SGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1203 MDEATANVDPET-----DNLIQeaIHTKFaHCTVLTIAHRLHTVMDN-DRVMVVDMGRVVELGHPHELLHN 1267
Cdd:COG1118 157 LDEPFGALDAKVrkelrRWLRR--LHDEL-GGTTVFVTHDQEEALELaDRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
445-620 |
1.95e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGvlsyapqEPWL-LRGSLRDNILF------------ 511
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRrQRDEYHQDLLYlghqpgiktelt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 -----------TEPYDEQRYLEVLRVCHLdRDVEQLPLGdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLDDPLSA 580
Cdd:PRK13538 91 alenlrfyqrlHGPGDDEALWEALAQVGL-AGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 221460257 581 VDSHVSKMLLDRcLNEFLSKK-IRILVTHrvQLLRHVDHLV 620
Cdd:PRK13538 160 IDKQGVARLEAL-LAQHAEQGgMVILTTH--QDLPVASDKV 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1044-1264 |
1.96e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.04 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgPYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRlaHING-------HISIDGFETSQLGLHDL 1116
Cdd:PRK13652 4 IETRDLCYSYSGS-KEALNNINFIAPRNSRIAVIGPNGAGKST----LFR--HFNGilkptsgSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1117 RRRISIIPQDP--VLFS---------GSLRFNLDpfEEKTDEELWLALEAVKLKEfvsnLKDGINCRLhdcganfSMGQR 1185
Cdd:PRK13652 77 RKFVGLVFQNPddQIFSptveqdiafGPINLGLD--EETVAHRVSSALHMLGLEE----LRDRVPHHL-------SGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1186 QLVCLARALLRQNKILIMDEATANVDPE-TDNLIQ--EAIHTKFAHcTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHP 1261
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQgVKELIDflNDLPETYGM-TVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTV 222
|
...
gi 221460257 1262 HEL 1264
Cdd:PRK13652 223 EEI 225
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
90-327 |
2.30e-07 |
|
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: 54.09 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 90 ASIVYSIMAIAvhttQPLMLGGLVSFFsesTGKITKHSAYLYAMGVVLCSLISGLFFHPFMKYLFRVGSRVRLACAGLVY 169
Cdd:cd07346 7 LLLLATALGLA----LPLLTKLLIDDV---IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 170 RKFLRVSVAADNSGVSGYAISLMATDLPTFNESFY-CFHELWRGPLEgVVFVYIIYQLIGWP-AVVGLGTIVAFIPLQAW 247
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLT-LIGALVILFYLNWKlTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 248 AARAIARYKRSSADVGDERVKLMNEIIAAMQLIKMYAWEKS----FAKLIGKVRKEEMDSIRGSTYIYAGLQCTGMISKL 323
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTALGTA 238
|
....
gi 221460257 324 SLFL 327
Cdd:cd07346 239 LVLL 242
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1060-1242 |
2.70e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHinghisidgfETSQLGLHDLRRRISIIPQdpvlfsgslRFNLD 1139
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA----------PDEGVIKRNGKLRIGYVPQ---------KLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1140 PFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLHDCG-ANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETD--- 1215
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQval 159
|
170 180
....*....|....*....|....*...
gi 221460257 1216 -NLIQEAIHTkfAHCTVLTIAHRLHTVM 1242
Cdd:PRK09544 160 yDLIDQLRRE--LDCAVLMVSHDLHLVM 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
440-631 |
2.96e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.94 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 440 RHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGEldiiSGSVEVNGVLSYAPQEPWLLRGSLRDNIlftepydeqr 519
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLI---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 520 ylevlrvchlDRDVEQLPLGDSTrvgeggASLSGGQKARVSLARAVYR--KADIYLLDDPLSAVDSHVSKMLLDrCLNEF 597
Cdd:cd03238 73 ----------DVGLGYLTLGQKL------STLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLE-VIKGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 221460257 598 LSKKIR-ILVTHRVQLLRHVDHLVLL------EGGRISVQG 631
Cdd:cd03238 136 IDLGNTvILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
444-611 |
4.06e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 52.73 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVI--LGELdI----ISGSVEVNGVLSYAPQ-EPWLLR-------------- 502
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDL-IpgarVEGEILLDGEDIYDPDvDVVELRrrvgmvfqkpnpfp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 503 GSLRDNILF-------TEPYD-EQRYLEVLRVCHL-----DRdveqlpLGDStrvgegGASLSGGQKARVSLARAVYRKA 569
Cdd:COG1117 106 KSIYDNVAYglrlhgiKSKSElDEIVEESLRKAALwdevkDR------LKKS------ALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 570 DIYLLDDPLSAVD----SHVSKMLLDrclnefLSKKIRI-LVTHRVQ 611
Cdd:COG1117 174 EVLLMDEPTSALDpistAKIEELILE------LKKDYTIvIVTHNMQ 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1044-1274 |
4.32e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPY--ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL------AHINGHISIDG---FETSQLG 1112
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvVYPSGDIRFHGeslLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1113 LHDLR-RRISIIPQDPVLfsgslrfNLDPFE--EKTDEELwLAL------EAVKlKEFVSNL-KDGIN---CRLHDCGAN 1179
Cdd:PRK15134 86 LRGVRgNKIAMIFQEPMV-------SLNPLHtlEKQLYEV-LSLhrgmrrEAAR-GEILNCLdRVGIRqaaKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1180 FSMGQRQLVCLARALLRQNKILIMDEATANVDPEtdnlIQEAIHTKFA------HCTVLTIAHRLHTVMD-NDRVMVVDM 1252
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQN 232
|
250 260
....*....|....*....|...
gi 221460257 1253 GRVVELGHPHELLHN-RHGYLHR 1274
Cdd:PRK15134 233 GRCVEQNRAATLFSApTHPYTQK 255
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
442-627 |
4.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 442 RHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVN--------------------GVLSYAPQEPWLL 501
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpvrkkvGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 502 RGSLRD------NILFTEPYDEQRYLEVLRVCHLDRDV-EQLPLgdstrvgeggaSLSGGQKARVSLARAVYRKADIYLL 574
Cdd:PRK13643 100 ETVLKDvafgpqNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPF-----------ELSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 575 DDPLSAVD--SHVSKMLLDRCLNEflSKKIRILVTHRV-QLLRHVDHLVLLEGGRI 627
Cdd:PRK13643 169 DEPTAGLDpkARIEMMQLFESIHQ--SGQTVVLVTHLMdDVADYADYVYLLEKGHI 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
425-640 |
4.49e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.87 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 425 VHKLSASWDQKKQEKRHRHIE---DVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG-VLSYAP----- 495
Cdd:PRK15112 7 VRNLSKTFRYRTGWFRRQTVEavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLHFGDysyrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 496 -------QEP-----------WLLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRD-VEQLPlgdstrvgeggASLSGGQK 556
Cdd:PRK15112 87 qrirmifQDPstslnprqrisQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYP-----------HMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 557 ARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLnEFLSKK--IRILVTHRVQLLRHV-DHLVLLEGGRISVQGH- 632
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLML-ELQEKQgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSt 234
|
250
....*....|....*.
gi 221460257 633 --------YDALKKLI 640
Cdd:PRK15112 235 advlasplHELTKRLI 250
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
423-621 |
6.03e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.42 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 423 ITVHKLSASWDQKkqekrhRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVL--SYAPQEPWL 500
Cdd:PRK09544 5 VSLENVSVSFGQR------RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 lrgslrDNILftePYDEQRYLEvLRVCHLDRDVeqLPLGDstRVGEGG------ASLSGGQKARVSLARAVYRKADIYLL 574
Cdd:PRK09544 79 ------DTTL---PLTVNRFLR-LRPGTKKEDI--LPALK--RVQAGHlidapmQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221460257 575 DDPLSAVDSHVSKMLLDrclnefLSKKIRILVTHRVQLLRHVDHLVL 621
Cdd:PRK09544 145 DEPTQGVDVNGQVALYD------LIDQLRRELDCAVLMVSHDLHLVM 185
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
763-959 |
6.69e-07 |
|
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: 52.56 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 763 MMILYTFLILCTLIFYVLrtfgFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAID----VNLPQA 838
Cdd:cd18557 42 LLAIYLLQSVFTFVRYYL----FNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQsavtDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 839 MMDSIEFAVNaLAVLAVVS---TANIWLLIPATVVVALLYGcrclyigasRSLKRIE-TISRSPIYSHTNA--TFKGLAT 912
Cdd:cd18557 118 LRNILQVIGG-LIILFILSwklTLVLLLVIPLLLIASKIYG---------RYIRKLSkEVQDALAKAGQVAeeSLSNIRT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221460257 913 IRALNGTKYMERDF-----HYYQNENTSALY--LHVSINRAFAFWTdLICVLYI 959
Cdd:cd18557 188 VRSFSAEEKEIRRYsealdRSYRLARKKALAnaLFQGITSLLIYLS-LLLVLWY 240
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
457-627 |
7.13e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILGELDIISGSVEvngvlsyapqepwLLRGslrdnilFTEPYDEQRYLEVLR-----VCHLDR 531
Cdd:PRK10636 341 IGLLGRNGAGKSTLIKLLAGELAPVSGEIG-------------LAKG-------IKLGYFAQHQLEFLRadespLQHLAR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 532 DVEQLP-------LG----DSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDrCLNEFlsK 600
Cdd:PRK10636 401 LAPQELeqklrdyLGgfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE-ALIDF--E 477
|
170 180
....*....|....*....|....*...
gi 221460257 601 KIRILVTHRVQLLRH-VDHLVLLEGGRI 627
Cdd:PRK10636 478 GALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1044-1287 |
7.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.43 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHGPYILKGLtFTIRGEEKIG----IVGHTAAGKSSIvhalfrLAHINGHIS-----------IDGFET 1108
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAL-FDIDLEVKKGsytaLIGHTGSGKSTL------LQHLNGLLQptegkvtvgdiVVSSTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1109 SQLGLHDLRRRISIIPQDP--VLFSGSL----RFNLDPFEEKTDEELWLALEAVKL----KEFvsnlkdgincrLHDCGA 1178
Cdd:PRK13643 75 KQKEIKPVRKKVGVVFQFPesQLFEETVlkdvAFGPQNFGIPKEKAEKIAAEKLEMvglaDEF-----------WEKSPF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1179 NFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQ---EAIHTKFAhcTVLTIAHRLHTVMD-NDRVMVVDMGR 1254
Cdd:PRK13643 144 ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVADyADYVYLLEKGH 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 221460257 1255 VVELGHP------------HELLHNRHGYLHRFVEKTGVGTAQHL 1287
Cdd:PRK13643 222 IISCGTPsdvfqevdflkaHELGVPKATHFADQLQKTGAVTFEKL 266
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1059-1259 |
7.75e-07 |
|
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: 51.38 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1059 YILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLH-----DLRRRisiipqDPVLFSG 1132
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsGTVTVRGRVSSLLGLGggfnpELTGR------ENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1133 SLrFNLDPFE--EKTDEelwlaleavkLKEFvSNLKDGINCRLhdcgANFSMGQRQLVCLARALLRQNKILIMDEATANV 1210
Cdd:cd03220 110 RL-LGLSRKEidEKIDE----------IIEF-SELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1211 DPETDNLIQEAIHTKFAHC-TVLTIAHRLHTVMDN-DRVMVVDMGRVVELG 1259
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1060-1264 |
7.86e-07 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 51.85 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahinghisIDGFETSQLG--------LHDL---RRRISIIPQDPV 1128
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRL--------IAGFETPTSGeilldgkdITNLpphKRPVNTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1129 LFSgslrfNLDPFE-------------EKTDEELWLALEAVKLKEFVSNLKDGIncrlhdcganfSMGQRQLVCLARALL 1195
Cdd:cd03300 83 LFP-----HLTVFEniafglrlkklpkAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1196 RQNKILIMDEATANVDP--------ETDNLiQEAIHTKFAHCT-----VLTIAhrlhtvmdnDRVMVVDMGRVVELGHPH 1262
Cdd:cd03300 147 NEPKVLLLDEPLGALDLklrkdmqlELKRL-QKELGITFVFVThdqeeALTMS---------DRIAVMNKGKIQQIGTPE 216
|
..
gi 221460257 1263 EL 1264
Cdd:cd03300 217 EI 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
763-1213 |
9.44e-07 |
|
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: 53.26 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 763 MMILYTFLILCTLIFYVLRTFGFFMMTL--RISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAID---VNLPQ 837
Cdd:COG4615 48 ARLLLLFAGLLVLLLLSRLASQLLLTRLgqHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISqafVRLPE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 838 AMMDSIeFAVNALAVLAVVStaniW--LLIPATVVVALLYGCRCLYIGASRSLKRIETisrspiysHTNATFKGLATIra 915
Cdd:COG4615 128 LLQSVA-LVLGCLAYLAWLS----PplFLLTLVLLGLGVAGYRLLVRRARRHLRRARE--------AEDRLFKHFRAL-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 916 LNGTKymE--------RDFHYYQNENTSALYLHVSInRAFAFWTDLI----CVLYIL------------------AVTFS 965
Cdd:COG4615 193 LEGFK--ElklnrrrrRAFFDEDLQPTAERYRDLRI-RADTIFALANnwgnLLFFALiglilfllpalgwadpavLSGFV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 966 FLLFdkhrgYYSGDVGLAItQSMKLVLMCQAGMRQTVELENMMTSvervmeyvnipSEPAYETEESVNLPKHWPSggqLD 1045
Cdd:COG4615 270 LVLL-----FLRGPLSQLV-GALPTLSRANVALRKIEELELALAA-----------AEPAAADAAAPPAPADFQT---LE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1046 FRDLRLRYSNHG---PYILKGLTFTIRGEEKIGIVGHTAAGKSSIVH---ALFRLAHinGHISIDGFETSQLGLHDLRRR 1119
Cdd:COG4615 330 LRGVTYRYPGEDgdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKlltGLYRPES--GEILLDGQPVTADNREAYRQL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1120 ISIIPQDPVLFSGSLRFNLDPFEEKTDEelWlaLEAVKLKEFVSnLKDGincRLHDcgANFSMGQRQLVCLARALLRQNK 1199
Cdd:COG4615 408 FSAVFSDFHLFDRLLGLDGEADPARARE--L--LERLELDHKVS-VEDG---RFST--TDLSQGQRKRLALLVALLEDRP 477
|
490
....*....|....
gi 221460257 1200 ILIMDEATANVDPE 1213
Cdd:COG4615 478 ILVFDEWAADQDPE 491
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
398-629 |
9.58e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 398 KEAEDnPEH-----GNFFGRTHKpkAEVKSITVHKLSASWDQKKQEKRHRHieDVSFQaqDQQFVGIVGTVGAGKSTLLQ 472
Cdd:TIGR01257 902 EEMED-PEHpeginDSFFERELP--GLVPGVCVKNLVKIFEPSGRPAVDRL--NITFY--ENQITAFLGHNGAGKTTTLS 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 473 VILGELDIISGSVEVNG------------VLSYAPQEPWLLRG-SLRDNILFTEPYDEQRYLEVlrvcHLDRDVEQLPLG 539
Cdd:TIGR01257 975 ILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA----QLEMEAMLEDTG 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 540 DSTRVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLnEFLSKKIRILVTHrvqllrHVDHL 619
Cdd:TIGR01257 1051 LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL-KYRSGRTIIMSTH------HMDEA 1123
|
250
....*....|
gi 221460257 620 VLLeGGRISV 629
Cdd:TIGR01257 1124 DLL-GDRIAI 1132
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1061-1264 |
1.16e-06 |
|
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: 51.19 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDlrRRISIIPQDPVLF-----SGSL 1134
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERpDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFrhmtvFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1135 RFNLD-------PFEEKTDEELWLALEAVKLKEFVSNLKdgincrlhdcgANFSMGQRQLVCLARALLRQNKILIMDEA- 1206
Cdd:cd03296 96 AFGLRvkprserPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDEPf 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 1207 ---TANVDPETDNLIQEaIHTKFAHCTVLtIAHRLHTVMD-NDRVMVVDMGRVVELGHPHEL 1264
Cdd:cd03296 165 galDAKVRKELRRWLRR-LHDELHVTTVF-VTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
444-577 |
1.37e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG--VLSYAPQEpwllRGSLRDN-ILFTEPYDEQRY 520
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtvKLAYVDQS----RDALDPNkTVWEEISGGLDI 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 521 LEVlrvchLDRDV--------------EQlplgdSTRVGEggasLSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:TIGR03719 414 IKL-----GKREIpsrayvgrfnfkgsDQ-----QKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1044-1267 |
1.42e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.14 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSnhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHAL------------FRLAHINGHisiDGFETSQL 1111
Cdd:PRK11300 6 LSVSGLMMRFG--GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLtgfykptggtilLRGQHIEGL---PGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1112 GL-----H-DLRRRISII-----PQDPVLFSGSLR--FNLDPFEEKTDEELWLA---LEAVKLKEFvSNLKDGincrlhd 1175
Cdd:PRK11300 81 GVvrtfqHvRLFREMTVIenllvAQHQQLKTGLFSglLKTPAFRRAESEALDRAatwLERVGLLEH-ANRQAG------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1176 cgaNFSMGQRQLVCLARALLRQNKILIMDEATANVDP-ETDNLIQEAIHTKFAH-CTVLTIAHRLHTVMD-NDRVMVVDM 1252
Cdd:PRK11300 153 ---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPkETKELDELIAELRNEHnVTVLLIEHDMKLVMGiSDRIYVVNQ 229
|
250
....*....|....*
gi 221460257 1253 GRVVELGHPHELLHN 1267
Cdd:PRK11300 230 GTPLANGTPEEIRNN 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
444-608 |
1.54e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.03 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG---------------VL-SYA--PQEpwllrgSL 505
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthrsiqqrdicmVFqSYAlfPHM------SL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 506 RDNI-----LFTEPYDE--QRYLEVLRVCHL----DRDVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLL 574
Cdd:PRK11432 96 GENVgyglkMLGVPKEErkQRVKEALELVDLagfeDRYVDQI---------------SGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221460257 575 DDPLSAVDSHvskmlLDRCLNEflskKIRIL----------VTH 608
Cdd:PRK11432 161 DEPLSNLDAN-----LRRSMRE----KIRELqqqfnitslyVTH 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
444-630 |
1.61e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.58 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQViLGELDI-ISGSVEVNG----VLSYAPqepwllRGSLRDNIL-------- 510
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHL-LGGLDTpTSGDVIFNGqpmsKLSSAA------KAELRNQKLgfiyqfhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 511 ----FT--------------EPYD-EQRYLEVLRVCHLDRDVEQLPlgdstrvgeggASLSGGQKARVSLARAVYRKADI 571
Cdd:PRK11629 98 llpdFTalenvamplligkkKPAEiNSRALEMLAAVGLEHRANHRP-----------SELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 572 YLLDDPLSAVDSHVSKMLLDrCLNEFLSKK--IRILVTHRVQLLRHVDHLVLLEGGRISVQ 630
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQ-LLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
444-631 |
1.96e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.14 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQEpwllrgSLRDN--ILFTEPyDEQRY 520
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItISKENLK------EIRKKigIIFQNP-DNQFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 521 -----------LEVLRVchlDRDVEQLPLGD-STRVGEGGA------SLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:PRK13632 98 gatveddiafgLENKKV---PPKKMKDIIDDlAKKVGMEDYldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221460257 583 ----SHVSKMLLDrcLNEFLSKKIrILVTHRVQLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK13632 175 pkgkREIKKIMVD--LRKTRKKTL-ISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
444-631 |
2.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWLLRGSLrdNILFTEP--------Y 515
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV--GIVFQNPetqfvgrtV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 516 DEQRYLEVLRVC--------HLDRDVEQLPLGDSTRvgEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSK 587
Cdd:PRK13644 96 EEDLAFGPENLClppieirkRVDRALAEIGLEKYRH--RSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221460257 588 MLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK13644 174 AVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
452-624 |
2.55e-06 |
|
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: 49.11 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 452 QDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-LSYAPQEpwllrgslrdnilftepydeqrylevlrvchld 530
Cdd:cd03222 23 KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGItPVYKPQY--------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 531 rdveqlplgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDS----HVSKMLldRCLNEFlSKKIRILV 606
Cdd:cd03222 70 ------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAI--RRLSEE-GKKTALVV 128
|
170
....*....|....*....
gi 221460257 607 THRVQLLRHV-DHLVLLEG 624
Cdd:cd03222 129 EHDLAVLDYLsDRIHVFEG 147
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
444-627 |
2.61e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVI-----LGELDIISGSVEVNGVLSYAPQ-EPWLLRGSLRDNILFTEPYDE 517
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDvDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 518 QRYLE-----------VLRVCHLDRDVE----QLPLGDST--RVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSA 580
Cdd:PRK14267 100 LTIYDnvaigvklnglVKSKKELDERVEwalkKAALWDEVkdRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221460257 581 VDShVSKMLLDRCLNEFLSKKIRILVTHR-VQLLRHVDHLVLLEGGRI 627
Cdd:PRK14267 180 IDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKL 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1044-1251 |
2.72e-06 |
|
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: 49.95 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDlrRRISI 1122
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTsGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLF---------SGSLRFNLDPfEEKTDEELWLALEAVKLKEFVSNLKDGIncrlhdcganfSMGQRQLVCLARA 1193
Cdd:cd03301 77 VFQNYALYphmtvydniAFGLKLRKVP-KDEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1194 LLRQNKILIMDEATANVDP--------ETDNLiQEAIHTKFAHCT-----VLTIAHRLhTVMDNDRVMVVD 1251
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAklrvqmraELKRL-QQRLGTTTIYVThdqveAMTMADRI-AVMNDGQIQQIG 213
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1044-1269 |
3.08e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.96 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRY-SNHGPY-ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDGFETSQLGLHDL----R 1117
Cdd:PRK15093 4 LDIRNLTIEFkTSDGWVkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLspreR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1118 RR-----ISIIPQDPvlfsgslRFNLDPfEEKTDEEL------------------WLALEAVKLKEFVSnLKDGINCrLH 1174
Cdd:PRK15093 84 RKlvghnVSMIFQEP-------QSCLDP-SERVGRQLmqnipgwtykgrwwqrfgWRKRRAIELLHRVG-IKDHKDA-MR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1175 DCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIH--TKFAHCTVLTIAHRLHTVMD-NDRVMVVD 1251
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLY 233
|
250
....*....|....*...
gi 221460257 1252 MGRVVELGHPHELLHNRH 1269
Cdd:PRK15093 234 CGQTVETAPSKELVTTPH 251
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
434-631 |
3.15e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.55 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 434 QKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV-------------------LSYA 494
Cdd:PRK13646 13 QKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithktkdkyirpvrkrigMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 495 PQEPWLLRGSLRDNIL-----FTEPYDE--QRYLEVLRVCHLDRDV-EQLPLgdstrvgeggaSLSGGQKARVSLARAVY 566
Cdd:PRK13646 93 FPESQLFEDTVEREIIfgpknFKMNLDEvkNYAHRLLMDLGFSRDVmSQSPF-----------QMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 567 RKADIYLLDDPLSAVD--SHVSKMLLDRCLNEFLSKKIrILVTHRV-QLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDpqSKRQVMRLLKSLQTDENKTI-ILVSHDMnEVARYADEVIVMKEGSIVSQT 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
422-631 |
3.36e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 422 SITVHKLSASWDQKkQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGEL----------DIISGSVEVNGVL 491
Cdd:PRK13631 21 ILRVKNLYCVFDEK-QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygtiqvgDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 492 SYAPQ---------------------EPWLLRGSLRDNILF-----TEPYDEQR-----YLEV--LRVCHLDRDveqlPL 538
Cdd:PRK13631 100 ITNPYskkiknfkelrrrvsmvfqfpEYQLFKDTIEKDIMFgpvalGVKKSEAKklakfYLNKmgLDDSYLERS----PF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 539 GdstrvgeggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRV-QLLRHVD 617
Cdd:PRK13631 176 G-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVAD 244
|
250
....*....|....
gi 221460257 618 HLVLLEGGRISVQG 631
Cdd:PRK13631 245 EVIVMDKGKILKTG 258
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
444-627 |
4.48e-06 |
|
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: 50.05 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELD---IISGSVEVNG--VLSYAPQEPWLLRGslRD-NILFTEPYDe 517
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGedLLKLSEKELRKIRG--REiQMIFQDPMT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 518 qrYL-----------EVLRVcHLDRD--------VEQLplgdsTRVGEGGAS---------LSGGQKARVSLARAVYRKA 569
Cdd:COG0444 98 --SLnpvmtvgdqiaEPLRI-HGGLSkaeareraIELL-----ERVGLPDPErrldrypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 570 DIYLLDDPLSAVDshVS------KMLLDrclnefLSKKIR---ILVTHRVQLLRHV-DHLVLLEGGRI 627
Cdd:COG0444 170 KLLIADEPTTALD--VTiqaqilNLLKD------LQRELGlaiLFITHDLGVVAEIaDRVAVMYAGRI 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
444-582 |
5.62e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG------VLSYAPQ----------EPWLlrgSLRD 507
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTYQKQlcfvghrsgiNPYL---TLRE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 508 NILFtEPYDEQRYLEVLRVCHLDRdVEQL---PLGdstrvgeggaSLSGGQKARVSLARAVYRKADIYLLDDPLSAVD 582
Cdd:PRK13540 94 NCLY-DIHFSPGAVGITELCRLFS-LEHLidyPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
419-631 |
6.03e-06 |
|
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: 50.45 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 419 EVKSITVH-KLSASWdQKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGeLDIISGSVEVNGV-LSYAPQ 496
Cdd:COG4172 277 EARDLKVWfPIKRGL-FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 497 EPWL-LR-----------GSL--RDNI--LFTEPydeqryLEVLRVcHLDRD-----VEQLpLgdsTRVGEGGASL---- 551
Cdd:COG4172 355 RALRpLRrrmqvvfqdpfGSLspRMTVgqIIAEG------LRVHGP-GLSAAerrarVAEA-L---EEVGLDPAARhryp 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 552 ---SGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRcLNEfLSKKIR---ILVTHRVQLLRHV-DHLVLLEG 624
Cdd:COG4172 424 hefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDL-LRD-LQREHGlayLFISHDLAVVRALaHRVMVMKD 501
|
....*..
gi 221460257 625 GRISVQG 631
Cdd:COG4172 502 GKVVEQG 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
442-627 |
6.38e-06 |
|
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: 50.57 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 442 RHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVN-----------GVLSYAPQEPWL---------- 500
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGRGRAKRYIgilhqeydly 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 501 ----LRGSLRDNILFTEPyDE---QRYLEVLRVCHLDRD-----VEQLPlgdstrvgeggASLSGGQKARVSLARAVYRK 568
Cdd:TIGR03269 378 phrtVLDNLTEAIGLELP-DElarMKAVITLKMVGFDEEkaeeiLDKYP-----------DELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 569 ADIYLLDDPLSAVDSHVSKMLLDRCLN--EFLSKKIrILVTHRVQLLRHV-DHLVLLEGGRI 627
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKarEEMEQTF-IIVSHDMDFVLDVcDRAALMRDGKI 506
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1044-1264 |
7.06e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.83 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRYSnhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHdlRRRISI 1122
Cdd:PRK11607 20 LEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQpTAGQIMLDGVDLSHVPPY--QRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1123 IPQDPVLF-----SGSLRFNLD----PFEEKTD--EELwlaLEAVKLKEFVSNlkdgincRLHdcgaNFSMGQRQLVCLA 1191
Cdd:PRK11607 96 MFQSYALFphmtvEQNIAFGLKqdklPKAEIASrvNEM---LGLVHMQEFAKR-------KPH----QLSGGQRQRVALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 1192 RALLRQNKILIMDEATANVDPETDNLIQ----EAIHTKFAHCTVLTiaHRLHTVMD-NDRVMVVDMGRVVELGHPHEL 1264
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVT--HDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1033-1257 |
1.18e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1033 NLPKHWPSGGQ-LDFRDLRLRYSNHgpYILKGLTFTIRGEEKIGIVGHTAAGKSSivhaLFRLahINGHISID-GfeTSQ 1110
Cdd:COG0488 304 RFPPPERLGKKvLELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKL--LAGELEPDsG--TVK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1111 LGlHDLrrRISIIPQDpvlfsgslRFNLDPfeEKTDEElWLALEAVKLKE-FVSNLkdgincrlhdCGA----------- 1178
Cdd:COG0488 374 LG-ETV--KIGYFDQH--------QEELDP--DKTVLD-ELRDGAPGGTEqEVRGY----------LGRflfsgddafkp 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1179 --NFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIhTKFAHcTVLTIAHRlHTVMDN--DRVMVVDMGR 1254
Cdd:COG0488 430 vgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL-DDFPG-TVLLVSHD-RYFLDRvaTRILEFEDGG 506
|
...
gi 221460257 1255 VVE 1257
Cdd:COG0488 507 VRE 509
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1181-1259 |
1.63e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1181 SMGQRQLVCLARALLRQNKILIMDEATANVDPETDN----LIQEAIHTKFAHCTV---LTIAHRLHTvmdndRVMVVDMG 1253
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAqivsIIRELAETGITQVIVtheVEVARKTAS-----RVVYMENG 217
|
....*.
gi 221460257 1254 RVVELG 1259
Cdd:PRK11124 218 HIVEQG 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
550-636 |
1.65e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.25 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 550 SLSGGQKARVSLARAVYRKADIYLLDDPLSAVD-SHVSKMLldrCLNEFLSKK---IRILVTHRVQL-LRHVDHLVLLEG 624
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVL---ALVHRLSQErglTVIAVLHDINMaARYCDYLVALRG 223
|
90
....*....|..
gi 221460257 625 GRISVQGHYDAL 636
Cdd:PRK10575 224 GEMIAQGTPAEL 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
444-637 |
1.72e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVE------------------------------------- 486
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 487 ----VNGVLSYApqEPWLLRGSLRDNILF------TEPYD-EQRYLEVLRVCHLDRD-VEQLPLGdstrvgeggasLSGG 554
Cdd:PRK13651 103 irrrVGVVFQFA--EYQLFEQTIEKDIIFgpvsmgVSKEEaKKRAAKYIELVGLDESyLQRSPFE-----------LSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 555 QKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRV-QLLRHVDHLVLLEGGRISVQGH- 632
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDt 249
|
....*
gi 221460257 633 YDALK 637
Cdd:PRK13651 250 YDILS 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1061-1263 |
1.78e-05 |
|
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: 49.05 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSS---IVHALFRLAHINGHISIDGFETSQLGLHDLRRR-ISIIPQDPVLFSG-SLR 1135
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTlmkILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1136 FNLDPFEEKTDEELWLALEAVKL--KEFVSNLK-DGINCRLHDcgANFSMGQRQLVCLARALLRQNKILIMDEATANV-D 1211
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLraKNLLRELQlDADNVTRPV--GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 1212 PETDNLIQEAIHTKFAHCTVLTIAHRLHTV-----------------------MDNDRVMVVDMGRVVELGHPHE 1263
Cdd:TIGR02633 175 KETEILLDIIRDLKAHGVACVYISHKLNEVkavcdticvirdgqhvatkdmstMSEDDIITMMVGREITSLYPHE 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
445-631 |
1.96e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVevngvlSYAPQEpwllrGSLRDniLFTEPYDEQRYLevL 524
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV------HYRMRD-----GQLRD--LYALSEAERRRL--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 525 R----VCHLD-RD------------VEQL-PLG--------------------DSTRVGEGGASLSGGQKARVSLARAVY 566
Cdd:PRK11701 88 RtewgFVHQHpRDglrmqvsaggniGERLmAVGarhygdiratagdwlerveiDAARIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 567 RKADIYLLDDPLSAVDSHVSKMLLD--RCL-NEF-LSKkirILVTHR---VQLLRHvdHLVLLEGGRISVQG 631
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDllRGLvRELgLAV---VIVTHDlavARLLAH--RLLVMKQGRVVESG 234
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
760-927 |
2.21e-05 |
|
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: 47.80 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 760 RLRMMILYTFLILctlIFYVLRTFGFFM-------MTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAID 832
Cdd:cd18552 34 DLEALLLVPLAII---GLFLLRGLASYLqtylmayVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 833 VNLPQAMMDSIEFAVNALAVLAVVSTANiWLLIPATVVVALLYGcrcLYIG-ASRSLKRI-----ETISRspIYSHTNAT 906
Cdd:cd18552 111 NALTSALTVLVRDPLTVIGLLGVLFYLD-WKLTLIALVVLPLAA---LPIRrIGKRLRKIsrrsqESMGD--LTSVLQET 184
|
170 180
....*....|....*....|.
gi 221460257 907 FKGLATIRALNGTKYMERDFH 927
Cdd:cd18552 185 LSGIRVVKAFGAEDYEIKRFR 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
412-571 |
2.33e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 412 RTHKPKAEVKSI--TVHKLSAswdqkKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNG 489
Cdd:COG3845 245 RVEKAPAEPGEVvlEVENLSV-----RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 490 V--------------LSYAPQEPwLLRG-----SLRDNILFTEpYDEQRYLE--VLRVCHLDRDVEQL-------PLGDS 541
Cdd:COG3845 320 EditglsprerrrlgVAYIPEDR-LGRGlvpdmSVAENLILGR-YRRPPFSRggFLDRKAIRAFAEELieefdvrTPGPD 397
|
170 180 190
....*....|....*....|....*....|..
gi 221460257 542 TRVGeggaSLSGG--QKarVSLARAVYRKADI 571
Cdd:COG3845 398 TPAR----SLSGGnqQK--VILARELSRDPKL 423
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1039-1271 |
2.77e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1039 PSGGQLDFRDLRLRYSNHGPYI--LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRL-AHINGHISIDGF--------- 1106
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLlEQAGGLVQCDKMllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1107 ----ETSQLGLHDLR-RRISIIPQDPVL-----------FSGSLRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGIN 1170
Cdd:PRK10261 88 ielsEQSAAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1171 crlhdcgaNFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHT--KFAHCTVLTIAHRLHTVMD-NDRV 1247
Cdd:PRK10261 168 --------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVlqKEMSMGVIFITHDMGVVAEiADRV 239
|
250 260
....*....|....*....|....*
gi 221460257 1248 MVVDMGRVVELGHPHELLHN-RHGY 1271
Cdd:PRK10261 240 LVMYQGEAVETGSVEQIFHApQHPY 264
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
457-641 |
3.35e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILGELDIISGSVevngvlsyapqepwlLRGSLRDNILFTEPYDEQRYLEVLRVCHLDRDVEQL 536
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV---------------FRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 537 P-------LGDSTRVG----EGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLnefLSKKIRIL 605
Cdd:PLN03073 603 PeqklrahLGSFGVTGnlalQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV---LFQGGVLM 679
|
170 180 190
....*....|....*....|....*....|....*...
gi 221460257 606 VTHRVQLLR-HVDHLVLLEGGRIS-VQGHYDALKKLIR 641
Cdd:PLN03073 680 VSHDEHLISgSVDELWVVSEGKVTpFHGTFHDYKKTLQ 717
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
403-628 |
3.46e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 403 NPEHGNFfgrTHKPKAEVKSITvhklsaSWDQKKqekrhrhIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIIS 482
Cdd:PRK09700 254 KENVSNL---AHETVFEVRNVT------SRDRKK-------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 483 GSVEVNGVlSYAPQEPW--------LLRGSLRDNILFT--------------------------EPYDEQRYLEVLRV-- 526
Cdd:PRK09700 318 GEIRLNGK-DISPRSPLdavkkgmaYITESRRDNGFFPnfsiaqnmaisrslkdggykgamglfHEVDEQRTAENQREll 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 527 ---CHldrDVEQlplgdstRVGEggasLSGGQKARVSLARAVYRKADIYLLDDPLSAVD----SHVSKMLldRCLNEflS 599
Cdd:PRK09700 397 alkCH---SVNQ-------NITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVM--RQLAD--D 458
|
250 260 270
....*....|....*....|....*....|
gi 221460257 600 KKIRILVTHRV-QLLRHVDHLVLLEGGRIS 628
Cdd:PRK09700 459 GKVILMVSSELpEIITVCDRIAVFCEGRLT 488
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
444-577 |
3.73e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVnG---VLSYAPQEpwllRGSLRDN-ILFTEPYDEQR 519
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvKLAYVDQS----RDALDPNkTVWEEISGGLD 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221460257 520 YLEVlrvchLDRDV---------------EQLPLGDstrvgeggasLSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:PRK11819 415 IIKV-----GNREIpsrayvgrfnfkggdQQKKVGV----------LSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
444-631 |
3.85e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.10 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGEL---DIISGSVEVNGVlSYAPQEPWLLRGslRDNILFTEPYD---- 516
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGI-TLTAKTVWDIRE--KVGIVFQNPDNqfvg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 517 -----------EQRYL---EVLRVCH-LDRDVEQLPLGDSTRvgeggASLSGGQKARVSLARAVYRKADIYLLDDPLSAV 581
Cdd:PRK13640 100 atvgddvafglENRAVprpEMIKIVRdVLADVGMLDYIDSEP-----ANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 582 DSHVSKMLLDRCLNEFLSKKIRIL-VTHRVQLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVIsITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1053-1267 |
3.93e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1053 YSNHGPYILKGL---TFTIRGEEKIGIVGHTAAGKSSIVHALFRL------AHINGHISIDGFETSQLGLHDLRRRISII 1123
Cdd:PRK13645 16 YAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTIVGDYAIPANLKKIKEVKRLRKEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1124 PQDP--VLFSGSLR-------FNLDPFEEKTDEELWLALEAVKL-KEFVSNlkdgincrlhdCGANFSMGQRQLVCLARA 1193
Cdd:PRK13645 96 FQFPeyQLFQETIEkdiafgpVNLGENKQEAYKKVPELLKLVQLpEDYVKR-----------SPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 1194 LLRQNKILIMDEATANVDP--ETD--NLIQEAihTKFAHCTVLTIAHRLHTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPkgEEDfiNLFERL--NKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
457-582 |
4.26e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILGEL------------------------------DIISGSVEVngvlSYAPQE----PWLLR 502
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELkpnlgdydeepswdevlkrfrgtelqdyfkKLANGEIKV----AHKPQYvdliPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 503 GSLRDnILftEPYDEQ----RYLEVLRVCH-LDRDVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:COG1245 178 GTVRE-LL--EKVDERgkldELAEKLGLENiLDRDISEL---------------SGGELQRVAIAAALLRDADFYFFDEP 239
|
....*
gi 221460257 578 LSAVD 582
Cdd:COG1245 240 SSYLD 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1061-1289 |
4.77e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.66 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLaHI--NGHISIDGFE-TSQLGLHDL---RRRISIIPQDP--VLFSG 1132
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL-HVptQGSVRVDDTLiTSTSKNKDIkqiRKKVGLVFQFPesQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1133 S----LRFNLDPFEEKTDEELWLALEAVKLKEFVSNLKDGINCRLhdcganfSMGQRQLVCLARALLRQNKILIMDEATA 1208
Cdd:PRK13649 102 TvlkdVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFEL-------SGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1209 NVDPETDNLIQEAIhtKFAHCTVLTIAHRLHtVMDN-----DRVMVVDMGRVVELGHPHELLHNRHgylhrFVEKTGVGT 1283
Cdd:PRK13649 175 GLDPKGRKELMTLF--KKLHQSGMTIVLVTH-LMDDvanyaDFVYVLEKGKLVLSGKPKDIFQDVD-----FLEEKQLGV 246
|
250
....*....|..
gi 221460257 1284 ------AQHLRH 1289
Cdd:PRK13649 247 pkitkfAQRLAD 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
436-577 |
4.94e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.00 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 436 KQEKRHRH-IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGeldII---SGSVEVNGVlsyapqEPWLLRGSLRDNI-- 509
Cdd:COG4586 29 RREYREVEaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---ILvptSGEVRVLGY------VPFKRRKEFARRIgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 510 -------------------LFTEPY--DEQRYLEvlrvcHLDRDVEQLPLGD--STRVGEggasLSGGQKARVSLARAVY 566
Cdd:COG4586 100 vfgqrsqlwwdlpaidsfrLLKAIYriPDAEYKK-----RLDELVELLDLGEllDTPVRQ----LSLGQRMRCELAAALL 170
|
170
....*....|.
gi 221460257 567 RKADIYLLDDP 577
Cdd:COG4586 171 HRPKILFLDEP 181
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
435-634 |
5.18e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 435 KKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVLSYAPQEPWlLRGSLR--DNILFt 512
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAG-LSGQLTgiENIEF- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 513 epydeqrylEVLRVCHLDRDVEQL--------PLGDStrVGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSH 584
Cdd:PRK13546 109 ---------KMLCMGFKRKEIKAMtpkiiefsELGEF--IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221460257 585 VSKMLLDRcLNEFLSKKIRI-LVTHRV-QLLRHVDHLVLLEGGRISVQGHYD 634
Cdd:PRK13546 178 FAQKCLDK-IYEFKEQNKTIfFVSHNLgQVRQFCTKIAWIEGGKLKDYGELD 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
444-584 |
5.46e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 45.89 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEV---NGVLSYA---PQEPWLLRgslRDNIlftePYDE 517
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAqasPREILALR---RRTI----GYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 518 QrYLEVL-RVCHLDRdVEQ--LPLGDSTRVGEGGA--------------SL-----SGGQKARVSLARAVYRKADIYLLD 575
Cdd:COG4778 100 Q-FLRVIpRVSALDV-VAEplLERGVDREEARARArellarlnlperlwDLppatfSGGEQQRVNIARGFIADPPLLLLD 177
|
....*....
gi 221460257 576 DPLSAVDSH 584
Cdd:COG4778 178 EPTASLDAA 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
442-609 |
6.85e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 442 RHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV---------------------LSYAP----- 495
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagvaiiyqeLHLVPemtva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 496 ------QEP----WLLRGSLRdnilftepYDEQRYLEvlrvcHLDRDVE-QLPLGdstrvgeggaSLSGGQKARVSLARA 564
Cdd:PRK11288 98 enlylgQLPhkggIVNRRLLN--------YEAREQLE-----HLGVDIDpDTPLK----------YLSIGQRQMVEIAKA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221460257 565 VYRKADIYLLDDPLSAVDSHVSKMLLdRCLNEFLSK-KIRILVTHR 609
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLF-RVIRELRAEgRVILYVSHR 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1064-1255 |
7.57e-05 |
|
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: 47.13 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1064 LTFTIRGEEKIGIVGHTAAGKSSIVHALFRL--AHINGHISIDGFETS-QLGLHDLRRRISIIPQD-------PVL---- 1129
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAypGKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILgvgk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1130 ---------FSGSLRFNldpfEEKTDEELWLALEAVKLKEFVSNLKDGincrlhdcgaNFSMGQRQLVCLARALLRQNKI 1200
Cdd:TIGR02633 359 nitlsvlksFCFKMRID----AAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1201 LIMDEATANVD----PETDNLIQEAIHTKFAhctVLTIAHRLHTVMD-NDRVMVVDMGRV 1255
Cdd:TIGR02633 425 LILDEPTRGVDvgakYEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
420-626 |
7.88e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 420 VKSITVHKLSASwDQKKQEKRHRHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGEL--DIISGSVEVNGvlsYAPQE 497
Cdd:PLN03211 61 IKRILGHKPKIS-DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANN---RKPTK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 498 PWLLRGSL--RDNILFtePYDEQRylEVLRVCHLDRDVEQLPLGDSTRVGEGGAS-------------------LSGGQK 556
Cdd:PLN03211 137 QILKRTGFvtQDDILY--PHLTVR--ETLVFCSLLRLPKSLTKQEKILVAESVISelgltkcentiignsfirgISGGER 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 557 ARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNefLSKKIRILVTHRVQ----LLRHVDHLVLLEGGR 626
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS--LAQKGKTIVTSMHQpssrVYQMFDSVLVLSEGR 284
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1059-1257 |
8.42e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1059 YILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHinghisidgfETSQLGLHDLRRriSIIPQDPVLfsgslrfnL 1138
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK----------GTPVAGCVDVPD--NQFGREASL--------I 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1139 DPFEEKTDeelwlALEAVKLkefvsnlkdgincrLHDCG-----------ANFSMGQRQLVCLARALLRQNKILIMDEAT 1207
Cdd:COG2401 104 DAIGRKGD-----FKDAVEL--------------LNAVGlsdavlwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1208 ANVDPETDNLIQEAIH--TKFAHCTVLTIAHR--LHTVMDNDRVMVVDMGRVVE 1257
Cdd:COG2401 165 SHLDRQTAKRVARNLQklARRAGITLVVATHHydVIDDLQPDLLIFVGYGGVPE 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
444-631 |
9.18e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.67 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVI--LGEL---DIISGSVEVNGVLSYAPQEPWLLRgslRDNILFTEPYD-- 516
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQDIFKMDVIELRR---RVQMVFQIPNPip 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 517 ------------------------EQRYLEVLRVCHLDRDVEQlplgdstRVGEGGASLSGGQKARVSLARAVYRKADIY 572
Cdd:PRK14247 96 nlsifenvalglklnrlvkskkelQERVRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 573 LLDDPLSAVD----SHVSKMLLDrclnefLSKKIRI-LVTH-RVQLLRHVDHLVLLEGGRISVQG 631
Cdd:PRK14247 169 LADEPTANLDpentAKIESLFLE------LKKDMTIvLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1043-1267 |
9.52e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.85 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1043 QLDFRDLRLRYSNHGPYILKGL---TFTIRGEEKIGIVGHTAAGKSS-IVH--AL---------FRLAHINGHISIDGFE 1107
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKALdnvSVEINQGEFIAIIGQTGSGKTTfIEHlnALllpdtgtieWIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1108 TSQLGL-------------HDLRRRISIIPQ--DPVLFS---------GSLRFNLDPFEEKTdeelwLALEAVKL----K 1159
Cdd:PRK13651 82 KVLEKLviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEqtiekdiifGPVSMGVSKEEAKK-----RAAKYIELvgldE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1160 EFvsnlkdgincrLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHTKFAHC-TVLTIAHRL 1238
Cdd:PRK13651 157 SY-----------LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDL 225
|
250 260 270
....*....|....*....|....*....|
gi 221460257 1239 HTVMD-NDRVMVVDMGRVVELGHPHELLHN 1267
Cdd:PRK13651 226 DNVLEwTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1181-1268 |
9.61e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.18 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1181 SMGQRQLVCLARALLRQNKILIMDEATANVDPETDnlIQEAIHTKFAH----CTVLTIAHRLHTVMD-NDRVMVVDMGRV 1255
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQMRIEISRLHkrlgRTMIYVTHDQVEAMTlADKIVVLDAGRV 212
|
90
....*....|....*.
gi 221460257 1256 VELGHPHELLH---NR 1268
Cdd:PRK11000 213 AQVGKPLELYHypaNR 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1064-1264 |
9.72e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 46.25 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1064 LTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHdlRRRISIIPQDPVLFSG-SLRFNLD-- 1139
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSLGENVGyg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1140 ------PFEE---KTDEelwlALEAVKLKEFVSNLKDGIncrlhdcganfSMGQRQLVCLARALLRQNKILIMDEATANV 1210
Cdd:PRK11432 103 lkmlgvPKEErkqRVKE----ALELVDLAGFEDRYVDQI-----------SGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 1211 DPETDNLIQEAI---HTKFaHCTVLTIAH-RLHTVMDNDRVMVVDMGRVVELGHPHEL 1264
Cdd:PRK11432 168 DANLRRSMREKIrelQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
442-637 |
1.12e-04 |
|
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: 45.05 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 442 RHIEDVSFQAQDQQFVGIVGTVGAGKST-------LLQVILGE-----LDIISGSVEVNGVLSYAPQEPWLLRG-SLRDN 508
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRatvagHDVVREPREVRRRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 509 I-----LFTEPYDE--QRYLEVLRVCHL----DRDVeqlplgdstrvgeggASLSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:cd03265 94 LyiharLYGVPGAErrERIDELLDFVGLleaaDRLV---------------KTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 578 LSAVDSHVSKMLLD--RCLNEFLSKKIrILVTHRV----QLlrhVDHLVLLEGGRISVQGHYDALK 637
Cdd:cd03265 159 TIGLDPQTRAHVWEyiEKLKEEFGMTI-LLTTHYMeeaeQL---CDRVAIIDHGRIIAEGTPEELK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1064-1261 |
1.17e-04 |
|
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: 46.93 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1064 LTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHINGHISIDGFETSQLGLHDLRRRISIIPQDPVLF-----SGSLRFNL 1138
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFhhltvAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1139 DpFEEKTDEELWLALEAVklkefvsnLKD-GINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNL 1217
Cdd:TIGR01257 1029 Q-LKGRSWEEAQLEMEAM--------LEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221460257 1218 IQEAIHTKFAHCTVLTIAHRLHTV-MDNDRVMVVDMGRVVELGHP 1261
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
764-876 |
1.33e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 45.61 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 764 MILYTFLILCTLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVlaidvnlpQAMMDSI 843
Cdd:cd18572 39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDC--------QKVSDPL 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 221460257 844 EFAVNAL---AVLAVVSTANIWLL-----------IPATVVVALLYG 876
Cdd:cd18572 111 STNLNVFlrnLVQLVGGLAFMFSLswrltllafitVPVIALITKVYG 157
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1048-1241 |
1.33e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.26 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1048 DLRLRYSNhGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALF---RLAHinGHISIDGFETSQLGLHDLrrrISIIP 1124
Cdd:PRK15056 11 DVTVTWRN-GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMgfvRLAS--GKISILGQPTRQALQKNL---VAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QD-------PVLFS-----------GSLRFNLDPFEEKTDEelwlALEAVKLKEFvsnlkdgincRLHDCGaNFSMGQRQ 1186
Cdd:PRK15056 85 QSeevdwsfPVLVEdvvmmgryghmGWLRRAKKRDRQIVTA----ALARVDMVEF----------RHRQIG-ELSGGQKK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1187 LVCLARALLRQNKILIMDEATANVDPETDNLIQEAI-HTKFAHCTVLTIAHRLHTV 1241
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSV 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1181-1238 |
1.74e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 1181 SMGQRQLVCLARALLRQNKILIMDEAT-ANVDPETDNL---IQEaihTKFAHCTVLTIAHRL 1238
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLfrvIRE---LKSQGRGIVYISHRL 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
457-608 |
1.74e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILGEL------------------------------DIISGSVEVngvlSYAPQE----PWLLR 502
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELipnlgdyeeepswdevlkrfrgtelqnyfkKLYNGEIKV----VHKPQYvdliPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 503 GSLRDnILftEPYDEQR----YLEVLRVCH-LDRDVEQLplgdstrvgeggaslSGGQKARVSLARAVYRKADIYLLDDP 577
Cdd:PRK13409 178 GKVRE-LL--KKVDERGkldeVVERLGLENiLDRDISEL---------------SGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|.
gi 221460257 578 LSAVDShVSKMLLDRCLNEFLSKKIRILVTH 608
Cdd:PRK13409 240 TSYLDI-RQRLNVARLIRELAEGKYVLVVEH 269
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
444-591 |
2.27e-04 |
|
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: 45.59 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILG-------ELDII-SGS---------VEVNGVlSYAPQEPWLLRG-SL 505
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwDGEIYwSGSplkasnirdTERAGI-VIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 506 RDNILF----TEPYDEQRYLEVLRVCH-LDRDVeQLPLGDSTR-VGEGGaslsGGQKARVSLARAVYRKADIYLLDDPLS 579
Cdd:TIGR02633 96 AENIFLgneiTLPGGRMAYNAMYLRAKnLLREL-QLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170
....*....|..
gi 221460257 580 AVDSHVSKMLLD 591
Cdd:TIGR02633 171 SLTEKETEILLD 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1061-1254 |
2.30e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1061 LKGLTFTIRGEEKIGIVGHTAAGKSS---IVHALFRLAHINGHISIDGFETSQLGLHDLRRR-ISIIPQDPVL------- 1129
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTlmkVLSGVYPHGTYEGEIIFEGEELQASNIRDTERAgIAIIHQELALvkelsvl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1130 ---FSGSlrfNLDPFEEKTDEELWLalEAVKLKEfvsNLKDGINCRLHDcgANFSMGQRQLVCLARALLRQNKILIMDEA 1206
Cdd:PRK13549 101 eniFLGN---EITPGGIMDYDAMYL--RAQKLLA---QLKLDINPATPV--GNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1207 TANV-DPETDNLIqEAIHTKFAH-CTVLTIAHRLHTVMD-NDRVMVVDMGR 1254
Cdd:PRK13549 171 TASLtESETAVLL-DIIRDLKAHgIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1039-1237 |
2.80e-04 |
|
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: 45.12 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1039 PSGGQLDFRDLRLRYSN------HGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHI-NGHISIDGfetsql 1111
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFENiplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVyGGRLTKPA------ 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1112 glhdlRRRISIIPQDPVLFSGSLRFNL------DPFEEK--TDEELWLALEAVKLKEFVSnlKDGINCRLHDCGANFSMG 1183
Cdd:TIGR00954 514 -----KGKLFYVPQRPYMTLGTLRDQIiypdssEDMKRRglSDKDLEQILDNVQLTHILE--REGGWSAVQDWMDVLSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221460257 1184 QRQLVCLARALLRQNKILIMDEATANVDPETDNLIQEaiHTKFAHCTVLTIAHR 1237
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR--LCREFGITLFSVSHR 638
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
444-636 |
2.81e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVlSYAPQEPWLLRGSLRDNI-LFTEPYDEQRYLE 522
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-DIAKISDAELREVRRKKIaMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 523 VLRVCHLDRDVEQLPLG-------DSTR-VG-EGGA-----SLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKM 588
Cdd:PRK10070 123 VLDNTAFGMELAGINAEerrekalDALRqVGlENYAhsypdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 589 LLDRcLNEFLSKKIR--ILVTHRV-QLLRHVDHLVLLEGGRISVQGHYDAL 636
Cdd:PRK10070 203 MQDE-LVKLQAKHQRtiVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
766-876 |
3.32e-04 |
|
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: 44.04 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 766 LYTFLILCTLIFYV--LRTFG-FFMMTL---RISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDVLAIDVNLPQAM 839
Cdd:cd18573 40 LKTFALALLGVFVVgaAANFGrVYLLRIageRIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 221460257 840 MD---SIEFAVNALAVLAVVS---TANIWLLIPATVVVALLYG 876
Cdd:cd18573 120 SDglrSLVSGVGGIGMMLYISpklTLVMLLVVPPIAVGAVFYG 162
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
446-582 |
4.20e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.84 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 446 DVSFQAQDQQFV-------------GIVGTVGAGKSTLLQVILGELDIISGSVEVNG-VLSYAPQEPWLLRGSLRdnILF 511
Cdd:PRK13638 6 DLWFRYQDEPVLkglnldfslspvtGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkPLDYSKRGLLALRQQVA--TVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 512 TEPyDEQ--------------RYLEVLRVCHLDRDVEQLPLGDSTRVGEGGAS-LSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:PRK13638 84 QDP-EQQifytdidsdiafslRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
....*.
gi 221460257 577 PLSAVD 582
Cdd:PRK13638 163 PTAGLD 168
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
457-575 |
5.06e-04 |
|
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: 44.40 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 457 VGIVGTVGAGKSTLLQVILG----EldiiSGSVEVNGVLSyapqePWLLRGSLRDNI--------LFTEPYDEQRYLEVL 524
Cdd:COG4615 361 VFIVGGNGSGKSTLAKLLTGlyrpE----SGEILLDGQPV-----TADNREAYRQLFsavfsdfhLFDRLLGLDGEADPA 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 525 RVCHLdrdVEQLPLGDSTRVgEGGA----SLSGGQKARVSLARAVYRKADIYLLD 575
Cdd:COG4615 432 RAREL---LERLELDHKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFD 482
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
444-654 |
5.79e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.55 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISG-----SVEVNG--VLSYAP------------QEPWLLRGS 504
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGrsIFNYRDvlefrrrvgmlfQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 505 LRDNILF------TEPYDEQRYLEVLRVChldrdveQLPLGDST--RVGEGGASLSGGQKARVSLARAVYRKADIYLLDD 576
Cdd:PRK14271 117 IMDNVLAgvrahkLVPRKEFRGVAQARLT-------EVGLWDAVkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 577 PLSAVDSHVSKMlLDRCLNEFLSKKIRILVTHRV-QLLRHVDHLVLLEGGRISVQGHYDAL------KKLIRFRMSVAND 649
Cdd:PRK14271 190 PTSALDPTTTEK-IEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLfsspkhAETARYVAGLSGD 268
|
....*
gi 221460257 650 VEVAK 654
Cdd:PRK14271 269 VKDAK 273
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
459-623 |
9.23e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 459 IVGTVGAGKSTLLQVIL----GEL-----------DIIsGSVEVNGVLSyapqepwlLRGSLRDNilftEPYDEQRYLEV 523
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELppnskggahdpKLI-REGEVRAQVK--------LAFENANG----KKYTITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 524 LR---VCHldrdveQlplGDSTR-VGEGGASLSGGQKA------RVSLARAVYRKADIYLLDDPLSAVDS-HVSKMLLDr 592
Cdd:cd03240 94 LEnviFCH------Q---GESNWpLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAE- 163
|
170 180 190
....*....|....*....|....*....|...
gi 221460257 593 CLNEFLSKKIR--ILVTHRVQLLRHVDHLVLLE 623
Cdd:cd03240 164 IIEERKSQKNFqlIVITHDEELVDAADHIYRVE 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
551-627 |
9.93e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.17 E-value: 9.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460257 551 LSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLdRCLNEFLSKKIRILV-THRVQLLRHVDHLVL-LEGGRI 627
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL-RLFEEFNRVGVTVLMaTHDIGLISRRSYRMLtLSDGHL 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1168-1218 |
1.05e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.07 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1168 GINCRLHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNLI 1218
Cdd:PRK10584 135 GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
550-638 |
1.07e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 550 SLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMlldrcLNEFLSK--KIRILVTHRVQLLRH-VDHLVLLEGGR 626
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLW-----LETYLLKwpKTFIVVSHAREFLNTvVTDILHLHGQK 418
|
90
....*....|...
gi 221460257 627 I-SVQGHYDALKK 638
Cdd:PLN03073 419 LvTYKGDYDTFER 431
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
755-876 |
1.20e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 42.62 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 755 EYHRTRLRMMILYTFLILCTL----IFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSD--V 828
Cdd:cd18780 32 SGGEEALRALNQAVLILLGVVligsIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDtqV 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 221460257 829 L--AIDVNLPQAMMdSIEFAVNALAVLAVVStaniWLL-------IPATVVVALLYG 876
Cdd:cd18780 112 LqnAVTVNLSMLLR-YLVQIIGGLVFMFTTS----WKLtlvmlsvVPPLSIGAVIYG 163
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
753-962 |
1.46e-03 |
|
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: 42.05 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 753 IPEYHRTRLRMM-ILYTFLILCTLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFsSDVL-- 829
Cdd:cd18570 33 IPSGDINLLNIIsIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANki 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 830 --AIDVNLPQAMMDSIeFAVNALAVLAVVStaniWLLIPATVVVALLYGcrCLYIGASRSLKRI---ETISRSPIYSHTN 904
Cdd:cd18570 112 reAISSTTISLFLDLL-MVIISGIILFFYN----WKLFLITLLIIPLYI--LIILLFNKPFKKKnreVMESNAELNSYLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221460257 905 ATFKGLATIRALNGTKYM----ERDFHYYQNENTSALYLhVSINRAFAFWTDLICVLYILAV 962
Cdd:cd18570 185 ESLKGIETIKSLNAEEQFlkkiEKKFSKLLKKSFKLGKL-SNLQSSIKGLISLIGSLLILWI 245
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
762-828 |
1.77e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 41.91 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460257 762 RMMILYTFLILCTLIFYVLRTfGFFMMTL-RISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDV 828
Cdd:cd18784 37 RAIIIMGLLAIASSVAAGIRG-GLFTLAMaRLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDT 103
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1076-1259 |
2.21e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.78 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1076 IVGHTAAGKSSIVHALFRLAH-------INGHISIDGFETSQLGLHdlRRRISIIPQDPVLF-----SGSLRFNLDpfee 1143
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRpqkgrivLNGRVLFDAEKGICLPPE--KRRIGYVFQDARLFphykvRGNLRYGMA---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1144 KTDEELW------LALEAVkLKEFVSNLkdgincrlhdcganfSMGQRQLVCLARALLRQNKILIMDEATANVD------ 1211
Cdd:PRK11144 103 KSMVAQFdkivalLGIEPL-LDRYPGSL---------------SGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkre 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221460257 1212 --PETDNLIQEaIHTKfahctVLTIAHRLHTVMD-NDRVMVVDMGRVVELG 1259
Cdd:PRK11144 167 llPYLERLARE-INIP-----ILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1060-1253 |
2.37e-03 |
|
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: 40.94 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1060 ILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAH-INGHISIDGFETSQLGLHDLRRRISIIPQDPVLFSGSLRFNL 1138
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPpLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1139 DPF-EEKTDEELWLALEAVKLKEFVsnlkdgincrlHDCGANFSMGQRQLVCLARALLRQNKILIMDEATANVDPETDNL 1217
Cdd:cd03231 95 RFWhADHSDEQVEEALARVGLNGFE-----------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 221460257 1218 IQEAI--HTKFAHCTVLTIAHRLHTVMDNDRVMvvDMG 1253
Cdd:cd03231 164 FAEAMagHCARGGMVVLTTHQDLGLSEAGAREL--DLG 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
444-631 |
2.82e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 444 IEDVSFQAQDQQFVGIVGTVGAGKS----TLLQVILGELDIISGSVEVNGVlsyaPQEPWLLRGSLRDNIL------FTe 513
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK----PVAPCALRGRKIATIMqnprsaFN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 514 PYDEQRY--LEVLRVCHLDRDVEQLP-------LGDSTRVGEGGA-SLSGGQKARVSLARAVYRKADIYLLDDPLSAVDS 583
Cdd:PRK10418 94 PLHTMHThaRETCLALGKPADDATLTaaleavgLENAARVLKLYPfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221460257 584 HVSKMLLDrclneFLSKKIR------ILVTHRVQLL-RHVDHLVLLEGGRISVQG 631
Cdd:PRK10418 174 VAQARILD-----LLESIVQkralgmLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1048-1262 |
3.13e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1048 DLRLRYSN-HGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHD-LRRRISIIP 1124
Cdd:PRK11288 255 EVRLRLDGlKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTaGQVYLDGKPIDIRSPRDaIRAGIMLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1125 QD-------PVL------------FSGSLRFNLDPFEEKTDEELWLALEAVKlkefVSNLKDGINcrlhdcgaNFSMGQR 1185
Cdd:PRK11288 335 EDrkaegiiPVHsvadninisarrHHLRAGCLINNRWEAENADRFIRSLNIK----TPSREQLIM--------NLSGGNQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1186 QLVCLARALLRQNKILIMDEATANVDPETDNLIQEAIHtKFAH--CTVLTIAHRLHTVMD-NDRVMVVDMGRVV-ELGHP 1261
Cdd:PRK11288 403 QKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIY-ELAAqgVAVLFVSSDLPEVLGvADRIVVMREGRIAgELARE 481
|
.
gi 221460257 1262 H 1262
Cdd:PRK11288 482 Q 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
442-625 |
3.41e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.69 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 442 RHIEDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGVlSYAPQEPwLLRGSLRDNILFTE--PYDEQR 519
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-NYNKLDH-KLAAQLGIGIIYQElsVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 520 YLEVLRVC-HLDRDVEQLPLGD-----------STRVG------EGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAV 581
Cdd:PRK09700 97 VLENLYIGrHLTKKVCGVNIIDwremrvraammLLRVGlkvdldEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221460257 582 -DSHVSK--MLLDRCLNEflSKKIrILVTHRVQLLRHV-DHLVLLEGG 625
Cdd:PRK09700 177 tNKEVDYlfLIMNQLRKE--GTAI-VYISHKLAEIRRIcDRYTVMKDG 221
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
784-828 |
4.27e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 40.78 E-value: 4.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 221460257 784 GFFMMTL-RISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDV 828
Cdd:cd18590 58 GLFMCTLsRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDT 103
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
445-490 |
4.72e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 4.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 221460257 445 EDVSFQAQDQQFVGIVGTVGAGKSTLLQVILGELDIISGSVEVNGV 490
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK 315
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1044-1256 |
6.49e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.78 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1044 LDFRDLRLRySNHGPYILKGLTFTIRGEEKIGIVGHTAAGKSSIVHALFRLAHIN-GHISIDGFETSQLGLHDLRRR-IS 1121
Cdd:COG3845 258 LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAsGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 1122 IIPQDP-----VLfSGSLRFNL-------DPFEEKtdeeLWLALEAVklKEFVSNLKDGINCRLHDCGA---NFSMGQRQ 1186
Cdd:COG3845 337 YIPEDRlgrglVP-DMSVAENLilgryrrPPFSRG----GFLDRKAI--RAFAEELIEEFDVRTPGPDTparSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460257 1187 LVCLARALLRQNKILIMDEATANVDPETdnliQEAIHTKF-----AHCTVLTIAHRLHTVMD-NDRVMVVDMGRVV 1256
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGA----IEFIHQRLlelrdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
530-658 |
6.63e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 530 DRDVEQLPLGDSTrvGEGGASLSGGQKARVSLARAVYRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHR 609
Cdd:NF000106 126 DELLERFSLTEAA--GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQY 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 221460257 610 VQLLRHVDH-LVLLEGGRISVQGHYDALKKLIRFRMSVANDVEVAKLRAM 658
Cdd:NF000106 204 MEEAEQLAHeLTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRM 253
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
765-926 |
7.11e-03 |
|
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: 40.15 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 765 ILYTFLILCTLIFYVLRTFGFFMMTLRISLRIHDQLFQGVIRAFMHFFTLATSGRILNRFSSDV----LAIDVNLPQAMM 840
Cdd:cd18577 51 LYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTnliqDGIGEKLGLLIQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460257 841 DSIEFaVNALAV-------LAVVSTAniwlLIPATVVVALLYGcrclyigasRSLKRIETISRSpIYSHTNA----TFKG 909
Cdd:cd18577 131 SLSTF-IAGFIIafiyswkLTLVLLA----TLPLIAIVGGIMG---------KLLSKYTKKEQE-AYAKAGSiaeeALSS 195
|
170
....*....|....*..
gi 221460257 910 LATIRALNGTKYMERDF 926
Cdd:cd18577 196 IRTVKAFGGEEKEIKRY 212
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
551-620 |
7.12e-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: 38.88 E-value: 7.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221460257 551 LSGGQKARVSLARAV----YRKADIYLLDDPLSAVDSHVSKMLLDRCLNEFLSKKIRILVTHRVQLLRHVDHLV 620
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| |
