|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-906 |
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: 678.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 6 VQIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedpsnperet 85
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 86 aadsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 165
Cdd:TIGR00957 696 ------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQ--AGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI-------- 235
Cdd:TIGR00957 770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRILVTHGISYLPQVDVIIVMSGGKIsemgsyqe 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 236 --QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKETVM----------ERK---APEPSQGLPRAMSSRDGL 293
Cdd:TIGR00957 848 llQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIENGMlvtdvvgkqlQRQlsaSSSDSGDQSRHHGSSAEL 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 294 LLDEDEEEEEAAESEEDDNLSSVlhqRAKIPWractKYLSSAGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALVLSP 373
Cdd:TIGR00957 928 QKAEAKEETWKLMEADKAQTGQV---ELSVYW----DYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGT 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 374 AARNcslsqecALDQSVYAmvftvlcSLGI---ALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILN 450
Cdd:TIGR00957 1001 QNNT-------SLRLSVYG-------ALGIlqgFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVN 1066
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 451 RFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSH 530
Cdd:TIGR00957 1067 RFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSH 1146
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 531 FAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATS-ISNSlhrELSAGLVG 609
Cdd:TIGR00957 1147 FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAvISRH---SLSAGLVG 1223
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 610 LGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSS 684
Cdd:TIGR00957 1224 LSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQIqetapPSGWPPRGRVEFRNYCLRYRED 1297
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 685 LKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIR 764
Cdd:TIGR00957 1298 LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLR 1377
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 765 FNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE 844
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 845 NILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKdSVFASFVR 906
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-907 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 577.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 6 VQIIGGFFTWTPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSgavfwnsslpdsegedpsnpere 84
Cdd:PLN03130 615 ISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS----------------------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 85 taaDSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQR 164
Cdd:PLN03130 672 ---DASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD- 243
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEl 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 244 ------FQrsecQLFEHWKTLMNRQDQELEKE---TVMERKAPEPSQGLPRAMSSRDgllldedeeeeeaaeseEDDNLS 314
Cdd:PLN03130 827 snngplFQ----KLMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKK-----------------KSKEGK 885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 315 SVLHQRAK-----IPWRACTKYLSSAGVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLS--PAARNcslsqecal 386
Cdd:PLN03130 886 SVLIKQEEretgvVSWKVLERYKNALGGAWVVMILFLCYVLTEVFrVSSSTWLSEWTDQGTPKThgPLFYN--------- 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 387 dqSVYAMVF--TVLCSLGIALCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIP 464
Cdd:PLN03130 957 --LIYALLSfgQVLVTLLNSYWLIMS------SLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVA 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 465 STLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF 544
Cdd:PLN03130 1029 VFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAY 1108
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 545 RYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMVSNY 621
Cdd:PLN03130 1109 KAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVmqnGRAENQAAFASTMGLLLSYALNITSL 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 622 LNWMVRNLADMEIQLGAVKRIHTLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALI 696
Cdd:PLN03130 1189 LTAVLRLASLAENSLNAVERVGTYIDLPSE------APLVIennrpPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEI 1262
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 697 APGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDS 776
Cdd:PLN03130 1263 SPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDA 1342
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 777 TLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFA 856
Cdd:PLN03130 1343 DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK 1422
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 857 DRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRA 907
Cdd:PLN03130 1423 SCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-907 |
5.50e-179 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 557.67 E-value: 5.50e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 6 VQIIGGFFTW-TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqrvsgavfwnssLPDSEgedpsnpere 84
Cdd:PLN03232 615 ISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE-------------LSHAE---------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 85 taaDSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQR 164
Cdd:PLN03232 672 ---TSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDF 244
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 245 QRSEcQLFEHWKT---LMNRQDQELEKETVMERKAPEPS-----QGLPRAMSSRDGllldedeeeeeaaeseeddnlSSV 316
Cdd:PLN03232 827 SKSG-SLFKKLMEnagKMDATQEVNTNDENILKLGPTVTidvseRNLGSTKQGKRG---------------------RSV 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 317 L-----HQRAKIPWRACTKYLSSAGVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLSpaarncslsqecaLDQSV 390
Cdd:PLN03232 885 LvkqeeRETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLrVSSSTWLSIWTDQSTPKS-------------YSPGF 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 391 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 470
Cdd:PLN03232 952 YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMF 1031
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 471 SRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARF 550
Cdd:PLN03232 1032 MNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRM 1111
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 551 QQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMVSNYLNWMVR 627
Cdd:PLN03232 1112 AKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTLLSGVLR 1191
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 628 NLADMEIQLGAVKRIHTLLKTEAEsyegllAPSLIPKN-----WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKI 702
Cdd:PLN03232 1192 QASKAENSLNSVERVGNYIDLPSE------ATAIIENNrpvsgWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKV 1265
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 703 GICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEAL 782
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEAL 1345
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 783 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 862
Cdd:PLN03232 1346 ERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLV 1425
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 34784298 863 IAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRA 907
Cdd:PLN03232 1426 IAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-907 |
5.68e-159 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 505.47 E-value: 5.68e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfWNsslpdsegedpsnperetaadsdARSrgpVAYASQ 102
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA-----------------------ERS---IAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDD 182
Cdd:PTZ00243 729 QAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 183 PFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS---------ECQLFE 253
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyatlaaeLKENKD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 254 HWKTLMNRQDQELE----KETVMERKAPEP----SQGLPRAMSSRDGLLLdedeeeeeaaeseeddnlssVLHQRA--KI 323
Cdd:PTZ00243 887 SKEGDADAEVAEVDaapgGAVDHEPPVAKQegnaEGGDGAALDAAAGRLM--------------------TREEKAsgSV 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 324 PWRACTKYLSS-AGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTdsalvlspaarncslSQECALDQSVYAMVFTVLCSLG 402
Cdd:PTZ00243 947 PWSTYVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSMWS---------------TRSFKLSAATYLYVYLGIVLLG 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 403 IA---LCLVTSVTVEWTGlkvAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVS 479
Cdd:PTZ00243 1012 TFsvpLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICS 1088
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 480 ALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTD 559
Cdd:PTZ00243 1089 SILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLD 1168
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 560 SNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELS--AGLVGLGLTYALMVSNYLNWMVRNLADMEIQLG 637
Cdd:PTZ00243 1169 VVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMN 1248
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 638 AVKR----IHTL-------LKTE---AESYEGLLA---------PSLIPKNWP---DQGKIQIQNLSVRYDSSLKPVLKH 691
Cdd:PTZ00243 1249 SVERllyyTDEVphedmpeLDEEvdaLERRTGMAAdvtgtvviePASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRG 1328
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 692 VNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEK 771
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFL 1408
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 772 KCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFI-MDEATASIDMATENILQKV 850
Cdd:PTZ00243 1409 EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQAT 1488
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 851 VMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRA 907
Cdd:PTZ00243 1489 VMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
670-909 |
3.00e-156 |
|
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: 458.60 E-value: 3.00e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 670 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 829
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 830 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRADK 909
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-234 |
1.30e-150 |
|
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: 442.54 E-value: 1.30e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 6 VQIIGGFFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGedpsnperet 85
Cdd:cd03290 1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPS---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 86 AADSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 165
Cdd:cd03290 70 FEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 234
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
350-644 |
2.81e-150 |
|
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: 445.12 E-value: 2.81e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 350 KHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLL 429
Cdd:cd18602 11 KQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 430 NRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 509
Cdd:cd18602 91 RNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 510 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLI 589
Cdd:cd18602 171 RASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 590 AAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHT 644
Cdd:cd18602 251 AALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLE 305
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
670-890 |
8.52e-116 |
|
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: 352.57 E-value: 8.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 670 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 829
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 830 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKP 890
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-909 |
1.01e-107 |
|
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: 364.23 E-value: 1.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 10 GGFFT-WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQrvsgavfwnsslpdsegedPSnperetaaD 88
Cdd:TIGR01271 428 GLFFSnFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE-------------------PS--------E 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 89 SDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 168
Cdd:TIGR01271 481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 248
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 249 ---------CQLFEHWK----------TL--------------------------------------------------- 258
Cdd:TIGR01271 639 pdfsslllgLEAFDNFSaerrnsilteTLrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkfsfv 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 259 ------MNRQDQELEKETVMERK---APEPSQG---LPRAMSSRDGLLLDEDEEEEEAAESEEDDNLSSVLHQRakipwR 326
Cdd:TIGR01271 719 qmgpqkAQATTIEDAVREPSERKfslVPEDEQGeesLPRGNQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQL-----Q 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 327 ACTKYLSSAGVLLLSLLVF-----------------------------------------------SQLLKHMVLVAI-- 357
Cdd:TIGR01271 794 TSFRKKSSITQQNELASELdiysrrlskdsvyeiseeineedlkecfaderenvfetttwntylryITTNRNLVFVLIfc 873
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 358 -DYWLAKWTDSALVL-----SPAARNcSLSQECALDQS---VYAMVFTVLCSLGI------------ALCLVTSVTVEWT 416
Cdd:TIGR01271 874 lVIFLAEVAASLLGLwlitdNPSAPN-YVDQQHANASSpdvQKPVIITPTSAYYIfyiyvgtadsvlALGFFRGLPLVHT 952
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 417 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALL 496
Cdd:TIGR01271 953 LLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAI 1032
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 497 PLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF----RYEARFQQKLLEYTdsnniASLFLTAAN 572
Cdd:TIGR01271 1033 PVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgrqsYFETLFHKALNLHT-----ANWFLYLST 1107
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 573 -RWLEVRMEYIgaCVVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAE 651
Cdd:TIGR01271 1108 lRWFQMRIDII--FVFFFIAVTFIAIGTNQD-GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQE 1184
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 652 SYE-------GLLAPSLIPKN------WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLA 718
Cdd:TIGR01271 1185 EPRpsggggkYQLSTVLVIENphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA 1264
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 719 FFRMVDMfEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGL 798
Cdd:TIGR01271 1265 LLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKL 1343
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 799 DAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMV 878
Cdd:TIGR01271 1344 DFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLV 1423
|
1050 1060 1070
....*....|....*....|....*....|.
gi 34784298 879 LKRGAILEFDKPEKLLSQKDSVFASFVRADK 909
Cdd:TIGR01271 1424 IEGSSVKQYDSIQKLLNETSLFKQAMSAADR 1454
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-234 |
1.99e-104 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 322.11 E-value: 1.99e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 6 VQIIGGFFTWTPDGI---PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpdsegedpsnpe 82
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 83 retaadsdarsrgpVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 162
Cdd:cd03250 68 --------------IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 234
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
391-907 |
7.55e-98 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 318.26 E-value: 7.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 391 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 470
Cdd:COG1132 63 LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 471 SRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 546
Cdd:COG1132 143 VRSVVTLIGALVVLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKAFGR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 547 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMV 626
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 627 RNLADMEIQLGAVKRIHTLLKTEAESYEGLLAPSLIPknwpDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICG 706
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPP----VRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 707 RTGSGKSSF-SLaFFRM------------VDMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 770
Cdd:COG1132 374 PSGSGKSTLvNL-LLRFydptsgrilidgVDI------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 771 KkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 850
Cdd:COG1132 441 A--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 851 VMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASFVRA 907
Cdd:COG1132 519 LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL-ARGGLYARLYRL 574
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
355-643 |
3.65e-90 |
|
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: 287.86 E-value: 3.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 355 VAIDYWLAKWTDSAlvlspaarncslSQECALDQSVYAMVFTVLCSLG-IALCLVTSVTVEWTGLKVAKRLHRSLLNRII 433
Cdd:cd18580 16 QFSNIWLDWWSSDW------------SSSPNSSSGYYLGVYAALLVLAsVLLVLLRWLLFVLAGLRASRRLHDKLLRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 434 LAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVAS 513
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 514 RDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAAT 593
Cdd:cd18580 164 RQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 34784298 594 SIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 643
Cdd:cd18580 244 AV--LLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
351-643 |
1.06e-85 |
|
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: 276.28 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 351 HMVLVAIDYWLAKWTDSALVLSPAA---RNCSLSqecaldqsVYAM--VFTVLCSLGIALCLVTSvtvewtGLKVAKRLH 425
Cdd:cd18603 12 QAFSVGSNIWLSEWSDDPALNGTQDteqRDYRLG--------VYGAlgLGQAIFVFLGSLALALG------CVRASRNLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 426 RSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFI 505
Cdd:cd18603 78 NKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 506 QKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGAC 585
Cdd:cd18603 158 QRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 586 VVLIAAATSIsnsLHRE-LSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 643
Cdd:cd18603 238 IVLFAALFAV---LSRDsLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIK 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
390-906 |
5.48e-82 |
|
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: 279.41 E-value: 5.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 390 VYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLEC 469
Cdd:COG2274 197 VLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 470 LSRSTLLCVSALTVISY----VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 545
Cdd:COG2274 276 ALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQ----SLLVETLRGIETIKALG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 546 YEARFQQK-------LLEYTDSNNIASLFLTAANRWLEVrmeyIGACVVLIAAATSIsnsLHRELSAGlvglGLTYALMV 618
Cdd:COG2274 352 AESRFRRRwenllakYLNARFKLRRLSNLLSTLSGLLQQ----LATVALLWLGAYLV---IDGQLTLG----QLIAFNIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 619 SNYLNWMVRNLADM--EIQ--LGAVKRIHTLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSLKPVLKHVNA 694
Cdd:COG2274 421 SGRFLAPVAQLIGLlqRFQdaKIALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPPVLDNISL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 695 LIAPGQKIGICGRTGSGKSSFS--LAFFRM----------VDMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGT 762
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLklLLGLYEptsgrilidgIDL------------RQIDPASLRRQIGVVLQDVFLFSGT 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 763 IRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASI 839
Cdd:COG2274 565 IRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 840 DMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASFVR 906
Cdd:COG2274 643 DAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL-ARKGLYAELVQ 708
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
351-643 |
1.25e-81 |
|
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: 265.49 E-value: 1.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 351 HMVLVAIDYWLAKWT---DSALVLSPAARNcslsqecaldQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRS 427
Cdd:cd18604 12 QLLSVGQSWWLGIWAsayETSSALPPSEVS----------VLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 428 LLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQK 507
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 508 YFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVV 587
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 588 LIAAATSISNslhRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 643
Cdd:cd18604 242 FATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQ 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
666-890 |
2.53e-79 |
|
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: 255.80 E-value: 2.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 666 WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTL 745
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 746 RSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEiaqlklvvkalpggldaiITEGGENFSQGQRQLFCLARAFVR 825
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 826 KTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKP 890
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
356-643 |
7.73e-76 |
|
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: 249.75 E-value: 7.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 356 AIDYWLAKWTDSAlvlspaarNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILA 435
Cdd:cd18605 17 LIDFWLSYWVSHS--------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 436 PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRD 515
Cdd:cd18605 89 KMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 516 LQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSI 595
Cdd:cd18605 169 LKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 34784298 596 -SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 643
Cdd:cd18605 249 vQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
358-644 |
2.60e-70 |
|
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: 235.54 E-value: 2.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 358 DYWLAKW------TDSALVLSPAARNCSLSQECALD--QSVYAMVFTVLCSLGIALCLVTSVTVewtgLKVAKRLHRSLL 429
Cdd:cd18599 23 DWWLSYWlkqgsgNTTNNVDNSTVDSGNISDNPDLNfyQLVYGGSILVILLLSLIRGFVFVKVT----LRASSRLHNKLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 430 NRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 509
Cdd:cd18599 99 QKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 510 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLI 589
Cdd:cd18599 179 RRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLI 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 590 AAATSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHT 644
Cdd:cd18599 259 TALLVV--LLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILE 311
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
355-643 |
6.39e-69 |
|
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: 230.82 E-value: 6.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 355 VAIDYWLAKWTDSALVLSpaarncslsqecaldQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIIL 434
Cdd:cd18606 16 VFTNLWLSFWTEDFFGLS---------------QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 435 APMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASR 514
Cdd:cd18606 81 APMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 515 DLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASlFLTAAN-RWLEVRMEYIGACVVLIAAAT 593
Cdd:cd18606 161 ELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAY-FLTIANqRWLAIRLDLLGSLLVLIVALL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 34784298 594 SISNSLHreLSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 643
Cdd:cd18606 240 CVTRRFS--ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLL 287
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
670-898 |
2.22e-61 |
|
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: 207.85 E-value: 2.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 670 GKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFSGTIRFNLDPEKKCSDSTLW-EALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 828
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 829 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 898
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
417-897 |
1.59e-60 |
|
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: 216.16 E-value: 1.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 417 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFL 492
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWlsglILL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 493 VA--LLPLAVVcyFIQKYFRVASRdlQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASL---- 566
Cdd:COG4988 166 VTapLIPLFMI--LVGKGAAKASR--RQWRALARLS--GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMkvlr 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 567 --FLTAAnrwleVrME---YIGACVVLIAAATSisnslhreLSAGLVGL--GLTYALMVSNYLNWMvRNL-----ADMEI 634
Cdd:COG4988 240 vaFLSSA-----V-LEffaSLSIALVAVYIGFR--------LLGGSLTLfaALFVLLLAPEFFLPL-RDLgsfyhARANG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 635 qLGAVKRIHTLLKTEAESyeglLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSS 714
Cdd:COG4988 305 -IAAAEKIFALLDAPEPA----APAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 715 FSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVV 791
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPD--ASDEELEAALEAAGLDEFV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 792 KALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL 871
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
490 500
....*....|....*....|....*.
gi 34784298 872 SADLVMVLKRGAILEFDKPEKLLSQK 897
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
358-642 |
1.67e-58 |
|
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: 202.94 E-value: 1.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 358 DYWLAKWTDS-----ALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRI 432
Cdd:cd18601 23 DWWLSYWANLeeklnDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 433 ILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVA 512
Cdd:cd18601 103 LRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 513 SRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA-SLFLTaANRWLEVRMEYIgaCVVLIAA 591
Cdd:cd18601 183 SREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAwFLFLA-TSRWLAVRLDAL--CALFVTV 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 592 ATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 642
Cdd:cd18601 260 VAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
408-903 |
1.13e-53 |
|
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: 196.86 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 408 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISY- 486
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYy 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 487 ---VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTtqlplLSHFA-ETVEGLTTIRAFRYEARFQQKLLEYTDSNN 562
Cdd:TIGR02203 153 swqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQ-----VTTVAeETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 563 IASLFLTAANRWLEVRMEYIG--ACVVLIAAATSISNSlhRELSAG-LVGLGLTYALMVSNylnwmVRNLADMEIQ---- 635
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIAslALAVVLFIALFQAQA--GSLTAGdFTAFITAMIALIRP-----LKSLTNVNAPmqrg 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 636 LGAVKRIHTLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSF 715
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 716 SLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkCSDSTLWEALEIAQLKLVVK 792
Cdd:TIGR02203 375 VNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQ-ADRAEIERALAAAYAQDFVD 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 793 ALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILS 872
Cdd:TIGR02203 454 KLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK 533
|
490 500 510
....*....|....*....|....*....|.
gi 34784298 873 ADLVMVLKRGAILEFDKPEKLLSQkDSVFAS 903
Cdd:TIGR02203 534 ADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
672-882 |
4.47e-50 |
|
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: 174.11 E-value: 4.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVLFSGTIRFNLdpekkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFI 831
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 832 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRG 882
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-248 |
2.62e-47 |
|
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: 178.03 E-value: 2.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNperetaADSDARSRGp 96
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-------GVDLSD------LDPASWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 175
Cdd:COG4988 413 IAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 176 NVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 248
Cdd:COG4988 493 PLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
392-897 |
7.03e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 177.60 E-value: 7.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 392 AMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 471
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 472 RSTLLcVSALTVISYVTP--VFLVALL--PLAVVCYFIQKYF------RVASRdLQQLDDTtqlpllshFAETVEGLTTI 541
Cdd:PRK10790 148 RSAAL-IGAMLVAMFSLDwrMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEVINGMSVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 542 RAFRYEARFQQKLLEYTDSNNIASL-------FLTaanRWLEVRMEYIGACVVLIAAATSisnslhrelSAGLVGLGLTY 614
Cdd:PRK10790 218 QQFRQQARFGERMGEASRSHYMARMqtlrldgFLL---RPLLSLFSALILCGLLMLFGFS---------ASGTIEVGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 615 ALMvsNYLNWMVRNLADMEIQ-------LGAVKRIHTLLKTEAESYegllAPSLIPKNwpdQGKIQIQNLSVRYDSSlKP 687
Cdd:PRK10790 286 AFI--SYLGRLNEPLIELTTQqsmlqqaVVAGERVFELMDGPRQQY----GNDDRPLQ---SGRIDIDNVSFAYRDD-NL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 688 VLKHVNALIAPGQKIGICGRTGSGKSSfsLAFFRM----VDMFEGRIIIDGIdiAKLPLHTLRSRLSIILQDPVLFSGTI 763
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyypLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 764 RFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 843
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 34784298 844 ENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 897
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
672-903 |
7.62e-46 |
|
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: 164.71 E-value: 7.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 828
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 829 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFAS 903
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAE 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
670-909 |
9.79e-46 |
|
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: 165.80 E-value: 9.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 670 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMfEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 829
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 830 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRADK 909
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDR 239
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
351-622 |
1.98e-44 |
|
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: 161.66 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 351 HMVLVAIDYWLAKWTDSALVLSPAARNcslsqecalDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLN 430
Cdd:pfam00664 12 GAISPAFPLVLGRILDVLLPDGDPETQ---------ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 431 RIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFR 510
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 511 VASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA 590
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 34784298 591 AATSISNSLHRELSAGLVGLGLTYALMVSNYL 622
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-240 |
8.16e-44 |
|
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: 170.01 E-value: 8.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnperetAADSDAR 92
Cdd:COG2274 481 FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID-------GID--------LRQIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 S-RGPVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISV 167
Cdd:COG2274 546 SlRRQIGVVLQDVFLFSGTIRENITLGDPdATDEE---IIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
420-905 |
1.48e-42 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 166.44 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 420 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVAL 495
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltmVTLINL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 496 LPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAF---RYEA-RFQQKLLEYTDSN---NIASLF 567
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFaaeEGEAsRFKEALEETLQLNkrkALAYAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 568 LTAANRWLE----VRMEYIGACVVLIAaatsisnslhrELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 643
Cdd:TIGR00958 387 YLWTTSVLGmliqVLVLYYGGQLVLTG-----------KVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVF 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 644 TLL-KTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR 721
Cdd:TIGR00958 456 EYLdRKPNIPLTGTLAPL------NLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 722 MVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPE-KKCSDSTLWEALEIAQLKLVVKALPGGLDA 800
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 801 IITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILSADLVMVLK 880
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLK 687
|
490 500
....*....|....*....|....*
gi 34784298 881 RGAILEFDKPEKLLSQKDsVFASFV 905
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQG-CYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
672-897 |
2.38e-42 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 154.31 E-value: 2.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 828
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 829 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 897
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
672-907 |
9.09e-42 |
|
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: 153.08 E-value: 9.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 750
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 751 IILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 827
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 828 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKdSVFASFVRA 907
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-245 |
1.05e-41 |
|
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: 154.24 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedpsnperetaadsdaRSRGPVA 98
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------------------------KHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 178
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 179 FLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 245
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
401-906 |
1.88e-40 |
|
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: 159.72 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 401 LGIALCLVTSVTVEWTGLKVAKRLHRSL--------LNRIILAPMRFFETTPLGSILNRFSSDcNTIDQHIPSTLECLSR 472
Cdd:TIGR03796 198 LGMGLTALLQGVLTWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTAL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 473 STLLCV-SALTVISYVTPVFLVALLPLAV---VCYFIQKYFRVASRDLQQldDTTQLpllshFAETVEGLTTIR------ 542
Cdd:TIGR03796 277 DAVMLVfYALLMLLYDPVLTLIGIAFAAInvlALQLVSRRRVDANRRLQQ--DAGKL-----TGVAISGLQSIEtlkasg 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 543 ----AFRYEARFQQKLL----EYTDSNNIASL---FLTAAN----------RWLEVRMEyIGACVvliaAATSISNSLHR 601
Cdd:TIGR03796 350 lesdFFSRWAGYQAKLLnaqqELGVLTQILGVlptLLTSLNsalilvvgglRVMEGQLT-IGMLV----AFQSLMSSFLE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 602 ELSaGLVGLGLTyalmvsnylnwmvrnLADMEiqlGAVKRIHTLLKTEAESYEGLLAP--SLIPKNWPDQGKIQIQNLSV 679
Cdd:TIGR03796 425 PVN-NLVGFGGT---------------LQELE---GDLNRLDDVLRNPVDPLLEEPEGsaATSEPPRRLSGYVELRNITF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 680 RYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVD----------MFEGRIIidgidiAKLPLHTLRSRL 749
Cdd:TIGR03796 486 GYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpwsgeiLFDGIPR------EEIPREVLANSV 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFSGTIRFNL---DPekKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRK 826
Cdd:TIGR03796 556 AMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 827 TSIFIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASF 904
Cdd:TIGR03796 634 PSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELW-AVGGAYARL 708
|
..
gi 34784298 905 VR 906
Cdd:TIGR03796 709 IR 710
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-240 |
2.58e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 157.63 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDPsnpeRETAADSdARSR 94
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLLLRFYDPT--SGRILID-------GVDI----RDLTLES-LRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 gpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 170
Cdd:COG1132 416 --IGVVPQDTFLFSGTIRENIRYGRPdATDEE---VEEAAkaaQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:COG1132 491 LLKDPPILILDEATSALDTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-233 |
1.34e-39 |
|
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: 144.45 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsDAR 92
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-------GVDLRDLDLE-----SLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SRgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALY 172
Cdd:cd03228 76 KN--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 173 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 233
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
670-884 |
5.48e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 144.27 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 670 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRK 826
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 827 TSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 884
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-239 |
7.25e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 143.88 E-value: 7.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpDSEGEDPSnperetaadsDAR 92
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT--DIRQLDPA----------DLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SRgpVAYASQKPWLLNATVEENITFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARAL 171
Cdd:cd03245 78 RN--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 239
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-240 |
9.66e-39 |
|
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: 152.61 E-value: 9.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpsnpERETAADSDAR 92
Cdd:COG4987 341 FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG--------------GVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SRGPVAYASQKPWLLNATVEENITFESPfNKQRYKM--VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 170
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELwaALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-240 |
2.31e-38 |
|
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: 143.14 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 12 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDpsnperetAADS 89
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPRFYDVD--SGRILID-------GHD--------VRDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 90 DARS-RGPVAYASQKPWLLNATVEENITFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 165
Cdd:cd03251 70 TLASlRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
408-897 |
2.37e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 148.63 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 408 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV 487
Cdd:PRK11176 84 ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 488 T---PVFLVALLPL-AVVCYFIQKYFRVASRDLQ----QLDDTTQLPL------LSHFAETVEglttirafryEARFQQK 553
Cdd:PRK11176 164 SwqlSLILIVIAPIvSIAIRVVSKRFRNISKNMQntmgQVTTSAEQMLkghkevLIFGGQEVE----------TKRFDKV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 554 lleytdSNNI--ASLFLTAANRWLEVRMEYIGA---CVVLIAAATSisnSLHRELSAGlvglglTYALMVSNYLNWM--V 626
Cdd:PRK11176 234 ------SNRMrqQGMKMVSASSISDPIIQLIASlalAFVLYAASFP---SVMDTLTAG------TITVVFSSMIALMrpL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 627 RNLADMEIQ----LGAVKRIHTLLKTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKI 702
Cdd:PRK11176 299 KSLTNVNAQfqrgMAACQTLFAILDLEQEKDEGKRVIE------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 703 GICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLD--PEKKCSDSTLWE 780
Cdd:PRK11176 373 ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 781 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 860
Cdd:PRK11176 453 AARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
|
490 500 510
....*....|....*....|....*....|....*..
gi 34784298 861 VTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 897
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
427-897 |
8.28e-37 |
|
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: 148.73 E-value: 8.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 427 SLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLeclsRSTLLCVSALTVISYV-----TPVFLVALL--PL- 498
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTI----LSLFLDMWILVIVGLFlvrqnMLLFLLSLLsiPVy 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 499 AVVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYEA-RFQQ----------KLLEYTDSNNIASLF 567
Cdd:TIGR01193 309 AVIIILFKRTFNKLNHDAMQ----ANAVLNSSIIEDLNGIETIKSLTSEAeRYSKidsefgdylnKSFKYQKADQGQQAI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 568 LTAANRWLEVRMEYIGACVVLIAAATsisnslhrelsaglVGLGLTYALMVSNYLNwMVRNLADMEIQLGAVK----RIH 643
Cdd:TIGR01193 385 KAVTKLILNVVILWTGAYLVMRGKLT--------------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvannRLN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 644 TLLKTEAESYEGLLAPSLIPKNwpdqGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV 723
Cdd:TIGR01193 450 EVYLVDSEFINKKKRTELNNLN----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 724 DMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAI 801
Cdd:TIGR01193 525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 802 ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILSADLVMVL 879
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSDKIIVL 681
|
490
....*....|....*...
gi 34784298 880 KRGAILEFDKPEKLLSQK 897
Cdd:TIGR01193 682 DHGKIIEQGSHDELLDRN 699
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
672-896 |
2.73e-36 |
|
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: 137.23 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVLFSGTIRFNL---DPekKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 828
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 829 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 896
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
474-879 |
6.91e-36 |
|
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: 143.58 E-value: 6.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 474 TLLCVSALTVISYVTPVFLVALLPLAVVcYFIQKYFRVASRDLQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQK 553
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPLIPI-FMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 554 LLEYTDSNniaslfltaANRWLEV-RMEYIGACVVLIAAATSISnslhreLSAGLVGLGLTY----------ALMVSNYL 622
Cdd:TIGR02857 209 IRRSSEEY---------RERTMRVlRIAFLSSAVLELFATLSVA------LVAVYIGFRLLAgdldlatglfVLLLAPEF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 623 NWMVRNL-----ADMEIQlGAVKRIHTLLkteaeSYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIA 697
Cdd:TIGR02857 274 YLPLRQLgaqyhARADGV-AAAEALFAVL-----DAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVP 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 698 PGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkcS 774
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--S 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 775 DSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTA 854
Cdd:TIGR02857 425 DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL 504
|
410 420
....*....|....*....|....*
gi 34784298 855 FADRTVVTIAHRVHTILSADLVMVL 879
Cdd:TIGR02857 505 AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
399-906 |
1.09e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 144.71 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 399 CSLGIALCLVTSVTVEWT-GLKVAK-------RLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECL 470
Cdd:TIGR03797 178 IALALLAAAVGAAAFQLAqSLAVLRletrmdaSLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 471 SRSTLLCVSALTVISYVTP---VFLVALLPLAVVCYFIQKYFRVA-SRDLQQLDDTTQLPLLshfaETVEGLTTIR---- 542
Cdd:TIGR03797 257 LLSGIFALLNLGLMFYYSWklaLVAVALALVAIAVTLVLGLLQVRkERRLLELSGKISGLTV----QLINGISKLRvaga 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 543 ---AF-RYEARF-QQKLLEYtDSNNIASlFLTAANRWLEVRmeyigACVVLIAAATSIsnslhreLSAGLVGLG--LTYA 615
Cdd:TIGR03797 333 enrAFaRWAKLFsRQRKLEL-SAQRIEN-LLTVFNAVLPVL-----TSAALFAAAISL-------LGGAGLSLGsfLAFN 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 616 LMVSNYLNWMvRNLADMEIQLGAV----KRIHTLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKH 691
Cdd:TIGR03797 399 TAFGSFSGAV-TQLSNTLISILAViplwERAKPILEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 692 VNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDG----IDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL 767
Cdd:TIGR03797 472 VSLQIEPGEFVAIVGPSGSGKSTL----LRLLLGFETPESGSVfydgQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 768 dpekkCSDSTL-----WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDma 842
Cdd:TIGR03797 548 -----AGGAPLtldeaWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD-- 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 843 teNILQKVVMTAFA--DRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASFVR 906
Cdd:TIGR03797 621 --NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM-AREGLFAQLAR 683
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
620-886 |
1.47e-35 |
|
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: 143.42 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 620 NYLNWMVR----NLADMEiqlgavkRIHTLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSlKPVLKHVNAL 695
Cdd:COG5265 313 NFLGFVYReirqALADME-------RMFDLLDQPPEVADAPDAPPLVVG----GGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 696 IAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkk 772
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPD-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 773 CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM 852
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270
....*....|....*....|....*....|....
gi 34784298 853 TAFADRTVVTIAHRVHTILSADLVMVLKRGAILE 886
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-240 |
1.57e-35 |
|
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: 134.66 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETAadsdaRSRgpVA 98
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-------GIDIRDISRKSL-----RSM--IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLLNATVEENITFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 175
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 176 NVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:cd03254 159 KILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-240 |
6.35e-34 |
|
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: 130.35 E-value: 6.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSlllaTLGEMQR----VSGAVFWNsslpdsegedpsnperetaaDSDAR 92
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydpTSGEILLD--------------------GVDIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 S------RGPVAYASQKPWLLNATVEENITFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQ 163
Cdd:cd03249 69 DlnlrwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 164 RISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-240 |
3.50e-33 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 135.65 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsdarSRGP-VAY 99
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD-------GADLSQWDRE--------ELGRhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWLLNATVEENIT-FESPfNKQRykmVIEACSLqpdIDI------LPHGDQTQIGERGINLSGGQRQRISVARALY 172
Cdd:COG4618 411 LPQDVELFDGTIAENIArFGDA-DPEK---VVAAAKL---AGVhemilrLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 173 QHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAA--IRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-240 |
8.34e-33 |
|
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: 126.96 E-value: 8.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDPsnpeRETAADSDARSR 94
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSILID-------GQDI----REVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 GPVAyasQKPWLLNATVEENITFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 169
Cdd:cd03253 78 GVVP---QDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 170 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:cd03253 151 AILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGT 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-230 |
1.50e-32 |
|
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: 133.57 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedpsnpeRETAADSDARSRGP 96
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--------------VPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENITFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 175
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 176 NVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 230
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
669-907 |
1.28e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 131.24 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 669 QGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSR 748
Cdd:PRK13657 332 KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 749 LSIILQDPVLFSGTIRFNLDPEKK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 827
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 828 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE---FDKpeklLSQKDSVFASF 904
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAAL 566
|
...
gi 34784298 905 VRA 907
Cdd:PRK13657 567 LRA 569
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
390-641 |
1.56e-31 |
|
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: 125.02 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 390 VYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 469
Cdd:cd18559 39 VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 470 LSRSTLLCVSALTVISYVTPVFLVAlLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEAR 549
Cdd:cd18559 119 WMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 550 FQQKLLEYTDsNNIASLFLTAANRWLEVRMEYIGACVVLIAA-ATSISnslhRELSAGLVGLGLTYALMVSNYLNWMVRN 628
Cdd:cd18559 198 FIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASfFAYVS----RHSLAGLVALKVFYSLALTTYLNWPLNM 272
|
250
....*....|...
gi 34784298 629 LADMEIQLGAVKR 641
Cdd:cd18559 273 SPEVITNIVAAEV 285
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-240 |
3.50e-31 |
|
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: 129.84 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEmqrvsgavfwnsslPDS-----EGEDpsnperet 85
Cdd:TIGR02203 338 FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYE--------------PDSgqillDGHD-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 86 AADSDARS-RGPVAYASQKPWLLNATVEENITFESP--FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 162
Cdd:TIGR02203 396 LADYTLASlRRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERGT 550
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
416-642 |
6.34e-31 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 124.14 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 416 TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVAL 495
Cdd:cd18600 97 TLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLAT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 496 LPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFR----YEARFQQKLLEYTdsnniASLFL-TA 570
Cdd:cd18600 177 VPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHT-----ANWFLyLS 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 571 ANRWLEVRMEYIgaCVVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 642
Cdd:cd18600 252 TLRWFQMRIEMI--FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-234 |
3.13e-30 |
|
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: 118.72 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpsnpERETAADSDAR 92
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD--------------GKDLTKLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 162
Cdd:cd03225 73 LRRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 234
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
423-866 |
3.34e-30 |
|
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: 126.32 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 423 RLHRSLLnRIILAPMRFFETtplGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVC 502
Cdd:TIGR02868 91 RVYERLA-RQALAGRRRLRR---GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 503 YFIQKYF-----RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEytdsnniASLFLTAANRwLEV 577
Cdd:TIGR02868 167 GFVAPLVslraaRAAEQALARLRGE----LAAQLTDALDGAAELVASGALPAALAQVEE-------ADRELTRAER-RAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 578 RMEYIGACVVLIAAATSISNSLhreLSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAESYEGLL 657
Cdd:TIGR02868 235 AATALGAALTLLAAGLAVLGAL---WAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 658 APSLI--------PKNWPDQG-KIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEG 728
Cdd:TIGR02868 312 DAAGPvaegsapaAGAVGLGKpTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 729 RIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEG 805
Cdd:TIGR02868 391 EVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRPD--ATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 806 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 866
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-248 |
6.13e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.04 E-value: 6.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnperetaadsdARSRGPV 97
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF-------GKPP------------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRIS 166
Cdd:COG1121 78 GYVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADR-PIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 167 VARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIqREGTLKDFQ 245
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHGPPEEVL 226
|
...
gi 34784298 246 RSE 248
Cdd:COG1121 227 TPE 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-238 |
9.48e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.04 E-value: 9.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsdar 92
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD-------GKPVTGPGPD-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 srgpVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSG 159
Cdd:COG1116 82 ----RGVVFQEpallPWL---TVLDNVALglelrgVPK--AERRERArelLELVGLAGFEDAYPH-----------QLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 160 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAMKD--GT 234
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSArpGR 218
|
....
gi 34784298 235 IQRE 238
Cdd:COG1116 219 IVEE 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-240 |
1.48e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 124.38 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpDSEGEDPSNPERETAADSdarsrgpVAYA 100
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV-------RLDGADLKQWDRETFGKH-------IGYL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLLNATVEENIT-FESPFNKQRykmVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 176
Cdd:TIGR01842 398 PQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 177 VVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-248 |
1.59e-29 |
|
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: 117.59 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSslllaTLGEM-QRV----SGAVFwnsslpdSEGEDpsnpereTAA 87
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKS-----TLTKLiQRFyvpeNGRVL-------VDGHD-------LAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 88 DSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQR 164
Cdd:cd03252 69 ADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDF 244
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
....
gi 34784298 245 QRSE 248
Cdd:cd03252 224 LAEN 227
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
492-896 |
3.50e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 123.67 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 492 LVALLPLAVVCYFIQKY-------FRVASRDLQQLDDTTQlpllshfaetvEGLTTIR---AFRyearfqqklLEYTDSN 561
Cdd:PRK10789 141 LLALLPMPVMAIMIKRYgdqlherFKLAQAAFSSLNDRTQ-----------ESLTSIRmikAFG---------LEDRQSA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 562 NIASLFLTAANRWLEV-RMEYIGACVVLIAAATS------------ISNSLHR-ELSAGLVGLGLTYALMVSnyLNWMVr 627
Cdd:PRK10789 201 LFAADAEDTGKKNMRVaRIDARFDPTIYIAIGMAnllaigggswmvVNGSLTLgQLTSFVMYLGLMIWPMLA--LAWMF- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 628 NLadMEIQLGAVKRIHTLLKTEAESYEGLLApslIPknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGR 707
Cdd:PRK10789 278 NI--VERGSAAYSRIRAMLAEAPVVKDGSEP---VP---EGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 708 TGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpEKKCSDSTLWEALEIAQL 787
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI--ALGRPDATQQEIEHVARL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 788 KLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAfADRTVVTI 863
Cdd:PRK10789 428 ASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWG-EGRTVIIS 506
|
410 420 430
....*....|....*....|....*....|...
gi 34784298 864 AHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 896
Cdd:PRK10789 507 AHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-244 |
3.72e-29 |
|
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: 116.28 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERetaadSDARSRgp 96
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-------GKDITKKNL-----RELRRK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPW--LLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 166
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 167 VARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTIQREGTLKDF 244
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-240 |
5.95e-29 |
|
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: 116.68 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 14 TWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSN-PERETAadsdaR 92
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD-------GRDLASlSRRELA-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SrgpVAYASQK---PWLLnaTVEENI--------TFESPFNKQRYKMVIEACslqpdidilphgDQTQIG---ERGIN-L 157
Cdd:COG1120 76 R---IAYVPQEppaPFGL--TVRELValgryphlGLFGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL-QYLPHADWIIAMKD 232
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKD 213
|
....*...
gi 34784298 233 GTIQREGT 240
Cdd:COG1120 214 GRIVAQGP 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-240 |
4.72e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 120.33 E-value: 4.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ-----RVSGAVFWNSSLPDSegedpsnperetaadsd 90
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIELRELDPESW----------------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 91 arsRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 169
Cdd:PRK11174 422 ---RKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 170 ALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
672-882 |
4.87e-28 |
|
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: 112.18 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDS---SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAffrmvdmfegriiidgiDIAKLPLH----T 744
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA-----------------LLGELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 745 LRSRLSIILQDPVLFSGTIRFN------LDPEKkcsdstLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFC 818
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENilfgkpFDEER------YEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 819 LARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILSADLVMVLKRG 882
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
655-884 |
8.97e-28 |
|
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: 112.18 E-value: 8.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 655 GLLAPSLIpknwpdQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMvdmFEGRIIID 733
Cdd:cd03248 1 GSLAPDHL------KGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF---YQPQGGQV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 734 GIDIAKLPLHT---LRSRLSIILQDPVLFSGTIRFNLD-PEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENF 809
Cdd:cd03248 72 LLDGKPISQYEhkyLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 810 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 884
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-240 |
9.97e-28 |
|
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: 111.82 E-value: 9.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSnpereTAADSDARSRgp 96
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID-------GVDIS-----KIGLHDLRSR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 173
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 174 HTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:cd03244 157 KSKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
23-238 |
1.75e-27 |
|
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: 111.02 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsdarsrgpVAYASQ 102
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD-------GEPVTGPGPD------------RGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 K----PWLlnaTVEENITFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 169
Cdd:cd03293 81 QdallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 170 ALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQRE 238
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQ-LQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
13-248 |
6.05e-27 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 117.54 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQRvsGAVFWNSSlpDSEGEDPSNPEREtaadsd 90
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQVLVDGV--DLAIADPAWLRRQ------ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 91 arsrgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRISV 167
Cdd:TIGR01846 533 ------MGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAI 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 247
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL 681
|
.
gi 34784298 248 E 248
Cdd:TIGR01846 682 Q 682
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
637-907 |
6.67e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 116.87 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 637 GAVKRIHTLLKTEAESYEGllAPSLIPKNWPDQgkIQIQNLSVR-YDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 715
Cdd:PRK11174 319 GAAESLVTFLETPLAHPQQ--GEKELASNDPVT--IEAEDLEILsPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 716 ------------SLaffrMVDMFEGriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWE 780
Cdd:PRK11174 393 lnallgflpyqgSL----KINGIEL---------RELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQ 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 781 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 860
Cdd:PRK11174 458 ALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 34784298 861 VTIAHRVHTILSADLVMVLKRGAILE---FDKpeklLSQKDSVFASFVRA 907
Cdd:PRK11174 538 LMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-239 |
8.22e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 107.91 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETAADSdarsrgpVAYASQ 102
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-------GKDLASLSPKELARK-------IAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 kpwllnatveenitfespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHTNVVFLD 181
Cdd:cd03214 81 --------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 182 DPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 239
Cdd:cd03214 123 EPTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-235 |
1.82e-26 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 108.35 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLATLGEMQRV-SGAVFwnsslpdSEGEDPSN-PERETAADsdarSRGPV 97
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKST-LLNILGGLDRPtSGEVR-------VDGTDISKlSEKELAAF----RRRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLL-NATVEENI----TFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQRQRISV 167
Cdd:cd03255 85 GFVFQSFNLLpDLTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 235
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-286 |
2.57e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 114.81 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAV-FWNSSLPDSEGEDpsnperetaadsdARSRgpVAY 99
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrFHDIPLTKLQLDS-------------WRSR--LAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 178
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 179 FLDDPFSALDVHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKdfqrsecQLFEH-- 254
Cdd:PRK10789 474 ILDDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD-------QLAQQsg 541
|
250 260 270
....*....|....*....|....*....|..
gi 34784298 255 WKTLMNRQdQELEKETvmeRKAPEPSQGLPRA 286
Cdd:PRK10789 542 WYRDMYRY-QQLEAAL---DDAPEIREEAVDA 569
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
23-247 |
3.02e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.23 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnpereTAADSDARSRgpVAYASQ 102
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-------GEDV------ARDPAEVRRR--IGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWL-LNATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARALYQH 174
Cdd:COG1131 81 EPALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKDFQRS 247
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-235 |
8.27e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnpeRETAADSDAR 92
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD-------GKP-----LSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SRgpVAYASQKPWLLNATVEENITF-----ESPFNKQRYKMVIEACSLQPDIdiLphgdQTQIGErginLSGGQRQRISV 167
Cdd:COG4619 74 RQ--VAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI--L----DKPVER----LSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 235
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEEL-LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-239 |
9.63e-26 |
|
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: 106.06 E-value: 9.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsdar 92
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------GRDVTGVPPE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 sRGPVAYASQK----PWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQ 161
Cdd:cd03259 71 -RRNIGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 162 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 239
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-231 |
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: 105.69 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnperetaadsdARSRGPV 97
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-------GKPL------------EKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRIS 166
Cdd:cd03235 71 GYVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 167 VARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 231
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
672-886 |
1.81e-25 |
|
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: 103.93 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPlHTLRSRLSI 751
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVLFSGTIRFNLdpekkcsdstlwealeiaqlklvvkalpggldaiitegGENFSQGQRQLFCLARAFVRKTSIFI 831
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 832 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE 886
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
667-898 |
2.99e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.46 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 667 PDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSS-FSLaFFRMVDMFEGRIIIDGIDIAKLPLHTL 745
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTlLQL-LTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 746 RSRLSIILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQL-KLVvkALPGGLDAIITEGGENFSQGQRQLFCLAR 821
Cdd:PRK11160 413 RQAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLeKLL--EDDKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 822 AFVRKTSIFIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 898
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
23-248 |
3.93e-25 |
|
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: 104.89 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSnperETAADSDARSRGPVAYASQ 102
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-------DGEDIS----GLSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARAL 171
Cdd:cd03261 85 SGALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQR 246
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
..
gi 34784298 247 SE 248
Cdd:cd03261 227 SD 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-243 |
4.28e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 4.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllATLgeMQRvsgavFWNSSlpdsEGE---DPSNPERETAADS 89
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI--ANL--LTR-----FYDID----EGEillDGHDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 90 darsRGPVAYASQKPWLLNATVEENITFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQR 164
Cdd:PRK11176 416 ----RNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 243
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
640-907 |
8.43e-25 |
|
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: 109.84 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 640 KRIHTLLKTEAESYEGLLAPslipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSfsLAf 719
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLP-------RPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKST--LA- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 720 fRM----------------VDMFEGRIIIDGIDIAKLPlhtlrsrlsiilQDPVLFSGTI-----RF-NLDPEKkcsdst 777
Cdd:COG4618 376 -RLlvgvwpptagsvrldgADLSQWDREELGRHIGYLP------------QDVELFDGTIaeniaRFgDADPEK------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 778 lweALEIAQL----KLVVKaLPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT 853
Cdd:COG4618 437 ---VVAAAKLagvhEMILR-LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA 512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 854 AFAD-RTVVTIAHRVHTILSADLVMVLKRGAILEFDKpekllsqKDSVFASFVRA 907
Cdd:COG4618 513 LKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP-------RDEVLARLARP 560
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
672-884 |
9.60e-25 |
|
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: 101.91 E-value: 9.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdmfegriiidgidiAKLPLHTLRsrlsi 751
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTL----------------------ARLILGLLR----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ilqdPVlfSGTIRfnLDpekkCSDSTLWEALEIAQLklvVKALPGglDAIITEG--GEN-FSQGQRQLFCLARAFVRKTS 828
Cdd:cd03246 54 ----PT--SGRVR--LD----GADISQWDPNELGDH---VGYLPQ--DDELFSGsiAENiLSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 829 IFIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 884
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-239 |
1.12e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 103.35 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSNPEREtaadsDARSRGP-VA 98
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF-------DGKDLLKLSRR-----LRKIRRKeIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSGGQRQRI 165
Cdd:cd03257 86 MVFQDPMSsLNPrmTIGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKDGTIQRE 238
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEE 227
|
.
gi 34784298 239 G 239
Cdd:cd03257 228 G 228
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
13-262 |
1.68e-24 |
|
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: 109.66 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSnperetAADSDA- 91
Cdd:TIGR03797 459 FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY-------DGQDLA------GLDVQAv 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 92 -RSRGPVAYASQkpwLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 170
Cdd:TIGR03797 526 rRQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQ 250
Cdd:TIGR03797 603 LVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGL 677
|
250
....*....|..
gi 34784298 251 LFEhwktLMNRQ 262
Cdd:TIGR03797 678 FAQ----LARRQ 685
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-234 |
2.51e-24 |
|
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: 100.01 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETAadsdarsRGPVA 98
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-------GKDIAKLPLEEL-------RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVV 178
Cdd:cd00267 77 YVPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 179 FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 234
Cdd:cd00267 103 LLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
20-238 |
3.62e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.66 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNsslpdseGEDPSnperetAADSDARSR-- 94
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLniLGGL---DRPtSGEVLID-------GQDIS------SLSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 ----GpvaYASQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 162
Cdd:COG1136 85 rrhiG---FVFQFFNLLpELTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 238
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-243 |
3.73e-24 |
|
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: 108.67 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETAadsdarsRGPVA 98
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-------GFSLKDIDRHTL-------RQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLLNATVEENITFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 175
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 176 NVVFLDDPFSALDVhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 243
Cdd:TIGR01193 631 KVLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-240 |
4.63e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.30 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 12 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadSDA 91
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-------GKDLTKLSRR----SLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 92 RSRGPVAYASQKPWL-LNA--TVEENITfESPFN------KQRYKMV---IEACSLQPD-IDILPHGdqtqigerginLS 158
Cdd:COG1123 339 ELRRRVQMVFQDPYSsLNPrmTVGDIIA-EPLRLhgllsrAERRERVaelLERVGLPPDlADRYPHE-----------LS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 159 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMK 231
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI--ADRVAVMY 479
|
....*....
gi 34784298 232 DGTIQREGT 240
Cdd:COG1123 480 DGRIVEDGP 488
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-218 |
7.40e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 106.68 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavfwnsSLPDSEGEDPSNPERETAADSDARSRgP 96
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG-------------LLDPLQGEVTLDGVPVSSLDQDEVRR-R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 175
Cdd:TIGR02868 411 VSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 34784298 176 NVVFLDDPFSALDVHLSDHLmqagiLELLRD--DKRTVVLVTHKL 218
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADEL-----LEDLLAalSGRTVVLITHHL 530
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-247 |
9.35e-24 |
|
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: 101.22 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnpereTAADSDARSRGP 96
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-------GED-------IREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLL-NATVEENIT-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRIS 166
Cdd:cd03295 77 IGYVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 167 VARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQ 245
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
..
gi 34784298 246 RS 247
Cdd:cd03295 225 RS 226
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
21-240 |
1.95e-23 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 105.94 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnssLPDseGEDPSNPEREtaadsDARSRgpVAYA 100
Cdd:TIGR02204 354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRI-----LLD--GVDLRQLDPA-----ELRAR--MALV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLLNATVEENITFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNV 177
Cdd:TIGR02204 420 PQDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 178 VFLDDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:TIGR02204 498 LLLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGT 557
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-239 |
4.87e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 97.00 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETaadsdar 92
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-------GVPVSDLEKAL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 sRGPVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALY 172
Cdd:cd03247 74 -SSLISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 173 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 239
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-247 |
5.10e-23 |
|
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: 99.11 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERetaadsdAR 92
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD-------GRPVTRRRR-------KA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SRGPVAYASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVIEACSLQPDI-DILPHgdqtQigerginLSGGQRQ 163
Cdd:COG1124 77 FRRRVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYPH----Q-------LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 164 RISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 238
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
....*....
gi 34784298 239 GTLKDFQRS 247
Cdd:COG1124 221 LTVADLLAG 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
17-245 |
7.86e-23 |
|
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: 98.41 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegeDPSNPERETAADSDARSRgp 96
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID---------GTDINKLKGKALRQLRRQ-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLN-ATVEENI---------TFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRGINLSGG 160
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 161 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 239
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDG 227
|
....*.
gi 34784298 240 TLKDFQ 245
Cdd:cd03256 228 PPAELT 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-185 |
9.22e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 95.41 E-value: 9.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsdaRSRGPVAYASQ 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD-------GQDLTDDERK-------SLRKEIGYVFQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLLNA-TVEENITFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARALYQHTNV 177
Cdd:pfam00005 67 DPQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKL 142
|
....*...
gi 34784298 178 VFLDDPFS 185
Cdd:pfam00005 143 LLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-235 |
1.04e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.13 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnssLPDseGEDPSnperetAADSDARsRGPVAYA 100
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLD--GADIS------QWDPNEL-GDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVVFL 180
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 181 DDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 235
Cdd:cd03246 121 DEPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-248 |
1.64e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNsslpdseGEDPSNperetaADSDARSRgPVA 98
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLsmISRLLPPD--SGEVLVD-------GLDVAT------TPSRELAK-RLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWL-LNATVEENITF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQRISVARA 170
Cdd:COG4604 79 ILRQENHInSRLTVRELVAFgRFPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDK-RTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 248
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-234 |
5.69e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 93.79 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETAAdsdarSRGPVA 98
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------GEDLTDLEDELPP-----LRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLL-NATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNV 177
Cdd:cd03229 80 MVFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 178 VFLDDPFSALDVhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 234
Cdd:cd03229 122 LLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-250 |
7.24e-22 |
|
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: 95.69 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsdARSRgpV 97
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-------GEDVRKEPRE------ARRQ--I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWL-LNATVEENITFESPFN-------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVAR 169
Cdd:COG4555 77 GVLPDERGLyDRLTVRENIRYFAELYglfdeelKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 170 ALYQHTNVVFLDDPFSALDVhLSDHLMQaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 248
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDV-MARRLLR-EILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEI 223
|
..
gi 34784298 249 CQ 250
Cdd:COG4555 224 GE 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-235 |
1.55e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 94.07 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSS-LPDSEGEdpsnperetaadsdaRSRG 95
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpISQYEHK---------------YLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 172
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 173 QHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 235
Cdd:cd03248 167 RNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-251 |
2.07e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.82 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQRVSGAVFWNsslpdseGEDPsnpereTAADS 89
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLD-------GRDL------LELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 90 DARSRGpVAYASQKPW--LLNATVEENITfESPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 159
Cdd:COG1123 79 ALRGRR-IGMVFQDPMtqLNPVTVGDQIA-EALENlglsraeaRARVLELLEAVGLERRLDRYPH-----------QLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 160 GQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQY-LPHADWIIAMKDGT 234
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergtTVLLITHDLGVvAEIADRVVVMDDGR 220
|
250
....*....|....*..
gi 34784298 235 IQREGTLKDFQRSECQL 251
Cdd:COG1123 221 IVEDGPPEEILAAPQAL 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
672-896 |
3.66e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.05 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD---MFEGRIIIDGIDIAKLPLHTLRSR 748
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 749 LSIILQDP--VLFSGTIRFNLD--PEKKCSDSTLWEALEIAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 824
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 825 RKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQ 896
Cdd:COG1123 159 LDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-909 |
5.72e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 99.33 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 139 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL 218
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 219 QYLPHADWIIAM----------------------------------------KDGTIQREGTLKDFQRSECQLFEH---- 254
Cdd:PTZ00265 641 STIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnNNNKINNAGSYIIEQGTHDALMKNkngi 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 255 WKTLMNRQ--------DQELEKETVMERKAPEPSQGLPRAmSSRDGLLLDEDEEEEEAAESEEDDNLSSVLHQRAKIPW- 325
Cdd:PTZ00265 721 YYTMINNQkvsskkssNNDNDKDSDMKSSAYKDSERGYDP-DEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFl 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 326 -RACTKYLSSAGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECALDQ-----SVYAMVftvlc 399
Cdd:PTZ00265 800 rNLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEAnsnkySLYILV----- 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 400 slgIALCLVTSVTVE-----WTGLKVAKRLHRSLLNRIILAPMRFFEttplgsilnrfsSDCNT---IDQHIPSTLECLS 471
Cdd:PTZ00265 875 ---IAIAMFISETLKnyynnVIGEKVEKTMKRRLFENILYQEISFFD------------QDKHApglLSAHINRDVHLLK 939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 472 RSTllcVSALTVISYVTPVFLVALLplavvcyfIQKYFrvasrdlqqlddttqLPLLshfAETVEGLTTI--RAFRYEAR 549
Cdd:PTZ00265 940 TGL---VNNIVIFTHFIVLFLVSMV--------MSFYF---------------CPIV---AAVLTGTYFIfmRVFAIRAR 990
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 550 F-QQKLLEYTDSNNIASLFLTAAN-------RWLEVRMEYIGACVV----------LIAAATSISNSLHRE---LSAGLV 608
Cdd:PTZ00265 991 LtANKDVEKKEINQPGTVFAYNSDdeifkdpSFLIQEAFYNMNTVIiygledyfcnLIEKAIDYSNKGQKRktlVNSMLW 1070
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 609 GLGLTYALMVSNYLNWmvrnLADMEIQLGAV------KRIHTLLKTEaeSYEGLLA-----------------PSLIPKN 665
Cdd:PTZ00265 1071 GFSQSAQLFINSFAYW----FGSFLIRRGTIlvddfmKSLFTFLFTG--SYAGKLMslkgdsenaklsfekyyPLIIRKS 1144
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 666 WPD---------------QGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDM---- 725
Cdd:PTZ00265 1145 NIDvrdnggiriknkndiKGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndh 1224
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 726 ---------------------------------FEGRIIIDGIDIAKL-----------------PLHTLRSRLSIILQD 755
Cdd:PTZ00265 1225 hivfknehtndmtneqdyqgdeeqnvgmknvneFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDLRNLFSIVSQE 1304
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 756 PVLFSGTIRFNLDPEKKcsDSTLWE---ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIM 832
Cdd:PTZ00265 1305 PMLFNMSIYENIKFGKE--DATREDvkrACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLL 1382
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 833 DEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILSADLVMVL----KRGAILEFDKP-EKLLSQKDSVFASFV 905
Cdd:PTZ00265 1383 DEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGThEELLSVQDGVYKKYV 1462
|
....
gi 34784298 906 RADK 909
Cdd:PTZ00265 1463 KLAK 1466
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
673-882 |
5.84e-21 |
|
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: 90.38 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 673 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 752
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 753 LQdpvlfsgtirfnldpekkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIM 832
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 34784298 833 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTI-LSADLVMVLKRG 882
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
672-898 |
1.04e-20 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 92.01 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAF------------FRMVDMfegriiidgidiAK 739
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsgevlVDGKDI------------TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 740 LPLHTLRSRLSIILQDPV--LFSGTIR---------FNLDPEkkcsdstlwEALEIAQ--LKLVvkalpgGLDAIITEGG 806
Cdd:COG1122 68 KNLRELRRKVGLVFQNPDdqLFAPTVEedvafgpenLGLPRE---------EIRERVEeaLELV------GLEHLADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 807 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAI 884
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
250
....*....|....
gi 34784298 885 LEFDKPEKLLSQKD 898
Cdd:COG1122 213 VADGTPREVFSDYE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
23-235 |
2.88e-20 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 88.99 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEREtaadsdARSRgpVAYASQ 102
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-------GKDIKKEPEE------VKRR--IGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLL-NATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLD 181
Cdd:cd03230 81 EPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 182 DPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 235
Cdd:cd03230 121 EPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-235 |
4.07e-20 |
|
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: 89.39 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 15 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpDSEGEDPSNPEREtaadsDARSR 94
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-------EIDGIDISTIPLE-----DLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 gpVAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQH 174
Cdd:cd03369 84 --LTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 175 TNVVFLDDPFSALDVHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 235
Cdd:cd03369 144 PRVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
672-893 |
5.49e-20 |
|
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: 89.55 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRII--------IDGIDIAKLPLH 743
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDegevlldgKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 744 tLRSRLSIILQDPVLFSGTIRFNLD--------PEKKCSDSTLWEALEIAQLKLVVKALPGGLDaiiteggenFSQGQRQ 815
Cdd:cd03260 79 -LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 816 LFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKL 893
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-240 |
6.13e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.44 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNsslpdseGEDpsnperetAADSDARSRG 95
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrmIAGLEDPT--SGEILIG-------GRD--------VTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 pVAYASQKPWLL-NATVEENITF------ESPfnKQRYKMVIEAcslqpdIDILphgdqtQIGE----RGINLSGGQRQR 164
Cdd:COG3839 77 -IAMVFQSYALYpHMTVYENIAFplklrkVPK--AEIDRRVREA------AELL------GLEDlldrKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQRE 238
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVE-MRAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQV 215
|
..
gi 34784298 239 GT 240
Cdd:COG3839 216 GT 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
23-248 |
1.50e-19 |
|
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: 88.88 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGED-PSNPERETAAdsdARSRgpVAYAS 101
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-------GQDiTGLSEKELYE---LRRR--IGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 102 QKPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARA 170
Cdd:COG1127 89 QGGALFDSlTVFENVAF--PLRehtdlseaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLS---DHLmqagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQR 246
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSaviDEL----IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
..
gi 34784298 247 SE 248
Cdd:COG1127 232 SD 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
23-254 |
1.54e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.98 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgEMQRvSGAVFWNsslpdseGEDpsnpereTAADSDARSRGpVAYA 100
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLriIAGL-ETPD-SGRIVLN-------GRD-------LFTNLPPRERR-VGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLL-NATVEENITF----ESPFNKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 172
Cdd:COG1118 81 FQHYALFpHMTVAENIAFglrvRPPSKAEIRARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 173 QHTNVVFLDDPFSALDVHLSDHLMQaGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDfqrsecqL 251
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRR-WLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE-------V 221
|
...
gi 34784298 252 FEH 254
Cdd:COG1118 222 YDR 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-242 |
1.59e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.02 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnssLPDseGEDPSnperetaaDSDARS-RG 95
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-----LLD--GVPLV--------QYDHHYlHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLLNATVEENITFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 174
Cdd:TIGR00958 556 QVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 175 TNVVFLDDPFSALDVHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 242
Cdd:TIGR00958 636 PRVLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-216 |
2.48e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 87.15 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnperetaADSDARSRGPVAYASQ 102
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-------GEPI--------RDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLLNA-TVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHTN 176
Cdd:COG4133 83 ADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 34784298 177 VVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTH 216
Cdd:COG4133 152 LWLLDEPFTALDAAGVALL--AELIAAHLARGGAVLLTTH 189
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-253 |
3.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.65 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEdpsnperetaadSDAR 92
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF------------EKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 93 SRGPVAYASQKPWLLNATVEENITFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQRISVARA 170
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQ 250
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
...
gi 34784298 251 LFE 253
Cdd:PRK13648 236 LTR 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-219 |
4.52e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 87.24 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNSSLPDSEGEDPSNPEREtaadsdarsrgpV 97
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELRRR------------V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLLNATVEENITF------ESPfNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQRQRISVA 168
Cdd:cd03260 84 GMVFQKPNPFPGSIYDNVAYglrlhgIKL-KEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQQRLCLA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 219
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-240 |
8.90e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATlgemqRvsgavFWNsslPDSeGEDPSNpERETAADSDA 91
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLqLLT-----R-----AWD---PQQ-GEILLN-GQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 92 RSRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQRISVARA 170
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD---DKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaqNK-TVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
672-896 |
1.18e-18 |
|
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: 86.45 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPLHtLRS 747
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMLAGLLKpdsgSILIDGEDVRKEPRE-ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 748 RLSIILQDPVLFSG-TIRFNLD---PEKKCSDSTLWEALEIaqlklVVKALpgGLDAIITEGGENFSQGQRQLFCLARAF 823
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIEE-----LIELL--GLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 824 VRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQ 896
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-218 |
1.34e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.59 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedpsnpERETAAdsdarsrgPV 97
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------------RRAGGA--------RV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQK---PWLLNATVEENITF-----ESPFNKQRY--KMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISV 167
Cdd:NF040873 58 AYVPQRsevPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGLADLAG---RQLGE----LSGGQRQRALL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTHKL 218
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDL 179
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-240 |
1.37e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.23 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSN--PERetaadsdarsRg 95
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-------GRDVTGlpPEK----------R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQR 164
Cdd:COG3842 78 NVGMVFQDyalfPHL---TVAENVAFglrmrgVPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKlQY--LPHADWIIAMKDGTIQREGT 240
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREE-MREELRRLQRELGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
673-882 |
2.19e-18 |
|
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: 84.44 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 673 QIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 752
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 753 LQDP--VLFSGTIR---------FNLDPEKkcSDSTLWEALEIAQLKLVVKALPggldaiiteggENFSQGQRQLFCLAR 821
Cdd:cd03225 81 FQNPddQFFGPTVEeevafglenLGLPEEE--IEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 822 AFVRKTSIFIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILS-ADLVMVLKRG 882
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-235 |
2.21e-18 |
|
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: 83.25 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNsslpdseGEdpsnpERETAADSDARSRGp 96
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMkiLS--GLYKPDSGEILVD-------GK-----EVSFASPRDARRAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTN 176
Cdd:cd03216 77 IAMVYQ------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 177 VVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 235
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
13-240 |
2.30e-18 |
|
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: 90.39 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLgeMQRVSGAVFWnsslpdsEGEDPSNPERETAADSd 90
Cdd:TIGR03796 485 FGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILF-------DGIPREEIPREVLANS- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 91 arsrgpVAYASQKPWLLNATVEENITFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISV 167
Cdd:TIGR03796 555 ------VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEI 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-235 |
2.88e-18 |
|
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: 89.36 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 1 ADNFCV--QIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGeMQRVSGAVFWNsslpdseGEDP 78
Cdd:COG4172 278 ARDLKVwfPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFD-------GQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 79 SNpeRETAADSDARSRGPVA----YASQKPWLlnaTVEENIT------FESPFNKQRYKMVIEACS---LQPD-IDILPH 144
Cdd:COG4172 350 DG--LSRRALRPLRRRMQVVfqdpFGSLSPRM---TVGQIIAeglrvhGPGLSAAERRARVAEALEevgLDPAaRHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 145 gdqtqigErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKLQ- 219
Cdd:COG4172 425 -------E----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-----QAQILDLLRDlqREHglAYLFISHDLAv 488
|
250
....*....|....*...
gi 34784298 220 --YLphADWIIAMKDGTI 235
Cdd:COG4172 489 vrAL--AHRVMVMKDGKV 504
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-240 |
3.70e-18 |
|
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: 89.11 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDPsnpeRETAADSDARSRGPVA 98
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRILID-------GQDI----RDVTQASLRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 yasQKPWLLNATVEENItfespfnkqRY----------KMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 168
Cdd:COG5265 439 ---QDTVLFNDTIAYNI---------AYgrpdaseeevEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSR-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-234 |
5.50e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.71 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavFWNS-----SLPDSEGedpsnperetaadsd 90
Cdd:COG4178 372 TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---------LWPYgsgriARPAGAR--------------- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 91 arsrgpVAYASQKPWLLNATVEENITF---ESPFNKQRYKMVIEACSLQpdiDILPHGDQTQIGERGinLSGGQRQRISV 167
Cdd:COG4178 428 ------VLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLG---HLAERLDEEADWDQV--LSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGT 234
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-230 |
7.94e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRvsGAVFWnsslpdsEGEDPS--NPERetaadsdarS 93
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLkiVASLISPTS--GTLLF-------EGEDIStlKPEI---------Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 RGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQRISVA 168
Cdd:PRK10247 80 RQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 230
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-244 |
1.90e-17 |
|
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: 82.10 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDpsnperETAADSDARSRGPVA 98
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-------DGRD------ITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLL-NATVEENITF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARALYQHT 175
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 176 NVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 244
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-239 |
2.01e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 81.77 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 30 IPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnperETAADSDARsrgPVAYASQKPWLL-N 108
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-------GVD------VTAAPPADR---PVSMLFQENNLFaH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 109 ATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHTNVVFLD 181
Cdd:cd03298 85 LTVEQNVGLGlspglklTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 182 DPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 239
Cdd:cd03298 154 EPFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-248 |
4.12e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.34 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 22 TLSNITIR-----------IPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnperETAADSD 90
Cdd:COG3840 3 RLDDLTYRygdfplrfdltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-------GQD------LTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 91 ARsrgPVAYASQK----PWLlnaTVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgDQtqigerginLSG 159
Cdd:COG3840 70 ER---PVSMLFQEnnlfPHL---TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 160 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQRE 238
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQE-MLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAAD 211
|
250
....*....|
gi 34784298 239 GTLKDFQRSE 248
Cdd:COG3840 212 GPTAALLDGE 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-240 |
4.25e-17 |
|
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: 81.62 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnperetAADSDARSRGpV 97
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-------GED--------ATDVPVQERN-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 165
Cdd:cd03296 77 GFVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 240
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-219 |
4.33e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAV-FWNSSLPDSEgEDPSnperetaadsDARSRgp 96
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVtFHGKNLYAPD-VDPV----------EVRRR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENITFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVARALYQH 174
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 34784298 175 TNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHKLQ 219
Cdd:PRK14243 170 PEVILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQ 211
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
25-247 |
5.14e-17 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 85.71 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQRVSGavfwnsslPDS-----EGEDPSNPERETAadsdarsRGPVAY 99
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYD--------PTVgqiliDGIDINTVTRESL-------RKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWLLNATVEENITF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNV 177
Cdd:TIGR01192 414 VFQDAGLFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 178 VFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 247
Cdd:TIGR01192 493 LVLDEATSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
664-879 |
5.44e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 664 KNWPDQGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAK-LP 741
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 742 LHTLRSRLSIILQDPVLFSGTIRFN----------------------------LDPEKKC--------------SDSTLW 779
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdlealsnyynedgndsqenKNKRNSCrakcagdlndmsntTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 780 -------------EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 843
Cdd:PTZ00265 535 iemrknyqtikdsEVVDVSKKVLIhdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|....*...
gi 34784298 844 ENILQKVV--MTAFADRTVVTIAHRVHTILSADLVMVL 879
Cdd:PTZ00265 615 EYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-248 |
6.66e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPsnpeRETAADSDARSRGPVAYasqkp 104
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-------DGEHI----QHYASKEVARRIGLLAQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 105 wllNATVEENITFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQRISVARAL 171
Cdd:PRK10253 89 ---NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 172 YQHTNVVFLDDPFSALDVhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQR 246
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT 233
|
..
gi 34784298 247 SE 248
Cdd:PRK10253 234 AE 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
689-837 |
9.61e-17 |
|
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: 78.07 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 689 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL 767
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 768 -------DPEKKCSDSTLWEALEiaqlKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 837
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALE----KL---GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-240 |
1.02e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQRVSGAVFWNSSLPDSEGEDPSNPERE------------- 84
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVmsLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEqnvgmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 85 TAADSDARS-------------------------RGPVAYASQKPWLLNATVEENITF-ESPFNKQRYKMVIEACSLQPD 138
Cdd:PTZ00265 1261 TKEGGSGEDstvfknsgkilldgvdicdynlkdlRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 139 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKL 218
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
250 260
....*....|....*....|....*..
gi 34784298 219 QYLPHADWIIAM----KDGT-IQREGT 240
Cdd:PTZ00265 1420 ASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-239 |
1.17e-16 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 79.61 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnperetAADSDARSRGpV 97
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-------GRD--------VTDLPPKDRD-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLL-NATVEENITFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQRISVARA 170
Cdd:cd03301 75 AMVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 239
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-243 |
1.47e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.97 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSN---PERetaadsdarsr 94
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL-------DGKDITNlppHKR----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 gPVAYASQKPWLL-NATVEENITF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISV 167
Cdd:cd03300 73 -PVNTVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 243
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
491-906 |
1.54e-16 |
|
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: 85.00 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 491 FLVALLPLAVVCYFIQKYFRVASRDLQQlddtTQLPLLShfaETVEGLTTIRAFRYEARFQQKLLEYTDSNniASLFLTA 570
Cdd:TIGR00957 466 VMVLMVPLNAVMAMKTKTYQVAHMKSKD----NRIKLMN---EILNGIKVLKLYAWELAFLDKVEGIRQEE--LKVLKKS 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 571 AnrWLEVRMEYIGAC----VVLIAAATSISNSLHRELSA--GLVGLGLTYALMVS-NYLNWMVRNLADMEIQLgavKRIH 643
Cdd:TIGR00957 537 A--YLHAVGTFTWVCtpflVALITFAVYVTVDENNILDAekAFVSLALFNILRFPlNILPMVISSIVQASVSL---KRLR 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 644 TLLKTEAesyeglLAPSLIPKNWPDQGK---IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFF 720
Cdd:TIGR00957 612 IFLSHEE------LEPDSIERRTIKPGEgnsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 721 RMVDMFEGRIiidgidiaklplhTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDA 800
Cdd:TIGR00957 686 AEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRT 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 801 IITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQKVV--MTAFADRTVVTIAHRVHTILSADLVM 877
Cdd:TIGR00957 753 EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVII 832
|
410 420
....*....|....*....|....*....
gi 34784298 878 VLKRGAILEFDKPEKLLsQKDSVFASFVR 906
Cdd:TIGR00957 833 VMSGGKISEMGSYQELL-QRDGAFAEFLR 860
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-243 |
2.05e-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: 79.55 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMQRvSGAVFWN----SSLPDSEgedpsnpEREtaa 87
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrCINGLERPT-SGSVLVDgtdlTLLSGKE-------LRK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 88 dsdARSRgpVAYASQKPWLLNA-TVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 159
Cdd:cd03258 80 ---ARRR--IGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 160 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGT 234
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGE 218
|
....*....
gi 34784298 235 IQREGTLKD 243
Cdd:cd03258 219 VVEEGTVEE 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
672-887 |
2.37e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.09 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------MFEGRIIIDGIDIAKLPLh 743
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLSRRLRKIR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 744 tlRSRLSIILQDPvlFSgtirfNLDPEKKCSDStLWEALEI--------AQLKLVVKALPG-GLDAII-----TEggenF 809
Cdd:cd03257 81 --RKEIQMVFQDP--MS-----SLNPRMTIGEQ-IAEPLRIhgklskkeARKEAVLLLLVGvGLPEEVlnrypHE----L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 810 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVMVLKRGAI 884
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
...
gi 34784298 885 LEF 887
Cdd:cd03257 225 VEE 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-216 |
2.53e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.19 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsSLPDSEGedpsnperetaadsdarsrg 95
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMPEGED-------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 pVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidILPHGDqtqigergiNLSGGQRQRISVARALYQHT 175
Cdd:cd03223 66 -LLFLPQRPYLPLGTLREQL-------------------------IYPWDD---------VLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 34784298 176 NVVFLDDPFSALDVHLSDHLMQagileLLRDDKRTVVLVTH 216
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-216 |
2.66e-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: 78.60 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNpERETAADSDARSRGp 96
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-------GQDVSD-LRGRAIPYLRRKIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKpWLLNATVEENITF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVAR 169
Cdd:cd03292 82 VVFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 34784298 170 ALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD-DKR--TVVLVTH 216
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTT-----WEIMNLLKKiNKAgtTVVVATH 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-243 |
3.06e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDsegedpsnpereTAADSDARSRGP 96
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID------------YSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRIS 166
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSF-GAVNlklpedevRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 167 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 243
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-240 |
3.14e-16 |
|
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: 79.61 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSNperetAADSDARS--RGPVAYASQ 102
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-------DGQDIAA-----MSRKELRElrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLL-NATVEENITF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQH 174
Cdd:cd03294 110 SFALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 175 TNVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 240
Cdd:cd03294 179 PDILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-240 |
3.45e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.09 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQRV----SGAVfwnssLPDseGEDPSNPERETAadsdarsRGP 96
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQRVfdpqSGRI-----LID--GTDIRTVTRASL-------RRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENITFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 174
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-240 |
4.18e-16 |
|
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: 80.62 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 38 IVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSN--PERetaadsdaRSRGPV--AYAsqkpWLLNATVEE 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD-------GEDVTNvpPHL--------RHINMVfqSYA----LFPHMTVEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 114 NITFESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHTNVVFLDDPFS 185
Cdd:TIGR01187 62 NVAFGLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 186 ALDVHLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 240
Cdd:TIGR01187 130 ALDKKLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
672-883 |
4.42e-16 |
|
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: 78.14 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRI--IIDGIDIAKLPLHTLRSRL 749
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIIL--QDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 827
Cdd:cd03290 80 SVAYaaQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 828 SIFIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVMVLKRGA 883
Cdd:cd03290 160 NIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-216 |
4.80e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.14 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavFwnssLPDSEGEDPSNPERETAADSDarsRGPVAya 100
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAG---------F----LAPSSGEITLDGVPVTGPGAD---RGVVF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 sQK----PWLlnaTVEENITFESPFNK----QRYKMVIEACSLqpdIDiLPHGDQTQIGErginLSGGQRQRISVARALY 172
Cdd:COG4525 83 -QKdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VG-LADFARRRIWQ----LSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 34784298 173 QHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTH 216
Cdd:COG4525 151 ADPRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-230 |
5.44e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.52 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGAVFWN----SSLPdsegedpsnPERet 85
Cdd:COG4136 7 LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNgrrlTALP---------AEQ-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 86 aadsdarsRGpVAYASQKPWLL-NATVEENITF---ESPFNKQRYKMVIEAcsLQpDIDiLPHgdqtqIGERGIN-LSGG 160
Cdd:COG4136 76 --------RR-IGILFQDDLLFpHLSVGENLAFalpPTIGRAQRRARVEQA--LE-EAG-LAG-----FADRDPAtLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 161 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 230
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQ-FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-239 |
6.53e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 77.72 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 33 GQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNSS-----LPdsegedpsnPERetaadsdarsRGpVAYASQ 102
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLrciagLEKPDGGTIVLNGTVLFDSrkkinLP---------PQQ----------RK-IGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLL-NATVEENITFESPFNKQRYKMVIEAcslqpdiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNVVFL 180
Cdd:cd03297 83 QYALFpHLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 181 DDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 239
Cdd:cd03297 156 DEPFSALDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-240 |
1.22e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.30 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavfwnsSLPDSEGE---DpsnpERETAADSDARSR 94
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG-------------YYPLTEGEirlD----GRPLSSLSHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 GPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 174
Cdd:PRK10790 415 QGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-237 |
1.71e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQRVSGAVFWNSslpdseGEDPSNPERETAAdsdARSRGPVAYASQ 102
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTYRVA------GQDVATLDADALA---QLRREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLL-NATVEENITFESPF-------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQH 174
Cdd:PRK10535 94 RYHLLsHLTAAQNVEVPAVYaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 237
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-243 |
1.88e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEdpsnperetAADSDARS--- 93
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-------IKGE---------PIKYDKKSlle 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 -RGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 162
Cdd:PRK13639 76 vRKTVGIVFQNPddQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTL 241
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTP 221
|
..
gi 34784298 242 KD 243
Cdd:PRK13639 222 KE 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-244 |
1.94e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.38 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---RVSGAV-FWNSSLPdsegedpsnpERETA 86
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRVeFFNQNIY----------ERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 87 ADsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGINLSGGQ 161
Cdd:PRK14258 83 LN---RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 162 RQRISVARALYQHTNVVFLDDPFSALDVHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 238
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
....*.
gi 34784298 239 GTLKDF 244
Cdd:PRK14258 232 GQLVEF 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-240 |
2.40e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.98 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedpsNPERETAADSDARSrgpVAYASQ 102
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-----------KPISMLSSRQLARR---LALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPwllnaTVEENITFE-------SPFNK------QRYKMVIEAcSLQpdidilphgdQTQIGE----RGINLSGGQRQRI 165
Cdd:PRK11231 84 HH-----LTPEGITVRelvaygrSPWLSlwgrlsAEDNARVNQ-AME----------QTRINHladrRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-243 |
2.77e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 76.22 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSN--PERETaadsdarsrgpVAYA 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN-------GKDITNlpPEKRD-----------ISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLL-NATVEENITF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARALYQH 174
Cdd:cd03299 77 PQNYALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 243
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-248 |
3.38e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.98 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdSEGEDPSNPERETAADSDARSRgpVAYASQ 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--------TIGERVITAGKKNKKLKPLRKK--VGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALY 172
Cdd:PRK13634 93 FPehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 173 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKD-FQRS 247
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREiFADP 237
|
.
gi 34784298 248 E 248
Cdd:PRK13634 238 D 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-217 |
4.00e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.39 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGAVFWNSSlpdsegedPSNPeretaadsdARSRGPVAY 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ--------PRKP---------DQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWLL-NATVEENITFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQRISVARA 170
Cdd:cd03234 86 VRQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHK 217
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
410-642 |
4.37e-15 |
|
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: 76.69 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 410 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV-- 487
Cdd:cd18552 60 TYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdw 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 488 --TPVFLVALLPLAVVCYFIQKYFRVASRDLQ-QLDDttqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN--- 561
Cdd:cd18552 140 klTLIALVVLPLAALPIRRIGKRLRKISRRSQeSMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLrrl 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 562 NIASLFLTAANRWLevrMEYIGACVVLIAAATSISNSLHRELSAG-LVGLgLTYALMVSNYLnwmvRNLADM--EIQ--L 636
Cdd:cd18552 215 SMKIARARALSSPL---MELLGAIAIALVLWYGGYQVISGELTPGeFISF-ITALLLLYQPI----KRLSNVnaNLQrgL 286
|
....*.
gi 34784298 637 GAVKRI 642
Cdd:cd18552 287 AAAERI 292
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
668-898 |
4.64e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.18 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 668 DQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRS 747
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 748 RLSIILQDP-VLFSGT-----IRFNLdpEKKCSDSTLWEALeIAQLKLVVkalpgGLDAIITEGGENFSQGQRQLFCLAR 821
Cdd:PRK13632 84 KIGIIFQNPdNQFIGAtveddIAFGL--ENKKVPPKKMKDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 822 AFVRKTSIFIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 898
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-264 |
8.90e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemQRVSGAVFWNSSlPDSEGEDPSNP-ERETAADSDAR-SRGPVAYA 100
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKS-AGSHIELLGRTvQREGRLARDIRkSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLLNA-TVEENITF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQRISVAR 169
Cdd:PRK09984 92 FQQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 170 ALYQHTNVVFLDDPFSALDVHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 244
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
250 260
....*....|....*....|
gi 34784298 245 QRSEcqlFEHWKTLMNRQDQ 264
Cdd:PRK09984 241 DNER---FDHLYRSINRVEE 257
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
14-239 |
1.04e-14 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 74.13 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 14 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpDSEGEDPSnperetaadsdars 93
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPY-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 RGPVAYASQKPWLL-NATVEENITFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRI 165
Cdd:TIGR01277 69 QRPVSMLFQENNLFaHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 239
Cdd:TIGR01277 138 ALARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-240 |
1.14e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 74.08 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpsnpERETAADSDARsRGPVAYA 100
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--------------GYSIRTDRKAA-RQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQK---PWLLnaTVEENITFESPF---NKQRYKMVIEA----CSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARA 170
Cdd:cd03263 81 PQFdalFDEL--TVREHLRFYARLkglPKSEIKEEVELllrvLGLTDKAN-------KRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRddKRTVVLVTHKLQ---YLphADWIIAMKDGTIQREGT 240
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDL-ILEVRK--GRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
391-642 |
1.22e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 75.66 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 391 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 470
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 471 SRSTLLCVSALTVISYVTPV-FLVALLPLAVVCYFIQKYF---RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAF-- 544
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLILRYFRrriRKASREVRESLAE----LSAFLQESLSGIRVVKAFaa 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 545 -RYE-ARFQQKLLEYTDSNNIASLFLTAANRWLEVrMEYIGACVVLIAAATSIsnsLHRELSAGlvglGLTYALMVSNYL 622
Cdd:cd07346 197 eEREiERFREANRDLRDANLRAARLSALFSPLIGL-LTALGTALVLLYGGYLV---LQGSLTIG----ELVAFLAYLGML 268
|
250 260
....*....|....*....|....
gi 34784298 623 NWMVRNLADM--EIQ--LGAVKRI 642
Cdd:cd07346 269 FGPIQRLANLynQLQqaLASLERI 292
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-248 |
1.58e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNsslpdseGE--DPSNPeretaadSDARSR 94
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMkiLS--GVYQPDSGEILLD-------GEpvRFRSP-------RDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 GpVAYASQKPWLL-NATVEENITFESPFNK----QRYKMVIEACSL--QPDIDILPHgdqTQIGErginLSGGQRQRISV 167
Cdd:COG1129 80 G-IAIIHQELNLVpNLSVAENIFLGREPRRggliDWRAMRRRARELlaRLGLDIDPD---TPVGD----LSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQR 246
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAELTE 229
|
..
gi 34784298 247 SE 248
Cdd:COG1129 230 DE 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
672-896 |
2.15e-14 |
|
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: 76.87 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLK---PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------MFEGRIIIDGIDIAklpL 742
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsgsiLFDGKDLTKLSRRS---L 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 743 HTLRSRLSIILQDPvlFSGtirfnLDPEKKCSDStLWEALEIAQL-------KLVVKAL------PGGLDAIITEggenF 809
Cdd:COG1123 338 RELRRRVQMVFQDP--YSS-----LNPRMTVGDI-IAEPLRLHGLlsraerrERVAELLervglpPDLADRYPHE----L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 810 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVMVLKRG 882
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 34784298 883 AILEFDKPEKLLSQ 896
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-235 |
2.17e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemqrvsgavfwnsslpdsegEDPSNPE--RETAADSDAR--SRGP 96
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrlLAGL---------------------ETPSAGEllAGTAPLAEARedTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWllnATVEENITFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQHT 175
Cdd:PRK11247 87 FQDARLLPW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 176 NVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 235
Cdd:PRK11247 153 GLLLLDEPLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-216 |
2.48e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsSLPDSEGEDPSNPERetaadsdarsrgpVAYASQ 102
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI----KLDGGDIDDPDVAEA-------------CHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 ----KPWLlnaTVEENITFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVARALYQHT 175
Cdd:PRK13539 81 rnamKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALARLLVSNR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 34784298 176 NVVFLDDPFSALDVH--------LSDHLMQAGIlellrddkrtVVLVTH 216
Cdd:PRK13539 147 PIWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-216 |
2.51e-14 |
|
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: 75.09 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQRVSGAVFWnsslpdsEGEDPSN-PERETAAdsd 90
Cdd:COG0444 13 TRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILF-------DGEDLLKlSEKELRK--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 91 ARSRGpVAYASQKPwlLNA-----TVEENITfESPFN------KQRYKMVIEA---CSLQPDIDIL---PHgdqtqiger 153
Cdd:COG0444 83 IRGRE-IQMIFQDP--MTSlnpvmTVGDQIA-EPLRIhgglskAEARERAIELlerVGLPDPERRLdryPH--------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 154 giNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTH 216
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITH 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-238 |
2.90e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.07 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 10 GGFFtWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPS--NPERETAA 87
Cdd:TIGR02769 15 GGLF-GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF-------RGQDLYqlDRKQRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 88 DSDARSRGPVAYASQKP-----WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQ 161
Cdd:TIGR02769 87 RRDVQLVFQDSPSAVNPrmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 162 RQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQ 236
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
..
gi 34784298 237 RE 238
Cdd:TIGR02769 231 EE 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-239 |
4.04e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDPSnperetAADSDARSRgPVA 98
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL-------VAGDDVE------ALSARAASR-RVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWL-LNATVEENITFESPFNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTN 176
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 177 VVFLDDPFSALDVHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 239
Cdd:PRK09536 160 VLLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-239 |
4.64e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.39 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSN-PERETAAdsdARSR- 94
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-------GQDLSRlKRREIPY---LRRRi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 GPVAyasQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 166
Cdd:COG2884 82 GVVF---QDFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 167 VARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPHADW-IIAMKDGTIQREG 239
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSW-----EIMELLEEINRrgtTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-216 |
5.08e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.87 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSN--PEREtaadsdarsrg 95
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-------DGVDLSHvpPYQR----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLL-NATVEENITFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 167
Cdd:PRK11607 92 PINMMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH 216
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-240 |
5.32e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMqrvsgavfwnssLPDSegedpsNPERETAADS--- 89
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL------------LPDD------NPNSKITVDGitl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 90 ------DARSRGPVAYASQKPWLLNATVEENITFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQ 161
Cdd:PRK13640 75 taktvwDIREKVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 162 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
387-642 |
6.82e-14 |
|
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: 73.36 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 387 DQSVYAMVFTVLCSLGIALCLVTSVTV---EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHI 463
Cdd:cd18557 31 DLDVLNELALILLAIYLLQSVFTFVRYylfNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 464 PSTLECLSRSTLLCVSA---LTVISY-VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFA-ETVEGL 538
Cdd:cd18557 111 TDNLSQLLRNILQVIGGliiLFILSWkLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD-----ALAKAGQVAeESLSNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 539 TTIRAF---RYE-ARFQQKLLEYTDSnNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSlhrELSAGLVGLGLTY 614
Cdd:cd18557 186 RTVRSFsaeEKEiRRYSEALDRSYRL-ARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSG---QLTVGELTSFILY 261
|
250 260
....*....|....*....|....*...
gi 34784298 615 ALMVSNYLNWMVRNLADMEIQLGAVKRI 642
Cdd:cd18557 262 TIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
669-897 |
7.46e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 669 QGKIQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMF-----EGRIIIDGIDIAKLPLH 743
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 744 TLRSRLSIILQDP------VLFSGT---IRFN-LDPEKKCSDSTLWEALEIAQLKLVVKalpGGLDAiiteGGENFSQGQ 813
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlSIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVK---DRLDA----PAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 814 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtilsADLVMVLKRGAILE- 886
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEw 226
|
250
....*....|....*..
gi 34784298 887 ------FDKPEKLLSQK 897
Cdd:PRK14247 227 gptrevFTNPRHELTEK 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-219 |
7.76e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsSLPDSEGEDPSnPERETAADSDARSrgpv 97
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI----TLDGKPVEGPG-AERGVVFQNEGLL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 ayasqkPWLlnaTVEENITFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTN 176
Cdd:PRK11248 83 ------PWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 34784298 177 VVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 219
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-230 |
8.89e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.46 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 11 GFFTwTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQRVSGAVFWNsslpdseGEDPSNPERETAADs 89
Cdd:PRK11308 20 GLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIE-TPTGGELYYQ-------GQDLLKADPEAQKL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 90 dARSR------GPvaYASQKP-WLLNATVEE----NITFESPFNKQRYKMVIEACSLQPD-IDILPHgdqtqigergiNL 157
Cdd:PRK11308 90 -LRQKiqivfqNP--YGSLNPrKKVGQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPH-----------MF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 230
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADEVMVM 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-240 |
1.15e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDPSNPERETAAdsdarsRGP 96
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-------VSGIDTGDFSKLQGI------RKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKP--WLLNATVEENITFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSGGQRQRI 165
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
672-895 |
2.10e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSL---AFFRMVDMFEGRIIIDGIDIAKLPlhTLRSR 748
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALhlnGLLRPQKGKVLVSGIDTGDFSKLQ--GIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 749 LSIILQDP-VLFSG-TIRFNL--DPEKKCSDSTlwealEIAqlKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAF 823
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLafGPENLCLPPI-----EIR--KRVDRALAEiGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 824 VRKTSIFIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLS 895
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-246 |
2.19e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.42 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPEretaadsdARSRgPVAYASQ 102
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-------GTDVSRLH--------ARDR-KVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQRISVARA 170
Cdd:PRK10851 82 HYALFrHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQR 246
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-235 |
2.71e-13 |
|
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: 70.71 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDPSNPERETAadsdaRSRgpVAYA 100
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV-------IDGIDISKLPLHTL-----RSR--LSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFL 180
Cdd:cd03288 101 LQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 181 DDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 235
Cdd:cd03288 181 DEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
23-235 |
3.11e-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: 69.87 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNsslpdseGEDPSNPERETAAdsdARSRgpVAYA 100
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTIIID-------GLKLTDDKKNINE---LRQK--VGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLL-NATVEENITfESP---FNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTN 176
Cdd:cd03262 82 FQQFNLFpHLTVLENIT-LAPikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 177 VVFLDDPFSALDVHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 235
Cdd:cd03262 156 VMLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-243 |
3.43e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.29 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSN--PEREtaadsdarsrg 95
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-------GQDITHvpAENR----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLL-NATVEENITF-----ESPfNKQRYKMVIEA---CSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 166
Cdd:PRK09452 87 HVNTVFQSYALFpHMTVFENVAFglrmqKTP-AAEITPRVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 167 VARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 243
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-219 |
3.64e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.45 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEM------QRVSGAVFWNsslpdseGEDPSNPERETAAdsdARSRgp 96
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLL-RCLNRMndlipgARVEGEILLD-------GEDIYDPDVDVVE---LRRR-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENITFESPFNKQRYKMVIEA--------CSLQPDI-DILphgdqtqiGERGINLSGGQRQRISV 167
Cdd:COG1117 94 VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVkDRL--------KKSALGLSGGQQQRLCI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD--DKRTVVLVTHKLQ 219
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPIST-----AKIEELILElkKDYTIVIVTHNMQ 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-216 |
3.89e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.92 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpdsegedPSNPERETAADSdarsrgpV 97
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT--------PLAEQRDEPHEN-------I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLLNA-TVEENITFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQRISVARA 170
Cdd:TIGR01189 76 LYLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 34784298 171 LYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 216
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
667-866 |
4.03e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 667 PDQGKIQIQNLSVRyDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKLPLH--- 743
Cdd:COG4178 358 SEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAI--------------AGLWPYgsg 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 744 --TLRSRLSIIL--QDPVLFSGTIRFNL---DPEKKCSDSTLWEALEIAQLKlvvkALPGGLDAIiTEGGENFSQGQRQL 816
Cdd:COG4178 419 riARPAGARVLFlpQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLG----HLAERLDEE-ADWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 34784298 817 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 866
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
146-239 |
4.35e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.38 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 146 DQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-A 224
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
|
90
....*....|....*
gi 34784298 225 DWIIAMKDGTIQREG 239
Cdd:PRK10619 220 SHVIFLHQGKIEEEG 234
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
391-642 |
4.86e-13 |
|
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: 70.65 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 391 YAMVFTVLCSLGIALC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 469
Cdd:cd18572 37 RAVLLLLLLSVLSGLFsGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 470 LSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLpllshfAETVEGL-TTIRA 543
Cdd:cd18572 117 FLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQDaLAEANQV------AEEALSNiRTVRS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 544 F---RYEA-RFQQKLLEYTDSN---NIASLFLTAANRWLevrmEYIGACVVLIAAATSIsnsLHRELSAG-LVGLGLtYA 615
Cdd:cd18572 191 FateEREArRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVLFYGGHLV---LSGRMSAGqLVTFML-YQ 262
|
250 260
....*....|....*....|....*..
gi 34784298 616 LMVSNYLNWMVRNLADMEIQLGAVKRI 642
Cdd:cd18572 263 QQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
672-896 |
4.93e-13 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrLSI 751
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKS------------------------------TL---LKA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 IL--QDPVlfSGTIRFNLDPEKKcsdstlwEALEIA---QLKLVVKALP--------GGLD--------------AIITE 804
Cdd:COG1121 52 ILglLPPT--SGTVRLFGKPPRR-------ARRRIGyvpQRAEVDWDFPitvrdvvlMGRYgrrglfrrpsradrEAVDE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 805 -----GGENF--------SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI 870
Cdd:COG1121 123 alervGLEDLadrpigelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAV 202
|
250 260
....*....|....*....|....*..
gi 34784298 871 LS-ADLVMVLKRGaILEFDKPEKLLSQ 896
Cdd:COG1121 203 REyFDRVLLLNRG-LVAHGPPEEVLTP 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
672-895 |
5.11e-13 |
|
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: 69.83 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSL--KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPvlfsgtiRFNLDPEKKCsDSTLWEALEIAQLKLVVKALPGGLDAIiteG-GENF--------SQGQRQLFCLA 820
Cdd:COG1124 82 QMVFQDP-------YASLHPRHTV-DRILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 821 RAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
673-884 |
5.47e-13 |
|
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: 69.10 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 673 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRM-----------VDMFEGRIIIDGIDIAKLP 741
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTL----LKAilgllkptsgsIRVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 742 LHTLRSRLS-IILQDPVLFSGTIRFNLDPEKKCSDstlWEALEIAqLKLVvkalpgGLDAI----ITEggenFSQGQRQL 816
Cdd:cd03235 75 QRRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKAD---KAKVDEA-LERV------GLSELadrqIGE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 817 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-SADLVMVLKRGAI 884
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLNRTVV 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-218 |
6.22e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 14 TWTpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdSEGEDPSNperetaadsDARS 93
Cdd:PRK15056 15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI--------SILGQPTR---------QALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 RGPVAYASQKP---WLLNATVEENIT---------FESPfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQ 161
Cdd:PRK15056 77 KNLVAYVPQSEevdWSFPVLVEDVVMmgryghmgwLRRA--KKRDRQIVTAALARVDMVEFRH---RQIGE----LSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 162 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL 218
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
673-885 |
1.05e-12 |
|
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: 67.46 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 673 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLRSRLSII 752
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKS------------------------------TLLKTLAGL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 753 LQdpvLFSGTIRFNLDPEKKcsdstlWEALEIAQLKLVV----KALpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 828
Cdd:cd03214 49 LK---PSSGEILLDGKDLAS------LSPKELARKIAYVpqalELL--GLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 829 IFIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILSADLVMVLKRGAIL 885
Cdd:cd03214 118 ILLLDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
656-891 |
1.11e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 71.64 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 656 LLA--PSLIPKNWPDQGK--IQIQNLSVRYD---SSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRM 722
Cdd:COG4172 256 LLAaePRGDPRPVPPDAPplLEARDLKVWFPikrGLFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 723 VD-----MFEGRIIIDGIDIAKLPlhtLRSRLSIILQDPvlFSgtirfNLDPEKKCSDsTLWEALEIAQLKL-------- 789
Cdd:COG4172 336 IPsegeiRFDGQDLDGLSRRALRP---LRRRMQVVFQDP--FG-----SLSPRMTVGQ-IIAEGLRVHGPGLsaaerrar 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 790 VVKAL------PGGLDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFA------- 856
Cdd:COG4172 405 VAEALeevgldPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehg 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 857 --------DRTVV-TIAHRvhtilsadlVMVLKRGAILE-------FDKPE 891
Cdd:COG4172 477 laylfishDLAVVrALAHR---------VMVMKDGKVVEqgpteqvFDAPQ 518
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-220 |
1.13e-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: 67.58 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWNSSlpdsegedPSNPERetaadsdarSRGPVAYA 100
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVLINGR--------PLDKRS---------FRKIIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLL-NATVEENITFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVF 179
Cdd:cd03213 88 PQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 34784298 180 LDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY 220
Cdd:cd03213 135 LDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
672-881 |
1.20e-12 |
|
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: 68.27 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSS--LKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAKlPLHTLRSRL 749
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLERPTSGEVLVDGE-PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFS-GTIRFN--LDPEKKCSDSTlwEALEIAQ--LKLVvkalpgGLdaiitEGGENF-----SQGQRQLFCL 819
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKA--EARERAEelLELV------GL-----SGFENAyphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 820 ARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLVMVLKR 881
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
1.46e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 3 NFCVQIIGGFFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG--EMQRVSGAVFwnsslpdsegedpsn 80
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiyLPQRGRVKVM--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 81 pERETAADSDARSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqi 150
Cdd:PRK13647 66 -GREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 151 gergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIA 229
Cdd:PRK13647 138 -----HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIV 210
|
250
....*....|
gi 34784298 230 MKDGTIQREG 239
Cdd:PRK13647 211 LKEGRVLAEG 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-257 |
2.29e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWnsslpdsEGEDPSNPERetaadSDARSRGPV 97
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVYL-------DGQDIFKMDV-----IELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPwLLNATVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVA 168
Cdd:PRK14247 87 VFQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKD- 243
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREv 232
|
250
....*....|....
gi 34784298 244 FQRSECQLFEHWKT 257
Cdd:PRK14247 233 FTNPRHELTEKYVT 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-230 |
2.54e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.99 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 10 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSNPERETAADs 89
Cdd:COG4608 21 GGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF-------DGQDITGLSGRELRP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 90 dARSR------GPvaYASqkpwlLNA--TVEENItfESPF-------NKQRYKMV---IEACSLQPD-IDILPHgdqtqi 150
Cdd:COG4608 93 -LRRRmqmvfqDP--YAS-----LNPrmTVGDII--AEPLrihglasKAERRERVaelLELVGLRPEhADRYPH------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 151 gErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-AD 225
Cdd:COG4608 157 -E----FSGGQRQRIGIARALALNPKLIVCDEPVSALDV--S---IQAQVLNLLEDLQDelglTYLFISHDLSVVRHiSD 226
|
....*
gi 34784298 226 WIIAM 230
Cdd:COG4608 227 RVAVM 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-247 |
2.80e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 69.37 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 26 ITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNSSlpdSEGEDPSnPERETaadsdarsrgpVAYA 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIrliagLTRPDEGEIVLNGRTLFDS---RKGIFLP-PEKRR-----------IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKPWLL-NATVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQH 174
Cdd:TIGR02142 81 FQEARLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 247
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
672-895 |
3.26e-12 |
|
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: 67.38 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKL----------- 740
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTL----LRAL--------------AGLlkpssgevlld 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 741 --PLHTLRSR-----LSIILQDPVL-FSGTIR--------------FNLDPE-KKCSDSTLwEALEIAQLKlvvkalpgg 797
Cdd:COG1120 62 grDLASLSRRelarrIAYVPQEPPApFGLTVRelvalgryphlglfGRPSAEdREAVEEAL-ERTGLEHLA--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 798 lDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILS 872
Cdd:COG1120 132 -DRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARY 204
|
250 260
....*....|....*....|...
gi 34784298 873 ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:COG1120 205 ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-230 |
3.63e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.58 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 26 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGED----PSNPERETAADSDARSRGPVAyaS 101
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL-------GKDllgmKDDEWRAVRSDIQMIFQDPLA--S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 102 QKPWLlnaTVEENI-----TFESPFNKQ----RYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARAL 171
Cdd:PRK15079 111 LNPRM---TIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 172 YQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 230
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-219 |
3.67e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.49 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 22 TLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---RVSGAVFWNsslpdseGEDPSNPERETAadsdaRSRGP 96
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsINRMNDLNpevTITGSIVYN-------GHNIYSPRTDTV-----DLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENITFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQRQRISV 167
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 34784298 168 ARALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 219
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
687-883 |
3.89e-12 |
|
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: 67.96 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 687 PVLKHVNALIAPGQKIGICGRTGSGKSSFslaffRMVDMFEGRIIIDGIDiaklplHTlrSRLSIILQDPVLFSGTIRFN 766
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSL-----LMLILGELEPSEGKIK------HS--GRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 767 LDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEN- 845
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 34784298 846 ILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGA 883
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-240 |
3.96e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.49 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 1 ADNFCVQIiggfftwtpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsSLPDSEGEDPSN 80
Cdd:PRK13548 5 ARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV----RLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 81 PERetaadsdARSRgpvAYASQK-----PWllnaTVEENITF-ESPF--NKQRYKMVIEACSLQPDIDILPHGDQTQige 152
Cdd:PRK13548 72 AEL-------ARRR---AVLPQHsslsfPF----TVEEVVAMgRAPHglSRAEDDALVAAALAQVDLAHLAGRDYPQ--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 153 rginLSGGQRQRISVARALYQHTN------VVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL---- 218
Cdd:PRK13548 135 ----LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVLHDLnlaa 205
|
250 260
....*....|....*....|..
gi 34784298 219 QYlphADWIIAMKDGTIQREGT 240
Cdd:PRK13548 206 RY---ADRIVLLHQGRLVADGT 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-243 |
4.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSS-------LLLATLGEMQrvsgAVFWNSSLPDSEGEDPSNPE------ 82
Cdd:PRK13651 16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIE----WIFKDEKNKKKTKEKEKVLEklviqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 83 ---RETAADSDARSRGPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqtqig 151
Cdd:PRK13651 92 trfKKIKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 152 ergINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAM 230
Cdd:PRK13651 164 ---FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIFF 238
|
250
....*....|....*..
gi 34784298 231 KDGTIQREG----TLKD 243
Cdd:PRK13651 239 KDGKIIKDGdtydILSD 255
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-241 |
4.90e-12 |
|
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: 65.42 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqrvSGAVFWNSSLPdsegedpsnperetaadsdARSRGPVAYASQ 102
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLP-------------------KFSRNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 kpwlLNATVEENITFespfnkqrykmvieacslqpdidiLPHGDQTQigergiNLSGGQRQRISVARALYQHT-NVVF-L 180
Cdd:cd03238 68 ----LQFLIDVGLGY------------------------LTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 181 DDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 241
Cdd:cd03238 114 DEPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
686-887 |
5.45e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 686 KPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdmfegriiidgidiaklpLHTLRSRLSI-------------I 752
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTL--------------------------LQSLLSQFEIsegrvwaersiayV 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 753 LQDPVLFSGTIRFNL---DPEKKcsdSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 829
Cdd:PTZ00243 727 PQQAWIMNATVRGNIlffDEEDA---ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 830 FIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAIlEF 887
Cdd:PTZ00243 804 YLLDDPLSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV-EF 861
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
672-896 |
5.54e-12 |
|
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: 66.45 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFE-------GRIIIDGIDIAKLPL 742
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsgsvLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 743 HTLRSRLSIILQDPVLFS-----GTIRFNLD---PEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQR 814
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 815 QLFCLARAFVRKTSIFIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKP 890
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 34784298 891 EKLLSQ 896
Cdd:cd03258 226 EEVFAN 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-248 |
6.86e-12 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 66.31 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnperETAADSDARSRGPVA 98
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-------GED------ITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLL-NATVEENI----------TFESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INLSGGQRQ 163
Cdd:cd03219 79 RTFQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 164 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLK 242
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPD 228
|
....*.
gi 34784298 243 DFQRSE 248
Cdd:cd03219 229 EVRNNP 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
672-888 |
7.39e-12 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 65.62 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPLHtlRS 747
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLERpdsgEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 748 RLSIILQDPVLFS-----GTIRFNLD----PEKKCSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 818
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKlrgvPKAEIRARVR-ELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 819 LARAFVRKTSIFIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFD 888
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
672-893 |
9.05e-12 |
|
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: 65.99 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLA----------FFRMVDMFEGRIIIdgidiak 739
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLlrLIVgllrpdsgevLIDGEDISGLSEAE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 740 lpLHTLRSRLSIILQDPVLFSG-TIR----FNLDPEKKCSDSTLweaLEIAQLKLVVKALPGGLDAIITEggenFSQGQR 814
Cdd:cd03261 72 --LYRLRRRMGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE----LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 815 QLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPE 891
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
..
gi 34784298 892 KL 893
Cdd:cd03261 223 EL 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
672-882 |
1.06e-11 |
|
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: 64.34 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRSRLSI 751
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTT-----------------------------LIKIILGL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDpvlfSGTIR-FNLDPEKkcsdstlwealEIAQLKLVVKALPGGlDAIITE--GGEN--FSQGQRQLFCLARAFVRK 826
Cdd:cd03230 50 LKPD----SGEIKvLGKDIKK-----------EPEEVKRRIGYLPEE-PSLYENltVRENlkLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 827 TSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILS-ADLVMVLKRG 882
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-243 |
1.11e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKS-------SLLLATlgemqrvSGAVFwnsslpdSEGEDPSNPERETaadsDARS 93
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKStiakhmnALLIPS-------EGKVY-------VDGLDTSDEENLW----DIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 RGPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 165
Cdd:PRK13633 86 KAGMVFQNPDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 243
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
14-218 |
1.49e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 14 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpsnpERETAAdsdarS 93
Cdd:PRK10771 8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-------GQD----HTTTPP-----S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 RGPVAYASQKPWLLN-ATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 165
Cdd:PRK10771 70 RRPVSMLFQENNLFShLTVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 218
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-257 |
1.52e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.63 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNSSLPDSEGEDPSNPERETaadsdarsrGPV 97
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRREV---------GMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 -AYASQKPWLlnaTVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISV 167
Cdd:PRK14267 91 fQYPNPFPHL---TIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 168 ARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQREG-TLKD 243
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRKV 235
|
250
....*....|....
gi 34784298 244 FQRSECQLFEHWKT 257
Cdd:PRK14267 236 FENPEHELTEKYVT 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-241 |
1.60e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpdsegedpSNPERETAADSDARSRgPVAYASQ 102
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---------PMSKLSSAAKAELRNQ-KLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLL-NATVEENITFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQHTNVVFL 180
Cdd:PRK11629 95 FHHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 181 DDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 241
Cdd:PRK11629 170 DEPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-243 |
1.87e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.78 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 13 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLA--------------------TLGEMQRVSGAVFWNssl 70
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTgllkpqsgeikidgitiskeNLKEIRKKIGIIFQN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 71 PDSEgedpsnperetaadsdarsrgpvayasqkpwLLNATVEENITFeSPFNKQ--RYKM--VIEACSLQPDI-DILPHG 145
Cdd:PRK13632 92 PDNQ-------------------------------FIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMeDYLDKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 146 DQtqigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHAD 225
Cdd:PRK13632 140 PQ--------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMDEAILAD 210
|
250
....*....|....*...
gi 34784298 226 WIIAMKDGTIQREGTLKD 243
Cdd:PRK13632 211 KVIVFSEGKLIAQGKPKE 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
672-866 |
2.08e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.33 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKL-PLHT------ 744
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRAL--------------AGLwPWGSgrigmp 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 745 LRSRLSIILQDPVLFSGTIRfnldpekkcsdstlwealeiaqlklvvkalpgglDAIITEGGENFSQGQRQLFCLARAFV 824
Cdd:cd03223 62 EGEDLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 34784298 825 RKTSIFIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 866
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
157-262 |
2.13e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 235
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
90 100
....*....|....*....|....*..
gi 34784298 236 QREGTLKdfqrsecQLFEHWKTLMNRQ 262
Cdd:PRK11264 223 VEQGPAK-------ALFADPQQPRTRQ 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-240 |
2.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.41 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegeDPSNPERETAADSDARSRG 95
Cdd:PRK13645 20 TPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG---------DYAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKP--WLLNATVEENITFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQRQRISVA 168
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
672-896 |
3.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVDMF----EGRIIIDGIDIAKLPLHTL-- 745
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLINGLllpdDNPNSKITVDGITLTAKTVwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 746 -RSRLSIILQDP-VLFSGT-----IRFNLD----PEKKcsdstlwealeiaQLKLVVKALP--GGLDAIITEGgENFSQG 812
Cdd:PRK13640 82 iREKVGIVFQNPdNQFVGAtvgddVAFGLEnravPRPE-------------MIKIVRDVLAdvGMLDYIDSEP-ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 813 QRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKP 890
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
....*.
gi 34784298 891 EKLLSQ 896
Cdd:PRK13640 228 VEIFSK 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
395-642 |
3.13e-11 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 65.20 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 395 FTVLCSLGIALCLVTSV---TVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 471
Cdd:cd18575 39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 472 RSTLLCVSALTVISYVTP---VFLVALLPLAVV-CYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAFRY 546
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQdRLADLS-----AFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 547 EARFQQKLLEYTDSNniaslfLTAANRWLEVRMEYIGACVVLIAAATS------ISNSLHRELSAGLVGLGLTYALMVSN 620
Cdd:cd18575 194 EDAERQRFATAVEAA------FAAALRRIRARALLTALVIFLVFGAIVfvlwlgAHDVLAGRMSAGELSQFVFYAVLAAG 267
|
250 260
....*....|....*....|..
gi 34784298 621 YLNWMVRNLADMEIQLGAVKRI 642
Cdd:cd18575 268 SVGALSEVWGDLQRAAGAAERL 289
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
25-252 |
3.15e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDpsnperetAADSDARSRGpVAYASQKP 104
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF-------IDGED--------VTHRSIQQRD-ICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 105 WLL-NATVEENITF-------ESPFNKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVARALYQH 174
Cdd:PRK11432 88 ALFpHMSLGENVGYglkmlgvPKEERKQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 175 TNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 252
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-225 |
3.48e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 24 SNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgeMQRVSGAVFWNsslpdseGEDpsnperetaadsdaRSRGPVAYAS 101
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQ-------GEP--------------IRRQRDEYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 102 QKPWL--LNA-----TVEENITFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NLSGGQRQ 163
Cdd:PRK13538 75 DLLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 164 RISVARALYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 225
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
394-554 |
3.74e-11 |
|
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: 64.84 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 394 VFTV--LCSLGIALCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 471
Cdd:cd18573 50 VFVVgaAANFGRVYLLRIA------GERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 472 RSTLLCVSALTVISYVTP-VFLVALL---PLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPllshfAETVEGLTTIRAF-- 544
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPkLTLVMLLvvpPIAVGAVFYGRYVRKLSKQVQDaLADATKVA-----EERLSNIRTVRAFaa 198
|
170
....*....|..
gi 34784298 545 -RYE-ARFQQKL 554
Cdd:cd18573 199 eRKEvERYAKKV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
672-882 |
3.79e-11 |
|
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: 62.59 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG------RIIIDGIDIAKLPLHTL 745
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEEpdsgsiLIDGEDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 746 RSRLSIILQDPVLFSG-TIRFNLdpekkcsdstlwealeiaqlklvvkALPggldaiiteggenFSQGQRQLFCLARAFV 824
Cdd:cd03229 75 RRRIGMVFQDFALFPHlTVLENI-------------------------ALG-------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34784298 825 RKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVMVLKRG 882
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
23-244 |
4.22e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.86 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNsslpdseGEDPSNPERETAAdsdARSRgpVAYA 100
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTITVD-------GEDLTDSKKDINK---LRRK--VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQK----PwllNATVEENITfESP-----FNKQrykmviEACSLQpdIDILphgDQTQIGERG----INLSGGQRQRISV 167
Cdd:COG1126 83 FQQfnlfP---HLTVLENVT-LAPikvkkMSKA------EAEERA--MELL---ERVGLADKAdaypAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 243
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELV-----GEVLDVMRDlakEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEE 222
|
.
gi 34784298 244 F 244
Cdd:COG1126 223 F 223
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-216 |
5.00e-11 |
|
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: 62.90 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlPDSEgedpsnperetAADSDARSrgpV 97
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDF-----------QRDSIARG---L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLLNA-TVEENITFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVARALYQHT 175
Cdd:cd03231 76 LYLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 34784298 176 NVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 216
Cdd:cd03231 145 PLWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
672-890 |
8.14e-11 |
|
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: 62.97 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP---LHTLRSR 748
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 749 LSIILQDpvlfsgtirFNLDPEK---------KCSDSTLWEAL-------EIAQ----LKLVvkalpgGLDAIITEGGEN 808
Cdd:cd03256 80 IGMIFQQ---------FNLIERLsvlenvlsgRLGRRSTWRSLfglfpkeEKQRalaaLERV------GLLDKAYQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 809 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILS-ADLVMVLKR 881
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKD 220
|
....*....
gi 34784298 882 GAILeFDKP 890
Cdd:cd03256 221 GRIV-FDGP 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
672-840 |
9.76e-11 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 62.11 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMV----DMFEGRIIIDGIDIAKLPLHtLRS 747
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 748 RLSIILQDPVLFSG-TIRFNLD-----PEKKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLFCLAR 821
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 34784298 822 AFVRKTSIFIMDEATASID 840
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-243 |
1.02e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNperETAADSDARSRgpVAYASQ 102
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------GVDITD---KKVKLSDIRKK--VGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSGGQRQRISVARA 170
Cdd:PRK13637 91 YPeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 243
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-240 |
1.38e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAV----FWNSslPDSEGEDPSNPERETAADSDA 91
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIG--DKKNNHELITNPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 92 RSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGG 160
Cdd:PRK13631 113 ELRRRVSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 161 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKDGTIQ 236
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
....
gi 34784298 237 REGT 240
Cdd:PRK13631 256 KTGT 259
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
672-865 |
1.40e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 60.15 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdmfegriiidgidiaklplhtlrsrLSI 751
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVLFSGTIRFNldpekkcsdstlwEALEIAQLklvvkalpggldaiiteggENFSQGQRQLFCLARAFVRKTSIFI 831
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 34784298 832 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 865
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-243 |
1.79e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 63.58 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLL--LATL-----GEMqRVSGAVFWNSS----LPdsegedpsnPERetaadsdars 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLraIAGLerpdsGRI-RLGGEVLQDSArgifLP---------PHR---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 RgPVAYASQK----PWLlnaTVEENITF---ESPFNKQRYKM--VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQR 164
Cdd:COG4148 77 R-RIGYVFQEarlfPHL---SVRGNLLYgrkRAPRAERRISFdeVVELLGIGHLLDRRPA-----------TLSGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKL---QYLphADWIIAMKDGTIQREGT 240
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDIpILYVSHSLdevARL--ADHVVLLEQGRVVASGP 217
|
...
gi 34784298 241 LKD 243
Cdd:COG4148 218 LAE 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-251 |
1.87e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPS-NPERETaadsdarsr 94
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKR--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 gpVAYASQKP--WLLNATVEENITFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARAL 171
Cdd:PRK13646 87 --IGMVFQFPesQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSECQ 250
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
.
gi 34784298 251 L 251
Cdd:PRK13646 240 L 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-245 |
2.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.83 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSegedpSNPERETAAdsdARSRG 95
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS-----TSKQKEIKP---VRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLLNATVEENITFeSPFNKQRYKMVIEACSLQpDIDILphGDQTQIGERG-INLSGGQRQRISVARALYQH 174
Cdd:PRK13643 87 GVVFQFPESQLFEETVLKDVAF-GPQNFGIPKEKAEKIAAE-KLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQ 245
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQ 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-239 |
2.38e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPDSEgedpsnperetaadsdaRSRGPV--A 98
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmNDVPPAE-----------------RGVGMVfqS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQkPWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARAL 171
Cdd:PRK11000 84 YALY-PHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 239
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
391-553 |
2.43e-10 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 62.41 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 391 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 470
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 471 SRSTLLCVSALTVISYV----TPVFLVALLPLAVVCYFIQKYFRVASRDL-QQLDDttqlpLLSHFAETVEGLTTIRAFR 545
Cdd:cd18544 123 IGDLLLLIGILIAMFLLnwrlALISLLVLPLLLLATYLFRKKSRKAYREVrEKLSR-----LNAFLQESISGMSVIQLFN 197
|
....*...
gi 34784298 546 YEARFQQK 553
Cdd:cd18544 198 REKREFEE 205
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
418-636 |
2.56e-10 |
|
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: 62.46 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 418 LKVAKRLHRSLL----NRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPST-LECLSRSTLLCVSALTVISYVTPVFL 492
Cdd:cd18570 67 LKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 493 VALLPL---AVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFRYE----ARFQQKLLEYTDSN---N 562
Cdd:cd18570 146 ITLLIIplyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEeqflKKIEKKFSKLLKKSfklG 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 563 IASLFLTAANRWLEVrmeyIGACVVLIAAATSIsnsLHRELSAGLVglgLTYALMVSNYLNwMVRNLADMEIQL 636
Cdd:cd18570 222 KLSNLQSSIKGLISL----IGSLLILWIGSYLV---IKGQLSLGQL---IAFNALLGYFLG-PIENLINLQPKI 284
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-217 |
2.73e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.00 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLATLGEMQRVSGAVFwnsSLPdsegedpsnperetaadsdarSRG 95
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGRL---TKP---------------------AKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLLNATVEENITF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LSGGQRQR 164
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQR 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHK 217
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-897 |
3.88e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------- 744
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpdvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 745 LRSRLSIILQDPVLFSG-TIRFN----------LDPEKKCSDSTLWeALEIAQLKLVVKALpggldaiITEGGENFSQGQ 813
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNvaigvklnglVKSKKELDERVEW-ALKKAALWDEVKDR-------LNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 814 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILSADLVMVLKRGAILE------ 886
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgptrk 234
|
250
....*....|..
gi 34784298 887 -FDKPEKLLSQK 897
Cdd:PRK14267 235 vFENPEHELTEK 246
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-254 |
4.13e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.57 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSL------LLA----------------TLGEMQRVSGAVFWNsslPDSEgedp 78
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLakllngLLLpeagtitvggmvlseeTVWDVRRQVGMVFQN---PDNQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 79 snperetaadsdarsrgpvayasqkpwLLNATVEENITF--EspfNKQ--RYKMV------IEACSLQPDIDILPHgdqt 148
Cdd:PRK13635 94 ---------------------------FVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNREPH---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 149 qigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKR-TVVLVTHKLQYLPHADWI 227
Cdd:PRK13635 140 -------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL--ETVRQLKEQKGiTVLSITHDLDEAAQADRV 210
|
250 260
....*....|....*....|....*..
gi 34784298 228 IAMKDGTIQREGTLKdfqrsecQLFEH 254
Cdd:PRK13635 211 IVMNKGEILEEGTPE-------EIFKS 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
597-886 |
4.18e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 597 NSLHRELSAGLvglgltyaLMVSNYLNwMVRNLAD--MEIQLGAV---KRIHTLLKTEAESY-EGLLA--PSLIPKNWPD 668
Cdd:PRK15134 200 RELQQELNMGL--------LFITHNLS-IVRKLADrvAVMQNGRCveqNRAATLFSAPTHPYtQKLLNsePSGDPVPLPE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 669 QGK--IQIQNLSV---------RYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD-----MFEGRIII 732
Cdd:PRK15134 271 PASplLDVEQLQVafpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINsqgeiWFDGQPLH 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 733 DGIDIAKLPlhtLRSRLSIILQDPvlfSGTIRFNLDPEKkcsdsTLWEALEIAQLKL--------VVKALPG-GLDAII- 802
Cdd:PRK15134 351 NLNRRQLLP---VRHRIQVVFQDP---NSSLNPRLNVLQ-----IIEEGLRVHQPTLsaaqreqqVIAVMEEvGLDPETr 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 803 ----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTIL 871
Cdd:PRK15134 420 hrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVR 490
|
330
....*....|....*.
gi 34784298 872 S-ADLVMVLKRGAILE 886
Cdd:PRK15134 491 AlCHQVIVLRQGEVVE 506
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-277 |
4.46e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.28 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWNSSL---------PDSEGE---------- 76
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIYHVALcekcgyverPSKVGEpcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 77 -------DPSNPERetaadsdARSRGPVAYASQKPWLL--NATVEENITfeSPFNKQRYKmviEACSLQPDIDILphgDQ 147
Cdd:TIGR03269 91 peevdfwNLSDKLR-------RRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 148 TQIGER----GINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH 223
Cdd:TIGR03269 156 VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 224 -ADWIIAMKDGTIQREGTLKDFQRSECQLFEhwktlmnrqdqELEKETVMERKAP 277
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVVAVFMEGVS-----------EVEKECEVEVGEP 278
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-902 |
4.50e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM------------VDMFEGRIIIDgidiaK 739
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesevrvegrVEFFNQNIYER-----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 740 LPLHTLRSRLSIILQDPVLFSGTI---------------RFNLDP--EKKCSDSTLWEalEIAQlKLVVKALpggldaii 802
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDivESALKDADLWD--EIKH-KIHKSAL-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 803 teggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTILS-ADLVM 877
Cdd:PRK14258 150 -----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFTA 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 34784298 878 VLKR-----GAILEFDKPEKLLSQ------KDSVFA 902
Cdd:PRK14258 223 FFKGnenriGQLVEFGLTKKIFNSphdsrtREYVLS 258
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
672-884 |
6.45e-10 |
|
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: 58.59 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrLSI 751
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKS------------------------------TL---MKI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 I--LQDPVlfSGTIRFNldpEKKCSDSTLWEALE-----IAQLklvvkalpggldaiiteggenfSQGQRQLFCLARAFV 824
Cdd:cd03216 46 LsgLYKPD--SGEILVD---GKEVSFASPRDARRagiamVYQL----------------------SVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 825 RKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRGAI 884
Cdd:cd03216 99 RNARLLILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
410-557 |
6.77e-10 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 60.96 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 410 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 489
Cdd:cd18576 57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 490 ---VFLVALLP-LAVVCYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAF---RYEA-RFQQKLLEY 557
Cdd:cd18576 137 kltLLMLATVPvVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIRVVKAFtreDYEIeRYRKALERV 208
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-240 |
8.63e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 60.32 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQRVSGA------VFWNSSLPdseGEDP-SN 80
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLehidkvIVIDQSPI---GRTPrSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 81 PERETAADSDARS------RGP--------VAYASQK-PWLLNATVEENITFESPFNKQRYKmvieacsLQPDIDIlphG 145
Cdd:cd03271 88 PATYTGVFDEIRElfcevcKGKrynretleVRYKGKSiADVLDMTVEEALEFFENIPKIARK-------LQTLCDV---G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 146 -DQTQIGERGINLSGGQRQRISVARALYQ---HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL 221
Cdd:cd03271 158 lGYIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLE--VLQRLVDKGNTVVVIEHNLDVI 235
|
250 260
....*....|....*....|....*
gi 34784298 222 PHADWIIAM------KDGTIQREGT 240
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
672-894 |
1.30e-09 |
|
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: 59.71 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF-SLAFFRM-----------------VDMFEgriiid 733
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLpptygndvrlfgerrggEDVWE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 734 gidiaklplhtLRSRLSII---LQDPVLFSGTIR-------FnldpekkcsDST-LWEALEIAQLKLVVKALPG-GLDAI 801
Cdd:COG1119 76 -----------LRKRIGLVspaLQLRFPRDETVLdvvlsgfF---------DSIgLYREPTDEQRERARELLELlGLAHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 802 ItegGENF---SQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILSA- 873
Cdd:COG1119 136 A---DRPFgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGi 210
|
250 260
....*....|....*....|.
gi 34784298 874 DLVMVLKRGAILEFDKPEKLL 894
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVL 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-216 |
1.42e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.86 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNsslpdseGEDPSN-PERETAAdsdARSRgpVA 98
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL---ERPtSGSVLVD-------GVDLTAlSERELRA---ARRK--IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLLNA-TVEENITFesPF------NKQRYKMVIEACSLqpdIDILPHGDQ--TQigerginLSGGQRQRISVAR 169
Cdd:COG1135 86 MIFQHFNLLSSrTVAENVAL--PLeiagvpKAEIRKRVAELLEL---VGLSDKADAypSQ-------LSGGQKQRVGIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 170 ALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTH 216
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITH 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-248 |
1.59e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQrvsgavfwnsslPDSEGEDPSNPERETAADSDARSRgPVAYASQ 102
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQ------------PPSEGEILLDAQPLESWSSKAFAR-KVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 K-PWLLNATVEENITF-ESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRISVARALY 172
Cdd:PRK10575 93 QlPAAEGMTVRELVAIgRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 173 QHTNVVFLDDPFSALDV-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSE 248
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-254 |
1.89e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.70 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETAAD---------SDArs 93
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-------GEPLAKLNRAQRKAfrrdiqmvfQDS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 94 rgPVAYASQKP--WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARA 170
Cdd:PRK10419 99 --ISAVNPRKTvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLkdfq 245
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPV---- 236
|
....*....
gi 34784298 246 rSECQLFEH 254
Cdd:PRK10419 237 -GDKLTFSS 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-248 |
2.03e-09 |
|
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: 58.84 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnpereTAADSDARSRGPV 97
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-------GEDI------TGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQK----PWLlnaTVEENIT--FESPFNKQRYKMVIEACslqpdIDILPhgdqtQIGER----GINLSGGQRQRISV 167
Cdd:COG0410 81 GYVPEGrrifPSL---TVEENLLlgAYARRDRAEVRADLERV-----YELFP-----RLKERrrqrAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 168 ARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDFQR 246
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFE--IIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
..
gi 34784298 247 SE 248
Cdd:COG0410 226 DP 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
158-240 |
2.72e-09 |
|
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: 58.15 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDG 233
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHG 208
|
....*..
gi 34784298 234 TIQREGT 240
Cdd:cd03265 209 RIIAEGT 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-238 |
3.18e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.25 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPSNPERETAADSDARSRGPVAY 99
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL-------VGQPLHQMDEEARAKLRAKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWLLNATveENITFESPFNKQRykmviEACSLQPDIDILphgDQTQIGER----GINLSGGQRQRISVARALYQHT 175
Cdd:PRK10584 96 SFMLIPTLNAL--ENVELPALLRGES-----SRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 176 NVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 238
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-255 |
3.73e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMQR-----VSGAVFWNSSLPDsegedpsnperetaaDSDARS-RG 95
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLrVLNLLEMPRsgtlnIAGNHFDFSKTPS---------------DKAIRElRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQK----PWLlnaTVEENITfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQR 162
Cdd:PRK11124 83 NVGMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALD-------VHLSDHLMQAGIlellrddkrTVVLVTHKLQYLPH-ADWIIAMKDGT 234
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI---------TQVIVTHEVEVARKtASRVVYMENGH 218
|
250 260
....*....|....*....|.
gi 34784298 235 IQREGTLKDFQRSECQLFEHW 255
Cdd:PRK11124 219 IVEQGDASCFTQPQTEAFKNY 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
23-239 |
3.73e-09 |
|
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: 57.59 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGqLTMIVGQVGCGKSSLL--LATLgeMQRVSGAVFWNsslpdseGEDPSNPERETaadsdarsRGPVAYA 100
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMriLATL--TPPSSGTIRID-------GQDVLKQPQKL--------RRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKP-WLLNATVEENITF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRISVARALY 172
Cdd:cd03264 78 PQEFgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 173 QHTNVVFLDDPFSALD----VHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 239
Cdd:cd03264 147 GDPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
158-235 |
4.02e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 230
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*
gi 34784298 231 KDGTI 235
Cdd:PRK11701 226 KQGRV 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
157-244 |
4.43e-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: 60.08 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL----QYlphADWII 228
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLgvvrRF---ADRVA 228
|
90
....*....|....*.
gi 34784298 229 AMKDGTIQREGTLKDF 244
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
672-870 |
4.94e-09 |
|
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: 57.42 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP---LHTLRSR 748
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 749 LSIILQDpvlfsgtirFNLDPEKKCSDSTLWeALEIAQL--KLVVKALPGGLDAIITEGGEN-----FSQGQRQLFCLAR 821
Cdd:cd03292 80 IGVVFQD---------FRLLPDRNVYENVAF-ALEVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 822 AFVRKTSIFIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 870
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
676-882 |
6.13e-09 |
|
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: 56.79 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 676 NLSVRYDSSL----KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVdmfEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:cd03213 8 NLTVTVKSSPsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTG---LGVSGEVLINGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFsgtirfnldpekkcSDSTLWEALEI-AQLKlvvkalpgGLdaiiteggenfSQGQRQLFCLARAFVRKTS 828
Cdd:cd03213 85 GYVPQDDILH--------------PTLTVRETLMFaAKLR--------GL-----------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 829 IFIMDEATASIDMATENILQKVVMtAFAD--RTVVTIAHRVHTIL--SADLVMVLKRG 882
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-240 |
6.46e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 60.03 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQRVSGA------VFWNSSLPdseGEDP-SN 80
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEGLehldkvIHIDQSPI---GRTPrSN 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 81 PERET----------AADSDARSRGpvaYaSQKPWLLNA--------------TVEEN------ITFES----PFNKQ-- 124
Cdd:TIGR00630 701 PATYTgvfdeirelfAETPEAKVRG---Y-TPGRFSFNVkggrceacqgdgviKIEMHflpdvyVPCEVckgkRYNREtl 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 125 --RYK---------MVI-EACSLQPDIDILPHGDQT---------QIGERGINLSGGQRQRISVARALYQ---HTNVVFL 180
Cdd:TIGR00630 777 evKYKgkniadvldMTVeEAYEFFEAVPSISRKLQTlcdvglgyiRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYIL 856
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 181 DDPFSALdvHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPHADWII------AMKDGTIQREGT 240
Cdd:TIGR00630 857 DEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTVVASGT 920
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-235 |
6.49e-09 |
|
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: 57.44 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 15 WTPDGIPT-LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNsslpdseGEDPsnpereTAADSD 90
Cdd:COG4181 19 GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLglLAGL---DRPtSGTVRLA-------GQDL------FALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 91 ARSR------GPVAYASQkpwLLNA-TVEENITFESPFN-----KQRYKMVIEACSLQPDIDILPHGdqtqigerginLS 158
Cdd:COG4181 83 ARARlrarhvGFVFQSFQ---LLPTlTALENVMLPLELAgrrdaRARARALLERVGLGHRLDHYPAQ-----------LS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 159 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDGT 234
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLFELNRergtTLVLVTHDPALAARCDRVLRLRAGR 223
|
.
gi 34784298 235 I 235
Cdd:COG4181 224 L 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
157-233 |
7.51e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 57.54 E-value: 7.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 233
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINL-MLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-235 |
7.59e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.79 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 12 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAtlgemqrVSGAVfwnssLPDS-----EGEDPSN-PERET 85
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA-------IAGSL-----PPDSgsiliDGKDVTKlPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 86 AADsdarsrgpVAYASQKPwLL----NATVEENI----------TFESPFNKQRYKMVIEACSlqpDIDI-LPHGDQTQI 150
Cdd:COG1101 79 AKY--------IGRVFQDP-MMgtapSMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLgLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 151 GergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagiL--ELLRDDKRTVVLVTHKLQY-LPHADWI 227
Cdd:COG1101 147 G----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRL 219
|
....*...
gi 34784298 228 IAMKDGTI 235
Cdd:COG1101 220 IMMHEGRI 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-248 |
7.68e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ--------RVSGAVFWNsslpdseGEdpsnPERETAADSDARSR 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN-------GE----PLAAIDAPRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 GPVAYASQKPWLLnaTVEENITFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQRQRISVA 168
Cdd:PRK13547 86 AVLPQAAQPAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 169 RALYQ---------HTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQRE 238
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLA-HQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAH 236
|
250
....*....|
gi 34784298 239 GTLKDFQRSE 248
Cdd:PRK13547 237 GAPADVLTPA 246
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
671-896 |
1.10e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.33 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 671 KIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVD-MFEGRIIIDGIDIAKLPLHT---LR 746
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLA----KLLNgLLLPEAGTITVGGMVLSEETvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 747 SRLSIILQDP-VLFSGT-----IRFNLDpEKKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 820
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGAtvqddVAFGLE-NIGVPREEMVERVDQA-LRQV------GMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 821 RAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 896
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-239 |
1.33e-08 |
|
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: 56.22 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 26 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpDSEGEDPSNPEREtaadsdARSRGPVAYASQK-- 103
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-------TVDGFDVVKEPAE------ARRRLGFVSDSTGly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 104 PWLlnaTVEENITFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHTN 176
Cdd:cd03266 91 DRL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 177 VVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 239
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
672-886 |
1.47e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRY---DSSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP- 741
Cdd:PRK10261 314 LQVRNLVTRFplrSGLLNRVTREVHAVekvsfdLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 742 --LHTLRSRLSIILQDPVLfsgtirfNLDPEKKCSDSTLwEALEIAQLkLVVKALPGGLDAIITEGG----------ENF 809
Cdd:PRK10261 394 gkLQALRRDIQFIFQDPYA-------SLDPRQTVGDSIM-EPLRVHGL-LPGKAAAARVAWLLERVGllpehawrypHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 810 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVHTILSADLVM 877
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHRVAVMYLGQIVE 544
|
....*....
gi 34784298 878 VLKRGAILE 886
Cdd:PRK10261 545 IGPRRAVFE 553
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-243 |
1.54e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 56.73 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEdPSNPE--RETaadsdarsRGPVAYA 100
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL-------IRGE-PITKEniREV--------RKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 170
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 171 LYQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 243
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-230 |
1.56e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 56.11 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL-GEMQR-----VSGAV---FWNSSLPDS---EGEDPS-NPERETAADS 89
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyAEGQRryvesLSAYArqfLGQMDKPDVdsiEGLSPAiAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 90 DARSRGPVAYASQKPWLLNATVeeNItfespfnKQRYKMVIEacslqpdidilphgdqtqIG------ERGIN-LSGGQR 162
Cdd:cd03270 91 PRSTVGTVTEIYDYLRLLFARV--GI-------RERLGFLVD------------------VGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 163 QRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 230
Cdd:cd03270 144 QRIRLATQIgSGLTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-234 |
1.57e-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: 54.38 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpV 97
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-------------------------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNV 177
Cdd:cd03221 66 GYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 178 VFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 234
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-235 |
1.64e-08 |
|
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: 55.13 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGED--PSNPeretaadSDARSRGpVAYA 100
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-------GKPvtRRSP-------RDAIRAG-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 S----QKPWLLNATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQHTN 176
Cdd:cd03215 81 PedrkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 177 VVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 235
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
419-553 |
1.88e-08 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 56.64 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 419 KVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LVALL- 496
Cdd:cd18547 75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtLIVLVt 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 497 -PLAVVC-YFI----QKYFRVASRDLQQLDdttqlpllSHFAETVEGLTTIRAFRYEARFQQK 553
Cdd:cd18547 155 vPLSLLVtKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEE 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
672-909 |
2.19e-08 |
|
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: 55.77 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVLFSG-TIRFN--LDP--EKkcsdstlWEALEIAQ-----LKLVvkalpgGLDaiITEGGENF----SQGQRQLF 817
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPklLK-------WPKEKIREradelLALV------GLD--PAEFADRYphelSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 818 CLARAFVRKTSIFIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILSADLVMVLKRGAILEFDKP 890
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTP 220
|
250 260
....*....|....*....|
gi 34784298 891 EKLL-SQKDSVFASFVRADK 909
Cdd:cd03295 221 DEILrSPANDFVAEFVGADR 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-282 |
2.25e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.12 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQRVSGAVFWNsslpdseGEDPsnpereTAADSDA--RSRG 95
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrCINLLE-RPTSGRVLVD-------GQDL------TALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLLNA-TVEENITFespfnkqrykmvieacSLQpdidiLPHGDQTQIGER--------GI---------NL 157
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVAL----------------PLE-----LAGTPKAEIKARvtellelvGLsdkadrypaQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKD 232
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVIDA 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 233 GTIQREGTLKDfqrsecqLFEHWKTLMNRQ------DQELEkETVMERKAPEPSQG 282
Cdd:PRK11153 217 GRLVEQGTVSE-------VFSHPKHPLTREfiqstlHLDLP-EDYLARLQAEPTTG 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-245 |
2.51e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnPERETAADSDARSRGPVAYA 100
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD-------GENI--PAMSRSRLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SqKPWLLNATVEENITF--------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 172
Cdd:PRK11831 92 S-GALFTDMNVFDNVAYplrehtqlPAPLLHSTVMMKLEAVGLRGAAKLMPS-----------ELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 173 QHTNVVFLDDPFSALD-------VHLSDHLMQA-GIlellrddkrTVVLVTHKL-QYLPHAD--WIIAmkDGTIQREGTL 241
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDpitmgvlVKLISELNSAlGV---------TCVVVSHDVpEVLSIADhaYIVA--DKKIVAHGSA 228
|
....
gi 34784298 242 KDFQ 245
Cdd:PRK11831 229 QALQ 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
691-884 |
2.95e-08 |
|
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: 55.19 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 691 HVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAKLPLHTLRSR--LSIILQDPVLFSG-TIRFNL 767
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL----LNLIAGFETPQSGRVLINGVDVTAAPPADrpVSMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 768 D----PEKKCSdstlwealEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 843
Cdd:cd03298 92 GlglsPGLKLT--------AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 34784298 844 ENILQKVVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRGAI 884
Cdd:cd03298 164 RAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-248 |
3.15e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.87 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedPSNPERETAADS-DARSRGPVAYAS 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV-------------KIDGELLTAENVwNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 102 QKPWLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHTNV 177
Cdd:PRK13642 90 PDNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 178 VFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 248
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-248 |
3.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.91 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 16 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSegedpsnpereTAADSDARS-R 94
Cdd:PRK13649 16 TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-----------TSKNKDIKQiR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 GPVAYASQKP--WLLNATVEENITFeSPFNKQRYKmvIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 172
Cdd:PRK13649 85 KKVGLVFQFPesQLFEETVLKDVAF-GPQNFGVSQ--EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 173 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSE 248
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiFQDVD 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-240 |
3.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ----RVSGAVFWNsslpdseGEDpsnperetAADSDA-RSRG 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLYF-------GKD--------IFQIDAiKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKP-WLLNATVEENITFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQRQRISVA 168
Cdd:PRK14246 91 EVGMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 169 RALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 240
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
672-865 |
3.71e-08 |
|
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: 54.80 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrL 749
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS------------------------------TL---L 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SII--LQDPVlfSGTIRFNLDPEKKCSDSTLWE--------------------ALEIAQLKLVVKALPG----------- 796
Cdd:cd03255 48 NILggLDRPT--SGEVRVDGTDISKLSEKELAAfrrrhigfvfqsfnllpdltALENVELPLLLAGVPKkerreraeell 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 797 ---GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAH 865
Cdd:cd03255 126 ervGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTH 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
672-865 |
3.98e-08 |
|
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: 54.84 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDpvlfsgtirFNLDPE--------------KKCSDStlwEALEIAQ--LKLVvkalpgGLDAIITEGGENFSQGQ 813
Cdd:cd03262 79 GMVFQQ---------FNLFPHltvlenitlapikvKGMSKA---EAEERALelLEKV------GLADKADAYPAQLSGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 814 RQLFCLARAFVRKTSIFIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAH 865
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTH 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
672-885 |
4.17e-08 |
|
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: 54.68 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiaklpLHTLRSRL 749
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRML------------------AGLLEPDA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIIL-------QDPVLFSGTIRFNLDPEKKCSDSTLWEALEI---------AQLKLVVKALPGGLD--AIITEGGENFSQ 811
Cdd:cd03266 60 GFATvdgfdvvKEPAEARRRLGFVSDSTGLYDRLTARENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFST 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 812 GQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAIL 885
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
672-900 |
4.62e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.53 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPV-LFSGTI-----RFNLD----PEKKCSdSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLAR 821
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLEnhavPYDEMH-RRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 822 AFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDS 899
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
.
gi 34784298 900 V 900
Cdd:PRK13648 236 L 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
672-886 |
5.14e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.67 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSF---------------SLAFFRMVDMfegriiidgiD 736
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLlkllygeerptsgqvLVNGQDLSRL----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 737 IAKLPLhtLRSRLSIILQDpvlfsgtirFNLDPEKkcsdsTLWE----ALEIAQ-------------LKLV-----VKAL 794
Cdd:COG2884 71 RREIPY--LRRRIGVVFQD---------FRLLPDR-----TVYEnvalPLRVTGksrkeirrrvrevLDLVglsdkAKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 795 PGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTI 870
Cdd:COG2884 135 PHEL-----------SGGEQQRVAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELV 200
|
250
....*....|....*..
gi 34784298 871 LSADL-VMVLKRGAILE 886
Cdd:COG2884 201 DRMPKrVLELEDGRLVR 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-897 |
5.15e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 686 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIA------KLPLHTLRSRLSIILQDPVLF 759
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 760 SG-TIRFNLD-PEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 837
Cdd:PRK14246 103 PHlSIYDNIAyPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 838 SIDMATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILE-------FDKPEKLLSQK 897
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
157-239 |
5.28e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 235
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
|
....
gi 34784298 236 QREG 239
Cdd:PRK09493 215 AEDG 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-218 |
5.42e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSL--LLAtlGEMQRVSGAVFWNsslpdseGE--DPSNPeretaadSDARSRGpVA 98
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLmkILY--GLYQPDSGEILID-------GKpvRIRSP-------RDAIALG-IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLLNA-TVEENI------TFESPFNKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISVARAL 171
Cdd:COG3845 84 MVHQHFMLVPNlTVAENIvlglepTKGGRLDRKAARARIRELSERYGLDVDPD---AKVED----LSVGEQQRVEILKAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL 218
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKL 201
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-248 |
5.55e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEdpsnperETAADSDARSRGPVAYA 100
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII-------IDGD-------LLTEENVWDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKP--WLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQH 174
Cdd:PRK13650 87 FQNPdnQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 175 TNVVFLDDPFSALDvhlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQR 246
Cdd:PRK13650 159 PKIIILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSR 230
|
..
gi 34784298 247 SE 248
Cdd:PRK13650 231 GN 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
157-240 |
9.02e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 235
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEV 243
|
....*
gi 34784298 236 QREGT 240
Cdd:PRK10070 244 VQVGT 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-239 |
1.16e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEdpsnpERETAADSDARSRGpVA 98
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-------GQ-----EMRFASTTAALAAG-VA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLL-NATVEENI---TFESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErginLSGGQRQRISVARAL 171
Cdd:PRK11288 83 IIYQELHLVpEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY----LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TIQREG 239
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-188 |
1.32e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLA---TLGEMQRVSGAVFWNSslpdsegedpsnperETAADSDARSR 94
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNG---------------IPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 95 GPVAYASQK----PWLlnaTVEENITFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQRISVARA 170
Cdd:cd03233 83 GEIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEA 132
|
170
....*....|....*...
gi 34784298 171 LYQHTNVVFLDDPFSALD 188
Cdd:cd03233 133 LVSRASVLCWDNSTRGLD 150
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-247 |
1.55e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPSNPERETAADSDaRSRGP-VA 98
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMR-HVRGAdMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWL-LNA--TVEENITfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQRQRISVARALY 172
Cdd:PRK10261 108 MIFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 173 QHTNVVFLDDPFSALDVhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 247
Cdd:PRK10261 185 CRPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-247 |
1.77e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.98 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGA--VFWNSSLpdsegEDPSNPERETAADSDarsrgpVAY 99
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgRVMAEklEFNGQDL-----QRISEKERRNLVGAE------VAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWL-LNA--TVEENI-----TFESPFNKQRYKMVIEACSLQ--PD----IDILPHgdqtqigergiNLSGGQRQRI 165
Cdd:PRK11022 94 IFQDPMTsLNPcyTVGFQImeaikVHQGGNKKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 240
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGK 237
|
....*..
gi 34784298 241 LKDFQRS 247
Cdd:PRK11022 238 AHDIFRA 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
672-898 |
1.98e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.58 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVD-MFEGRIIIDGIDIAKLPLHT---LR 746
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDgLLEAESGQIIIDGDLLTEENvwdIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 747 SRLSIILQDP-VLFSGT-----IRFNLDpEKKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 820
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGAtveddVAFGLE-NKGIPHEEMKERVNEA-LELV------GMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 821 RAFVRKTSIFIMDEATASID--------MATENILQKVVMtafadrTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEK 892
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQM------TVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
....*.
gi 34784298 893 LLSQKD 898
Cdd:PRK13650 227 LFSRGN 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-252 |
2.06e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIP-TLSNITIRIPRGQLTMIVGQVGCGKSSLLLaTLGEMQRVSGavfwnsslpdseGEDPSNpERETAADSDARSRGP 96
Cdd:PTZ00243 1320 EGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLL-TFMRMVEVCG------------GEIRVN-GREIGAYGLRELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLLNATVEENItfeSPFNKQRYKMV---IEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 173
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV---DPFLEASSAEVwaaLELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 174 HTNVVFLDDPFSALDVHLSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 252
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQIQATVMSAF--SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-227 |
2.46e-07 |
|
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: 53.14 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 30 IPR-GQLTMIVGQVGCGKSSLLLATLGEMQ----RVSGAVFWNSSLPDSEGEDPSNpERETAADSDARSRGPVAYASQKP 104
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKpnlgKFDDPPDWDEILDEFRGSELQN-YFTKLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 105 WLLNATVEENITFESPFNKQRYkmVIEACSLQPdidilphgdqtqIGERGI-NLSGGQRQRISVARALYQHTNVVFLDDP 183
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 34784298 184 FSALDVHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWI 227
Cdd:cd03236 167 SSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
386-573 |
2.51e-07 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 53.58 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 386 LDQSVYAMVFTVLCSLGIALCL------VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTI 459
Cdd:cd18554 37 LDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 460 DQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVA---LLPLAVVC-YFIQKYFRVASRDLQQLDDTTQlpllSHFAETV 535
Cdd:cd18554 117 KDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFYILAvKYFFGRLRKLTKERSQALAEVQ----GFLHERI 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 34784298 536 EGLTTIRAFRYEARFQQkllEYTDSNNiasLFLTAANR 573
Cdd:cd18554 193 QGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
672-895 |
2.65e-07 |
|
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: 54.42 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFsLAFFRMVDMFEGRIIIDGIDIAKLP---------- 741
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEPTSGRIIYHVALCEkcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 742 --------------------------LHTLRSRLSIILQDPvlfsgtirFNLDPEKKCSDSTLwEALEIAQLKlVVKALP 795
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRT--------FALYGDDTVLDNVL-EALEEIGYE-GKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 796 GGLDAI--------ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH 865
Cdd:TIGR03269 148 RAVDLIemvqlshrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 34784298 866 RVHTILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:TIGR03269 228 WPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-269 |
2.88e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.30 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNSS-----LPDSEGEDPSNPERETAADSDARSRG 95
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLkiLA--GELEPDSGEVSIPKGlrigyLPQEPPLDDDLTVLDTVLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVA---YASQKPWLLNATVEENITFESPFNkqrykmVIEACSLQPDIDI------LPHGDQTQ-IGErginLSGGQRQRI 165
Cdd:COG0488 92 LEAeleELEAKLAEPDEDLERLAELQEEFE------ALGGWEAEARAEEilsglgFPEEDLDRpVSE----LSGGWRRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 166 SVARALYQHTNVVFLDDPFSALDVHlsdhlmqaGIL---ELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ 236
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNYPGTVLVVSHdryfldRV-----ATRILELDRGKLT 228
|
250 260 270
....*....|....*....|....*....|....
gi 34784298 237 R-EGTLKDFQRSECQLFEHWKTLMNRQDQELEKE 269
Cdd:COG0488 229 LyPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKE 262
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
157-243 |
2.96e-07 |
|
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: 52.78 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP----HAdwiIAMKD 232
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL-LDKLAAEGAPTLVLVTHHVEEIPpgitHV---LLLKD 218
|
90
....*....|.
gi 34784298 233 GTIQREGTLKD 243
Cdd:COG1119 219 GRVVAAGPKEE 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
671-893 |
3.95e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 671 KIQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIdgidiAKLPLH------- 743
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVE-----GKVTFHgknlyap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 744 -----TLRSRLSIILQDPVLFSGTI-------------RFNLDP--EKKCSDSTLWEALEiAQLKlvvkalpggldaiit 803
Cdd:PRK14243 83 dvdpvEVRRRIGMVFQKPNPFPKSIydniaygaringyKGDMDElvERSLRQAALWDEVK-DKLK--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 804 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVHTI---LSAD 874
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMtafFNVE 226
|
250 260
....*....|....*....|
gi 34784298 875 LVMVLKR-GAILEFDKPEKL 893
Cdd:PRK14243 227 LTEGGGRyGYLVEFDRTEKI 246
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
689-895 |
4.46e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 689 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRS----RLSIILQDpvlfsgtir 764
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 765 FNLDPEKKCSDSTLWeALEIAQLKLVVKAlPGGLDAIITEGGENF--------SQGQRQLFCLARAFVRKTSIFIMDEAT 836
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 837 ASID--MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
157-240 |
5.00e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTI 235
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
....*
gi 34784298 236 QREGT 240
Cdd:PRK11650 214 EQIGT 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
153-239 |
5.40e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.99 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 153 RGIN--LSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWI 227
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRV 175
|
90
....*....|..
gi 34784298 228 IAMKDGTIQREG 239
Cdd:cd03217 176 HVLYDGRIVKSG 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
158-221 |
6.44e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 6.44e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 221
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-246 |
6.60e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.14 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpV 97
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK-------------------------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLL--NATVEENItfeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGergiNLSGGQRQRISVARALYQ 173
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDEL---RDGAPGGTEQEVRGY-LG---RFLFSGDDafKPVG----VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 174 HTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ-REGTLKDFQR 246
Cdd:COG0488 450 PPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHdryfldRV-----ATRILEFEDGGVReYPGGYDDYLE 519
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
23-233 |
6.84e-07 |
|
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: 51.13 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPSN--PEretaadsdarSRGpvAYA 100
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylPE----------ERG--LYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SQKpwllnatVEENITFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARALYQHT 175
Cdd:cd03269 84 KMK-------VIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 176 NVVFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 233
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-243 |
7.25e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.75 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQRVSGAVFWNSSLPDSEGEDpSNPERETAADSDARSRGPVAYASQ 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTL-------MQHFNALLKPSSGTITIAGYH-ITPETGNKNLKKLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQH 174
Cdd:PRK13641 95 EAQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 243
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKE 231
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
397-567 |
7.29e-07 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 52.03 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 397 VLCSLGIALCLVTS-VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 475
Cdd:cd18541 47 LLLALLIGIFRFLWrYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 476 LCVSALTVISYVTPVF-LVALLPL---AVVCYFIQKYFRVASRDLQQ----LDDTTQlpllshfaETVEGLTTIRAF--- 544
Cdd:cd18541 127 LGVLVLVMMFTISPKLtLIALLPLpllALLVYRLGKKIHKRFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFvqe 198
|
170 180
....*....|....*....|....*...
gi 34784298 545 -RYEARFQQKLLEYTDSNN----IASLF 567
Cdd:cd18541 199 eAEIERFDKLNEEYVEKNLrlarVDALF 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
672-900 |
8.90e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYD-SSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 750
Cdd:PRK13642 5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 751 IILQDP------VLFSGTIRFNLDPEKKCSDSTLweaLEIAQLKLVVKALPggldaIITEGGENFSQGQRQLFCLARAFV 824
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMENQGIPREEMI---KRVDEALLAVNMLD-----FKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 825 RKTSIFIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSV 900
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
395-900 |
1.09e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.28 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 395 FTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID---QHIPStlecLS 471
Cdd:PRK10522 54 FLGLLLLLMAVTLGSQLALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITiafVRLPE----LV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 472 RSTLLCVSALTVISYVTP-VFLVALLPLAVVcyFIQKYFRVAS-----RDLQQLDDTtqlpLLSHFAETVEG-----LTT 540
Cdd:PRK10522 130 QGIILTLGSAAYLAWLSPkMLLVTAIWMAVT--IWGGFVLVARvykhmATLRETEDK----LYNDYQTVLEGrkeltLNR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 541 IRA-FRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMeyigacvvliaaatsisnslhrelsAGLVGLgltyALMVS 619
Cdd:PRK10522 204 ERAeYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSNIMM-------------------------LGAIGL----VFYMA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 620 NYLNWmvrnlADMEIQ--------------LGAVKRIHTLL----------KTEAESYEGLLAPSLIPKNWPdqgKIQIQ 675
Cdd:PRK10522 255 NSLGW-----ADTNVAatysltllflrtplLSAVGALPTLLsaqvafnklnKLALAPYKAEFPRPQAFPDWQ---TLELR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 676 NLSVRYDS---SLKPVlkhvNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 752
Cdd:PRK10522 327 NVTFAYQDngfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 753 LQDPVLFSGTirfnLDPEKKCSDSTLWEA-LEIAQLKlvvkalpgglDAIITEGGE----NFSQGQRQLFCLARAFVRKT 827
Cdd:PRK10522 403 FTDFHLFDQL----LGPEGKPANPALVEKwLERLKMA----------HKLELEDGRisnlKLSKGQKKRLALLLALAEER 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 828 SIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSV 900
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-895 |
1.17e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 686 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------LRSRLSIILQDPVLF 759
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvleFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 760 SGTIRFN---------LDPEKkcsdstlwEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 830
Cdd:PRK14271 114 PMSIMDNvlagvrahkLVPRK--------EFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 831 IMDEATASIDMATENILQKVVMTaFADR-TVVTIAHRV-HTILSADLVMVLKRGAILEFDKPEKLLS 895
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-216 |
1.30e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATlgeMQRvsgavfwnsSLPDSEGeDPS---NPERETAADSDARSrgpvAY 99
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFR---------SPKGVKG-SGSvllNGMPIDAKEMRAIS----AY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWLLNA-TVEENITFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRISVA 168
Cdd:TIGR00955 104 VQQDDLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRLAFA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTH 216
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-248 |
1.32e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQRVSGAVfwnssLPDSeGEDPSNPERET-AADSDARSRGpV 97
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV-----PPDS-GTLEIGGNPCArLTPAKAHQLG-I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 98 AYASQKPWLL-NATVEENITFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSGGQRQRISVARAL 171
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 248
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
674-715 |
1.34e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.99 E-value: 1.34e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 34784298 674 IQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 715
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL 40
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
410-630 |
1.56e-06 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 50.93 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 410 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 489
Cdd:cd18545 61 IYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 490 VF-LVAL--LP-LAVVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYE----ARFQQKLLEYTDSN 561
Cdd:cd18545 141 RLaLVTLavLPlLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFAREdeneEIFDELNRENRKAN 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 562 ----NIASLF-----LTAAnrwlevrmeyIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYA-------LMVSNYLNWM 625
Cdd:cd18545 217 mravRLNALFwplveLISA----------LGTALVYWYGGKLV---LGGAITVGVLVAFIGYVgrfwqpiRNLSNFYNQL 283
|
....*
gi 34784298 626 VRNLA 630
Cdd:cd18545 284 QSAMA 288
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
807-905 |
1.75e-06 |
|
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: 50.03 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 807 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVMVLKRG 882
Cdd:cd03299 128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNG 206
|
90 100
....*....|....*....|....
gi 34784298 883 AILEFDKPEKLLSQKDSVF-ASFV 905
Cdd:cd03299 207 KLIQVGKPEEVFKKPKNEFvAEFL 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
157-233 |
1.75e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 231
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 34784298 232 DG 233
Cdd:PRK15134 232 NG 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
672-907 |
1.82e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.50 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDP--VLFSGTI-------RFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARA 822
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 823 FVRKTSIFIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEkLLSQ 896
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTD 227
|
250
....*....|.
gi 34784298 897 KDSVFASFVRA 907
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-219 |
1.82e-06 |
|
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: 50.02 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPSNPERETAAdsdarsRGPVAY 99
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-------GLVPWKRRKKFLR------RIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 A--SQKPWLLNA----TVEENITFESPFnkqRYKMVIEACSlqpdiDILPHGDQTQIGERgiNLSGGQRQRISVARALYQ 173
Cdd:cd03267 101 GqkTQLWWDLPVidsfYLLAAIYDLPPA---RFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLH 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 34784298 174 HTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 219
Cdd:cd03267 171 EPEILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-246 |
2.09e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 21 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEM----QRVSGAVfwnssLPDSEgedpsnpereTAADSDARSRgP 96
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRV-----LLDGK----------PVAPCALRGR-K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPwllnatveenitfESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GINLSGGQR 162
Cdd:PRK10418 81 IATIMQNP-------------RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFEMSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMKDGTIQR 237
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
250
....*....|
gi 34784298 238 EGTLKD-FQR 246
Cdd:PRK10418 222 QGDVETlFNA 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
672-865 |
2.09e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.16 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------- 744
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSprtdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 745 LRSRLSIILQDPVLFSGTI--------RFNLDPEKKCSDSTLWEALEIAQLKLVVKAlpggldaIITEGGENFSQGQRQL 816
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 34784298 817 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 865
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-233 |
2.34e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQRVSGAVFWNSSlpdsEGEDPSNPERETAAD-SDARSRGp 96
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTL-------MKVLSGVYPHGTY----EGEIIFEGEELQASNiRDTERAG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPWLL-NATVEENItF---E-SPFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGergiNLSGGQRQRISVA 168
Cdd:PRK13549 84 IAIIHQELALVkELSVLENI-FlgnEiTPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG----NLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 233
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-233 |
2.39e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 18 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWNSSlpdsegedpsnpERETAADSDARSRG 95
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGS------------PLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 96 PVAYASQKPWLLNATVEENI----TFESPFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQRQRISVA 168
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 233
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
596-896 |
2.66e-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: 50.96 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 596 SNSLHRELSAGLVGLGLTyaLMVSNYLNWMVRNLADMEIQL--GAVKRIHTLLKTEAESYEGllAPSLIPKNWPDQGK-- 671
Cdd:TIGR03269 204 AKLVHNALEEAVKASGIS--MVLTSHWPEVIEDLSDKAIWLenGEIKEEGTPDEVVAVFMEG--VSEVEKECEVEVGEpi 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPVLKHVNAL---IAPGQKIGICGRTGSGKSSFS--LA----------FFRM----VDMFEgriii 732
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSkiIAgvleptsgevNVRVgdewVDMTK----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 733 dgidiaklPLHTLRSR----LSIILQDPVLFsgtirfnldPEKKCSDStLWEAL------EIAQLKLVVKALPGGLD--- 799
Cdd:TIGR03269 355 --------PGPDGRGRakryIGILHQEYDLY---------PHRTVLDN-LTEAIglelpdELARMKAVITLKMVGFDeek 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 800 --AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-AD 874
Cdd:TIGR03269 417 aeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCD 496
|
330 340
....*....|....*....|..
gi 34784298 875 LVMVLKRGAILEFDKPEKLLSQ 896
Cdd:TIGR03269 497 RAALMRDGKIVKIGDPEEIVEE 518
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-216 |
2.67e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNssLPDsegeDPSNPEReTAADSDARsRGPVAYASQ 102
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--VPD----NQFGREA-SLIDAIGR-KGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 kpwLLNAT-VEENITFESPFNkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLD 181
Cdd:COG2401 118 ---LLNAVgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 34784298 182 DPFSALDVHLSdHLMQAGILELLRDDKRTVVLVTH 216
Cdd:COG2401 162 EFCSHLDRQTA-KRVARNLQKLARRAGITLVVATH 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-216 |
3.09e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 32 RGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpsNPERETAADSDARSrgpvayasqkpwllnatv 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI------------DGEDILEEVLDQLL------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 112 eenitfespfnkqrykmvieacslqpdidilphgdQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHL 191
Cdd:smart00382 51 -----------------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQ 95
|
170 180
....*....|....*....|....*....
gi 34784298 192 SDHLMQAGILELL----RDDKRTVVLVTH 216
Cdd:smart00382 96 EALLLLLEELRLLlllkSEKNLTVILTTN 124
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
388-560 |
3.28e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 49.74 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 388 QSVYAMVFTVLcsLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDC----NTIDQHI 463
Cdd:cd18551 37 GLLALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 464 PSTLEclsrSTLLCVSALTVISYVTPV-FLVAL--LPLAVVCYF-IQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGL 538
Cdd:cd18551 115 PQLVT----GVLTVVGAVVLMFLLDWVlTLVTLavVPLAFLIILpLGRRIRKASKRAQD-----ALGELSAALErALSAI 185
|
170 180
....*....|....*....|..
gi 34784298 539 TTIRAFRYEARFQQKLLEYTDS 560
Cdd:cd18551 186 RTVKASNAEERETKRGGEAAER 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-209 |
3.51e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 10 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPSNPER------ 83
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRrdiqfi 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 84 --ETAADSDARSrgPVAYASQKPWLLNATVEENITfespfnKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLSGG 160
Cdd:PRK10261 407 fqDPYASLDPRQ--TVGDSIMEPLRVHGLLPGKAA------AARVAWLLERVGLLPEHAWrYPH-----------EFSGG 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 34784298 161 QRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR 209
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-218 |
3.52e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 5 CVQIIGGFFTwtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnperE 84
Cdd:TIGR01257 930 CVKNLVKIFE--PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG-------GKDI-----E 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 85 TAADSDARSRGpvaYASQKPWLLN-ATVEENITFESPFNKQRYkmviEACSLQPDIDILPHGDQTQIGERGINLSGGQRQ 163
Cdd:TIGR01257 996 TNLDAVRQSLG---MCPQHNILFHhLTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQR 1068
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 164 RISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDK--RTVVLVTHKL 218
Cdd:TIGR01257 1069 KLSVAIAFVGDAKVVVLDEPTSGVDPY-----SRRSIWDLLLKYRsgRTIIMSTHHM 1120
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
385-570 |
3.77e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 49.80 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 385 ALDQSVYAMVFTVL--CSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILA--------PMRFFETTPLGSILNRFSS 454
Cdd:cd18546 25 GIDSGVRAGDLGVLllAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRvfahlqrlSLDFHERETSGRIMTRMTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 455 DCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFiqkyFRVASRDLQQLDDTTQLPLLSH 530
Cdd:cd18546 105 DIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRW----FRRRSSRAYRRARERIAAVNAD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 34784298 531 FAETVEGLTTIRAFRYEARFQQKLLEYTDSN---NIASLFLTA 570
Cdd:cd18546 181 LQETLAGIRVVQAFRRERRNAERFAELSDDYrdaRLRAQRLVA 223
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
392-606 |
3.89e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 49.77 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 392 AMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECLS 471
Cdd:cd18567 45 AIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 472 RSTLLCVSALTVI-SYVTPVFLVALlpLAVVCYFI-----QKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 545
Cdd:cd18567 124 LDGLMAILTLVMMfLYSPKLALIVL--AAVALYALlrlalYPPLRRATEEQIVASAKEQ----SHFLETIRGIQTIKLFG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 546 YEARFQQKLLE-YTDSNN------IASLFLTAANRWLeVRMEYIgacVVLIAAATSIsnsLHRELSAG 606
Cdd:cd18567 198 REAEREARWLNlLVDAINadirlqRLQILFSAANGLL-FGLENI---LVIYLGALLV---LDGEFTVG 258
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-240 |
4.19e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.11 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 20 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpDSEGEDPSNPERETAAdsdARSRGPVAY 99
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK--DITDWQTAKIMREAVA---IVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQkpwllnaTVEENITFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALYQHTNVV 178
Cdd:PRK11614 93 SRM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 179 FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 240
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFD--TIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
672-902 |
4.83e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.70 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYD------------SSLKPVlKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAK 739
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwqppKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 740 L---PLHTLRSRLSIILQDPvLFSgtirfnLDPEKKCSD------STLWEALEIAQLKLVVKAL---PGGLDAIITEGGE 807
Cdd:PRK15079 88 MkddEWRAVRSDIQMIFQDP-LAS------LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 808 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHR---VHTIlsADLVMVLK 880
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHDlavVKHI--SDRVLVMY 236
|
250 260
....*....|....*....|..
gi 34784298 881 RGAILEfdkpeklLSQKDSVFA 902
Cdd:PRK15079 237 LGHAVE-------LGTYDEVYH 251
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
672-895 |
5.71e-06 |
|
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: 48.20 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTlRSRLSI 751
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 IL--QDPVLFSG-TIRfnldpekkcsdstlwEALEIAQLKLVVKALPGGLDAII-----------TEGGeNFSQGQRQLF 817
Cdd:cd03224 78 GYvpEGRRIFPElTVE---------------ENLLLGAYARRRAKRKARLERVYelfprlkerrkQLAG-TLSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 818 CLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
672-715 |
7.28e-06 |
|
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: 7.28e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 715
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
670-905 |
8.03e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 48.92 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 670 GKIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRsrl 749
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKST-----------------------------LLR--- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 sII--LQDPVlfSGTIRFN------LDPEK-----------------------------KCS----DSTLWEALEIAQLK 788
Cdd:COG3839 48 -MIagLEDPT--SGEILIGgrdvtdLPPKDrniamvfqsyalyphmtvyeniafplklrKVPkaeiDRRVREAAELLGLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 789 LVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVVMTafadrTV 860
Cdd:COG3839 125 DLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TI 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 34784298 861 -VTiahrvH------TIlsADLVMVLKRGAILEFDKPEKLLSQKDSVF-ASFV 905
Cdd:COG3839 189 yVT-----HdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANLFvAGFI 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
158-218 |
8.07e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 8.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTHKL 218
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-243 |
8.16e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpsNPERETAADSDARSRGpVA 98
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN------------NINYNKLDHKLAAQLG-IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLLNA-TVEENI--------------TFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQ 163
Cdd:PRK09700 84 IIYQELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 164 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 242
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVS 230
|
.
gi 34784298 243 D 243
Cdd:PRK09700 231 D 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-248 |
1.29e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.24 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 152 ERGIN-LSGGQRQRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 228
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL--HQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 34784298 229 AM------KDGTIQREGTLKDFQRSE 248
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANP 586
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
415-642 |
1.50e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 47.89 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 415 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LV 493
Cdd:cd18563 69 RLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLaLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 494 ALLPLAVVCYFIQKYFRVASRDLQQL----DDTTqlpllSHFAETVEGLTTIRAF---RYE-ARFQQKLLEYTDSNNIAS 565
Cdd:cd18563 149 VLIPVPLVVWGSYFFWKKIRRLFHRQwrrwSRLN-----SVLNDTLPGIRVVKAFgqeKREiKRFDEANQELLDANIRAE 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 566 LFLTAANRWLEVRMEyIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 642
Cdd:cd18563 224 KLWATFFPLLTFLTS-LGTLIVWYFGGRQV---LSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-188 |
1.58e-05 |
|
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: 47.15 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnpereTAADSDARSRGPVAYASQ 102
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD-------GQDI------TKLPMHKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLL-NATVEENI--TFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVF 179
Cdd:cd03218 83 EASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLL 156
|
....*....
gi 34784298 180 LDDPFSALD 188
Cdd:cd03218 157 LDEPFAGVD 165
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
385-553 |
1.64e-05 |
|
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: 47.63 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 385 ALDQSVYAMVFTVLcsLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIP 464
Cdd:cd18780 40 ALNQAVLILLGVVL--IGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 465 STLECLSRSTLLCVSALTVISYV----TPVFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLT 539
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTswklTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQD-----ALAAASTVAEeSISNIR 192
|
170
....*....|....
gi 34784298 540 TIRAFRYEARFQQK 553
Cdd:cd18780 193 TVRSFAKETKEVSR 206
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
780-905 |
1.96e-05 |
|
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: 47.87 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 780 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVV 851
Cdd:TIGR01187 83 EALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkTIQEQLG 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 852 MtafadrTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKDSVF-ASFV 905
Cdd:TIGR01187 152 I------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
672-899 |
2.25e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 46.67 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslkpVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVD---MFEGRIIIDGIDIAKLPLhtlr 746
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLnlIAGFLPPDsgrILWNGQDLTALPPAERPV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 747 srlSIILQDPVLFSG-TIRFN----LDPEKKCSD---STLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 818
Cdd:COG3840 74 ---SMLFQENNLFPHlTVAQNiglgLRPGLKLTAeqrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 819 LARAFVRKTSIFIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
....
gi 34784298 896 QKDS 899
Cdd:COG3840 220 GEPP 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
689-898 |
2.34e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.13 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 689 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV----DMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGT 762
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 763 IRFNLDPEKKCSDSTLWEALEIAqLKLVVKAlpGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-M 841
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKA-LKWLKKV--GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 842 ATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKD 898
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
155-216 |
2.42e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.41 E-value: 2.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 155 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTH 216
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
780-906 |
2.77e-05 |
|
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: 46.87 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 780 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-- 857
Cdd:cd03294 143 EALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElq 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 858 RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQ-KDSVFASFVR 906
Cdd:cd03294 212 KTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR 262
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
672-886 |
3.52e-05 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 46.19 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDS--SLKPVLKHVNALIAPGQKIGICGRTGSGKSSF----------------------------SLAFFR 721
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnilggldrptsgevlidgqdisslserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 722 mvdmfegriiidgidiaklplhtlRSRLSIILQDpvlfsgtirFNLDPE-----------------KKCSDSTLWEALEI 784
Cdd:COG1136 85 ------------------------RRHIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLER 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 785 AQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFAD---RTV 860
Cdd:COG1136 132 VGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTI 198
|
250 260
....*....|....*....|....*.
gi 34784298 861 VTIAHRVHTILSADLVMVLKRGAILE 886
Cdd:COG1136 199 VMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
33-243 |
3.94e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 33 GQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlPDSEGEDPSNPERETAADSD-ARSRGPVAYASQkpwLLNATV 111
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-PLHFGDYSYRSQRIRMIFQDpSTSLNPRQRISQ---ILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 112 EENITFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH 190
Cdd:PRK15112 115 RLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 34784298 191 LSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 243
Cdd:PRK15112 184 MRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
147-239 |
4.25e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 147 QTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPH 223
Cdd:PRK14271 154 KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARI 228
|
90
....*....|....*.
gi 34784298 224 ADWIIAMKDGTIQREG 239
Cdd:PRK14271 229 SDRAALFFDGRLVEEG 244
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
387-617 |
4.28e-05 |
|
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: 46.54 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 387 DQSVYAMVFTVLCSLGIALCL-----VTSVTVEWTGLKVAKRLHRSLLNRIIlapmRFFETTPLGSILNRFSSDCNTIDQ 461
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAgirggLFTLAMARLNIRIRNLLFRSIVSQEI----GFFDTVKTGDITSRLTSDTTTMSD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 462 HIPSTLECLSRSTllcVSALTVIsyvtpVFLVAL-----------LPL-AVVCYFIQKYFRVASRDLQqlddtTQLPLLS 529
Cdd:cd18784 109 TVSLNLNIFLRSL---VKAIGVI-----VFMFKLswqlslvtligLPLiAIVSKVYGDYYKKLSKAVQ-----DSLAKAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 530 HFA-ETVEGLTTIRAF--------RYEARFQQ-------KLLEYTDSNNIASLFLTAanrwLEVRMEYIGACVVLIAAAT 593
Cdd:cd18784 176 EVAeETISSIRTVRSFanedgeanRYSEKLKDtyklkikEALAYGGYVWSNELTELA----LTVSTLYYGGHLVITGQIS 251
|
250 260
....*....|....*....|....*....
gi 34784298 594 S---ISNSLHR-ELSAGLVGLGLTYA-LM 617
Cdd:cd18784 252 GgnlISFILYQlELGSCLESVGSVYTgLM 280
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
414-561 |
4.41e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 46.27 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 414 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-L 492
Cdd:cd18542 64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 493 VALLPLAVVCYFIQKYFRVASRDLQQLDDttQLPLLSHFA-ETVEGLTTIRAF---RYE-ARFQQKLLEYTDSN 561
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKKVRPAFEEIRE--QEGELNTVLqENLTGVRVVKAFareDYEiEKFDKENEEYRDLN 215
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-188 |
4.76e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ----RVSGAVFWNSSLPDsegedpsnperetaaDSDARSRGPVA 98
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPE---------------EIKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQK----PWLlnaTVEENITF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGInlSGGQ 161
Cdd:TIGR00956 142 YNAETdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV--SGGE 214
|
170 180
....*....|....*....|....*..
gi 34784298 162 RQRISVARALYQHTNVVFLDDPFSALD 188
Cdd:TIGR00956 215 RKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
672-905 |
5.24e-05 |
|
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: 45.69 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAK----LPLHtlRS 747
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFETPTSGEILLDGKditnLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 748 RLSIILQDPVLFS-----GTIRFNLDpEKKCSDSTLWEALEiAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARA 822
Cdd:cd03300 73 PVNTVFQNYALFPhltvfENIAFGLR-LKKLPKAEIKERVA-EALDLV------QLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 823 FVRKTSIFIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILSADLVMVLKRGAILEFDKPEKLLSQKD 898
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
....*...
gi 34784298 899 SVF-ASFV 905
Cdd:cd03300 224 NRFvADFI 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
672-895 |
6.24e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 46.37 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDPVL---FSG-----------TIRFnlDPEKKCSDSTLWEALEiaqlklvvkalPGGLDAIITEGGENFSQGQRQLF 817
Cdd:PRK09536 82 VPQDTSLsfeFDVrqvvemgrtphRSRF--DTWTETDRAAVERAME-----------RTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 818 CLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLSA---DLVMVLKRGAILEFDKPEKL 893
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPPADV 226
|
..
gi 34784298 894 LS 895
Cdd:PRK09536 227 LT 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
672-884 |
6.92e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVDMFEGRIIIDGIDIAKlPLHTLRSRL 749
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLFSG-TIRFNL--------DPEKKCSDstLWEALEiAQLKLVVKAlpGGLDAiiteggenfsqGQRQLFCLA 820
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENIlfglpkrqASMQKMKQ--LLAALG-CQLDLDSSA--GSLEV-----------ADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34784298 821 RAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAI 884
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-243 |
7.50e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGED--PSNPeretaadSDARSRGpVAYASQ 102
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN-------GKDisPRSP-------LDAVKKG-MAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KP----WLLNATVEENITFESPFNKQRYKMVI----------EACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVA 168
Cdd:PRK09700 346 SRrdngFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVLIS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 169 RALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLR---DDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 243
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVG-----AKAEIYKVMRqlaDDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
155-241 |
7.92e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 155 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKD 232
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQ 204
|
....*....
gi 34784298 233 GTIQREGTL 241
Cdd:PRK11144 205 GKVKAFGPL 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
157-216 |
9.13e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.57 E-value: 9.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 216
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-219 |
9.35e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegEDPSnperetAADSDARSRGPVA 98
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDIS------LLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWL---------LNATVE--ENITFESpfNKQRYKMVIEACSLQPDIDILphgdqtqigerGINLSGGQRQRISV 167
Cdd:PRK10895 82 YLPQEASIfrrlsvydnLMAVLQirDDLSAEQ--REDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 34784298 168 ARALYQHTNVVFLDDPFSALD-VHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 219
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-235 |
9.36e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 26 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnssLPDSEGEDPSNPERETAAD-----SDARSRGPVAYA 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV-----YLDGKPIDIRSPRDAIRAGimlcpEDRKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 101 SqkpwllnatVEENITFESPFNKQRYKMVI----EACSLQPDIDIL----PHGDQtQIGergiNLSGGQRQRISVARALY 172
Cdd:PRK11288 347 S---------VADNINISARRHHLRAGCLInnrwEAENADRFIRSLniktPSREQ-LIM----NLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 173 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 235
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYN--VIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-218 |
9.45e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 9.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 155 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL 218
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
676-900 |
1.05e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.00 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 676 NLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIIL 753
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 754 QDP---VLFS---GTIRFNLdpekkcsdstlwEALEIAQLKLVVKALpgglDAIITEGGENF--------SQGQRQLFCL 819
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSL------------RNLGVPEAEITRRVD----EALTLVDAQHFrhqpiqclSHGQKKRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 820 ARAFVRKTSIFIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLL 894
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
....*.
gi 34784298 895 SQKDSV 900
Cdd:PRK13638 225 ACTEAM 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
662-905 |
1.14e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.60 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 662 IPKNWPDQGK-----IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGID 736
Cdd:PRK11607 5 IPRPQAKTRKaltplLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 737 IAKLPLHT--LRSRLSIILQDPVLF-----SGTIRFNLDPEKKCSD---STLWEALEIAQLKLVVKALPGGLdaiitegg 806
Cdd:PRK11607 79 DGVDLSHVppYQRPINMMFQSYALFphmtvEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQL-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 807 enfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRvhtilsad 874
Cdd:PRK11607 151 ---SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGR-------- 219
|
250 260 270
....*....|....*....|....*....|..
gi 34784298 875 lVMVLKRGAILEFDKPEKLLSQKDSVF-ASFV 905
Cdd:PRK11607 220 -IAIMNRGKFVQIGEPEEIYEHPTTRYsAEFI 250
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
672-898 |
1.21e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.79 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 751
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 752 ILQDP--VLFS---------GTIRFNLDPEkkcsdsTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 820
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEE------TVAHRVSSA-LHML------GLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 821 RAFVRKTSIFIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 34784298 896 QKD 898
Cdd:PRK13652 228 QPD 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-238 |
1.38e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 38 IVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGE--DPSNPeretaadSDARSRGpVAYAS----QKPWLLNATV 111
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLD-------GKpvRIRSP-------RDAIRAG-IAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 112 EENITFeSPFNKQRYKMVI-------EACSLQPDIDILPHGDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPF 184
Cdd:COG1129 348 RENITL-ASLDRLSRGGLLdrrreraLAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34784298 185 SALDVhlsdhlmqaG----ILELLR---DDKRTVVLVThklQYLP----HADWIIAMKDGTIQRE 238
Cdd:COG1129 423 RGIDV---------GakaeIYRLIRelaAEGKAVIVIS---SELPellgLSDRILVMREGRIVGE 475
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
696-842 |
1.39e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.19 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 696 IAPGQKIGICGRTGSGKSSF-SL-AFFRMVD---MFEGRIIIDGIDIAKLPLhtlrsrlSIILQDPVLFSG-TIRFN--- 766
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLlNLiAGFLTPAsgsLTLNGQDHTTTPPSRRPV-------SMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 767 -LDPEKKCSDSTLWEALEIAQ---LKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA 842
Cdd:PRK10771 95 gLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-231 |
1.55e-04 |
|
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: 43.12 E-value: 1.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 157 LSGGQRQRISVARAL----YQHTNVVFLDDPFSALDvhLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMK 231
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLD--PRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
110-188 |
1.71e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.25 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 110 TVEENI-----TFESPFNKQRYKMVieacSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVFLDDPF 184
Cdd:COG1137 94 TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
....
gi 34784298 185 SALD 188
Cdd:COG1137 165 AGVD 168
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
157-216 |
1.89e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.82 E-value: 1.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 216
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
389-553 |
1.92e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 44.39 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 389 SVYAMVFTVLcslGIALCLVTSVTV---EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID----Q 461
Cdd:cd18577 47 NKYALYFVYL---GIGSFVLSYIQTacwTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQdgigE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 462 HIPSTLECLSrstlLCVSALtVISYV---------TPVFLVALLPLAVVCYFIQKYFRvasrdlQQLDDTTQlplLSHFA 532
Cdd:cd18577 124 KLGLLIQSLS----TFIAGF-IIAFIyswkltlvlLATLPLIAIVGGIMGKLLSKYTK------KEQEAYAK---AGSIA 189
|
170 180
....*....|....*....|..
gi 34784298 533 -ETVEGLTTIRAFRYEARFQQK 553
Cdd:cd18577 190 eEALSSIRTVKAFGGEEKEIKR 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-220 |
1.95e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpVAYASQ 102
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLE-------------------------VAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLLNA--TVEENITFespfNKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQH 174
Cdd:PRK11147 390 HRAELDPekTVMDNLAE----GKQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 34784298 175 TNVVFLDDPFSALDVHLSDHLMqagilELLRDDKRTVVLVTHKLQY 220
Cdd:PRK11147 459 SNLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
698-891 |
2.52e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 698 PGQKIGICGRTGSGKSSFSLAFFRMVDmfegriiidgidiaklplhtlRSRLSIILQDPVLFSGTIRFNLdpekkcsdst 777
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG---------------------PPGGGVIYIDGEDILEEVLDQL---------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 778 lwealeiaqlklvvkalpggLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-- 855
Cdd:smart00382 50 --------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 34784298 856 -----ADRTVVTIAHRVHTILSADLVMVLKRgaILEFDKPE 891
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRRRFDR--RIVLLLIL 148
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
156-227 |
2.64e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.54 E-value: 2.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 156 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 227
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
35-216 |
3.23e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 35 LTMIVGQVGCGKSSLLLAtlgemqrVSGAVFWNSSLPDSEGEDPS--NPERETAadsdarsrgpvayasqkpwllnatve 112
Cdd:cd03279 30 LFLICGPTGAGKSTILDA-------ITYALYGKTPRYGRQENLRSvfAPGEDTA-------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 113 eNITFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHTNVV--- 178
Cdd:cd03279 77 -EVSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGARlea 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 34784298 179 -FLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTH 216
Cdd:cd03279 155 lFIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
797-885 |
3.38e-04 |
|
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: 43.19 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 797 GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-AD 874
Cdd:cd03219 132 GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlAD 211
|
90
....*....|.
gi 34784298 875 LVMVLKRGAIL 885
Cdd:cd03219 212 RVTVLDQGRVI 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-218 |
3.39e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpVAYASQ 102
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR-------------------------IGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 103 KPWLlNATVeenitfesPFNKQRYKMvieacsLQPDI---DILPHGDQTQIGERgIN-----LSGGQRQRISVARALYQH 174
Cdd:PRK09544 75 KLYL-DTTL--------PLTVNRFLR------LRPGTkkeDILPALKRVQAGHL-IDapmqkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 34784298 175 TNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRT----VVLVTHKL 218
Cdd:PRK09544 139 PQLLVLDEPTQGVDVN-----GQVALYDLIDQLRREldcaVLMVSHDL 181
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
671-901 |
3.50e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.46 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 671 KIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 750
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 751 IILQDPVLFSG-TIRfNLDPEKKCSDSTLWEALEIAQLKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTS 828
Cdd:PRK11231 80 LLPQHHLTPEGiTVR-ELVAYGRSPWLSLWGRLSAEDNARVNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 829 IFIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQK--DSVF 901
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGllRTVF 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
686-900 |
3.89e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 686 KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDMFEGRIIIDGIDIAKlplHTLRsRLSIILQDPVLFSG-T 762
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 763 IRFNLdpeKKCSDSTLWEALEiAQLKLVVKalpgglDAIITEGG----EN----------FSQGQRQLFCLARAFVRKTS 828
Cdd:PLN03211 157 VRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 829 IFIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILsaDLVMVLKRGAILEFDKPEKLLSQKDSV 900
Cdd:PLN03211 227 LLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
672-713 |
4.31e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.76 E-value: 4.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 672 IQIQNLSVRY------DSSLK--------------PVLKHVNALIAPGQKIGICGRTGSGKS 713
Cdd:COG1134 5 IEVENVSKSYrlyhepSRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS 66
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-217 |
4.73e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 23 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlgemQRVSGAVFwnsslpdSEGEDPSN-PERETaadSDARSRGPVay 99
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLnvLA-----ERVTTGVI-------TGGDRLVNgRPLDS---SFQRSIGYV-- 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 100 ASQKPWLLNATVEENITFE---------SPFNKQRY-KMVIEACSLQPDIDILphgdqtqIGERGINLSGGQRQRISVAR 169
Cdd:TIGR00956 842 QQQDLHLPTSTVRESLRFSaylrqpksvSKSEKMEYvEEVIKLLEMESYADAV-------VGVPGEGLNVEQRKRLTIGV 914
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 34784298 170 ALYQHTN-VVFLDDPFSALDVHLSdhlmqAGILELLR---DDKRTVVLVTHK 217
Cdd:TIGR00956 915 ELVAKPKlLLFLDEPTSGLDSQTA-----WSICKLMRklaDHGQAILCTIHQ 961
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
423-554 |
5.28e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 42.85 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 423 RLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIdQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPL 498
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPplalVALASLPPL 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 499 AVVCYFIQKYFRVASRDLQQL--DDTTqlpllsHFAETVEGLTTIRAFRYEARFQQKL 554
Cdd:cd18543 152 VLVARRFRRRYFPASRRAQDQagDLAT------VVEESVTGIRVVKAFGRERRELDRF 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-233 |
5.29e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 19 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsegedpSNPERETAADSDARSRGPVA 98
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF------------QGKEIDFKSSKEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 99 YASQKPWLLNATVEENITF-----ESPFNKQRyKMVIEACSL--QPDIDILPHgdqtqigERGINLSGGQRQRISVARAL 171
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLgryptKGMFVDQD-KMYRDTKAIfdELDIDIDPR-------AKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 172 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDG 233
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
672-898 |
5.52e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.11 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSL---KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR---------MVDMFEGRIIidgidiaK 739
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkiIIDGVDITDK-------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 740 LPLHTLRSRLSIILQDP--VLFSGT----IRF---NLDPEKKCSDSTLWEALEIAQLKlvvkalpggLDAIITEGGENFS 810
Cdd:PRK13637 76 VKLSDIRKKVGLVFQYPeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 811 QGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEF 887
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQ 226
|
250
....*....|.
gi 34784298 888 DKPEKLLSQKD 898
Cdd:PRK13637 227 GTPREVFKEVE 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
672-905 |
6.06e-04 |
|
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: 42.33 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAK-LPLHTLRSR-L 749
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGLERPDSGTILFGGEdATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDPVLF-----SGTIRFNLDPEKKcsdSTLWEALEIAQ-----LKLVvkalpgGLDAIITEGGENFSQGQRQLFCL 819
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRVKPR---SERPPEAEIRAkvhelLKLV------QLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 820 ARAFVRKTSIFIMDEATASIDMATENILQKVVmTAFADRTVVT---IAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 34784298 896 QKDSVF-ASFV 905
Cdd:cd03296 227 HPASPFvYSFL 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
672-896 |
6.16e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.77 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRY----DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM---------VDMFEGRIIIDgidia 738
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlipsegkvyVDGLDTSDEEN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 739 klpLHTLRSRLSIILQDP------------VLFSGTirfNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiitegg 806
Cdd:PRK13633 80 ---LWDIRNKAGMVFQNPdnqivativeedVAFGPE---NLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 807 enfSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILSADLVMVLK 880
Cdd:PRK13633 146 ---SGGQKQRVAIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMD 218
|
250
....*....|....*.
gi 34784298 881 RGAILEFDKPEKLLSQ 896
Cdd:PRK13633 219 SGKVVMEGTPKEIFKE 234
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
106-241 |
6.98e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 106 LLNATVEE-NITFesPFNKQrykmvIEAcSLQPDIDI----LPhgdqtqIGERGINLSGGQRQRISVARALY---QHTNV 177
Cdd:PRK00635 1658 LLQTPIEEvAETF--PFLKK-----IQK-PLQALIDNglgyLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTL 1723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784298 178 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 241
Cdd:PRK00635 1724 FLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKI 1785
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
672-715 |
7.62e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 42.45 E-value: 7.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 715
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTL 44
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
145-190 |
8.32e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.00 E-value: 8.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 34784298 145 GDQTQ-IGErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH 190
Cdd:TIGR03719 435 SDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
156-218 |
8.35e-04 |
|
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: 43.23 E-value: 8.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34784298 156 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSDHLMQAGILELLRDDKRTVVLVTHKL 218
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
155-236 |
9.03e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 155 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 234
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
..
gi 34784298 235 IQ 236
Cdd:PRK10522 527 LS 528
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
386-606 |
9.93e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 42.16 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 386 LDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLK------VAKRLHRSLL----NRIILAPMRFFETTPLGSILNRFSSD 455
Cdd:cd18568 29 LDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRqylldyFANRIDLSLLsdfyKHLLSLPLSFFASRKVGDIITRFQEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 456 cNTIdqhipstLECLSRSTL-LCVSALTVISYVTPVF-------LVAL---LPLAVVCYFIQKYFRVASRDLQQLDDTTQ 524
Cdd:cd18568 109 -QKI-------RRFLTRSALtTILDLLMVFIYLGLMFyynlqltLIVLafiPLYVLLTLLSSPKLKRNSREIFQANAEQQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 525 lpllSHFAETVEGLTTIRA--------FRYEARFQQKLLEYTDSNNIASLFLTAANrwlevRMEYIGACVVLIAAATSIs 596
Cdd:cd18568 181 ----SFLVEALTGIATIKAlaaerpirWRWENKFAKALNTRFRGQKLSIVLQLISS-----LINHLGTIAVLWYGAYLV- 250
|
250
....*....|
gi 34784298 597 nsLHRELSAG 606
Cdd:cd18568 251 --ISGQLTIG 258
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
157-240 |
1.34e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 157 LSGGQRQRISVA---------RALYqhtnvvFLDDPFSAL---DVHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHA 224
Cdd:PRK00349 831 LSGGEAQRVKLAkelskrstgKTLY------ILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTA 899
|
90 100
....*....|....*....|..
gi 34784298 225 DWIIAM------KDGTIQREGT 240
Cdd:PRK00349 900 DWIIDLgpeggdGGGEIVATGT 921
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
152-228 |
1.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 152 ERGIN-LSGGQRQRISVARALYQHTNVV--FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 228
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
671-895 |
1.59e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.61 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 671 KIQIQNLSVRYDSSLKPVLK---HVNALIAPGQKIGICGRTGSGKSSF-------------SLAFFRMVDMFEGRIIIDG 734
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFiehlnalllpdtgTIEWIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 735 IDIAKLPLHT-----------LRSRLSIILQ--DPVLFSGTIR---------FNLDPEkkcsdstlwEALEIAQ--LKLV 790
Cdd:PRK13651 82 KVLEKLVIQKtrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEkdiifgpvsMGVSKE---------EAKKRAAkyIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 791 vkalpgGLD-AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVH 868
Cdd:PRK13651 153 ------GLDeSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
250 260
....*....|....*....|....*...
gi 34784298 869 TILS-ADLVMVLKRGAILEFDKPEKLLS 895
Cdd:PRK13651 227 NVLEwTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
672-888 |
1.67e-03 |
|
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: 40.70 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPlhtLRS 747
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEptsgRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 748 R-LSIILQDPVLFS-----GTIRFNLD----PEKKCSDSTLWEAlEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLF 817
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPKDEIDERVREVA-ELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34784298 818 CLARAFVRKTSIFIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILSADLVMVLKRGAILEFD 888
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
672-898 |
1.69e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.37 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMF--EGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSsgRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDP--VLFSGTIR-------FNLD-PEKKCSdstlwealeiaqlKLVVKALP-GGLDAIITEGGENFSQGQRQLFC 818
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKlPEDEVR-------------KRVDNALKrTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 819 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LSADLVMVLKRGAILEFDKPEKLLS 895
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFA 231
|
...
gi 34784298 896 QKD 898
Cdd:PRK13636 232 EKE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
807-884 |
1.73e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.93 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 807 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRG 882
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDG 216
|
..
gi 34784298 883 AI 884
Cdd:COG1129 217 RL 218
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
397-572 |
1.82e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 41.23 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 397 VLCSLGIALC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 475
Cdd:cd18548 46 LLLALLGLIAgILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 476 LCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQ-QLDDTTQLpllshFAETVEGLTTIRAF---RYE 547
Cdd:cd18548 126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKAIPLFKKVQkKLDRLNRV-----VRENLTGIRVIRAFnreDYE 200
|
170 180
....*....|....*....|....*.
gi 34784298 548 -ARFQQKLLEYTDsNNIASLFLTAAN 572
Cdd:cd18548 201 eERFDKANDDLTD-TSLKAGRLMALL 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
672-886 |
1.97e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.22 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSsfSLAffRMVDMFEGriiidgidiaklP-------- 741
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLI--RCINLLER------------Ptsgsvlvd 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 742 -----------LHTLRSRLSIILQDpvlfsgtirFNLDPEKkcsdsTLWE----ALEIAQ-------------LKLV--- 790
Cdd:COG1135 66 gvdltalsereLRAARRKIGMIFQH---------FNLLSSR-----TVAEnvalPLEIAGvpkaeirkrvaelLELVgls 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 791 --VKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENIL---QKVvmtafADR---TVV 861
Cdd:COG1135 132 dkADAYPSQL-----------SGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIV 195
|
250 260
....*....|....*....|....*.
gi 34784298 862 TIAHRVHTILS-ADLVMVLKRGAILE 886
Cdd:COG1135 196 LITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
158-221 |
2.33e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34784298 158 SGGQRQRISVARALYQHTNVVFLDDPFSALDVH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 221
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
144-263 |
2.51e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 144 HGDQ-TQIGERginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 221
Cdd:PRK10636 420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 34784298 222 PHADWIIAMKDGTIQR-EGTLKDFQRsecqlfehWKTLMNRQD 263
Cdd:PRK10636 492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
417-561 |
2.52e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 40.99 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 417 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCntidQHIPSTLE-CLS---RSTLL---CVSALTVISYVTP 489
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV----QEFKSSFKqCVSqglRSVTQtvgCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 490 VFLVALLPLAVVC-YFIQKYFRVASRDLQQLDDTTqlplLSHFAETVEGLTTIRAFRYEAR----FQQKLLEYTDSN 561
Cdd:cd18574 146 LLLLVIVPVVVLVgTLYGSFLRKLSRRAQAQVAKA----TGVADEALGNIRTVRAFAMEDRelelYEEEVEKAAKLN 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-235 |
2.87e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.17 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 17 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPsnpereTAADSDARSRGP 96
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD-------GEDI------TGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQKPW----LLNATVEENITFES----PFNK----QRYKMVIEACSLQPDIDILPHGDQTQIGergiNLSGGQRQR 164
Cdd:COG3845 335 VAYIPEDRLgrglVPDMSVAENLILGRyrrpPFSRggflDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34784298 165 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTI 235
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQR-LLE-LRDAGAAVLLISEDLDeILALSDRIAVMYEGRI 480
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-216 |
2.90e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 25 NITIRIPRGQLTMIVGQVGCGKSSlllaTlgeMQRVSGAvfwnssLPDSEGE--------DPSnperetaaDSDARSRgp 96
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKST----T---MKMLTGL------LPASEGEawlfgqpvDAG--------DIATRRR-- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 97 VAYASQkpwllnA-------TVEENIT-----FESPFNK--QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 162
Cdd:NF033858 341 VGYMSQ------AfslygelTVRQNLElharlFHLPAAEiaARVAEMLERFDLADVADALPD-----------SLPLGIR 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 34784298 163 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTH 216
Cdd:NF033858 404 QRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL-LIELSREDGVTIFISTH 456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-233 |
3.27e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 145 GDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 224
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458
|
....*....
gi 34784298 225 DWIIAMKDG 233
Cdd:PRK10982 459 DRILVMSNG 467
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
672-900 |
3.68e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 40.45 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV--DMFEGRIIIDGIDIAKLPLHTLRSRL 749
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkpTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 750 SIILQDP--VLFSGTIRFNLdpekkcsdstlweALEIAQLKL----VVKALPGGLDAIITEGGEN-----FSQGQRQLFC 818
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDV-------------AFGPLNLGLskeeVEKRVKEALKAVGMEGFENkpphhLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 819 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTI-LSADLVMVLKRGAILEFDKPEKLLSQ 896
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....
gi 34784298 897 KDSV 900
Cdd:PRK13639 228 IETI 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
672-713 |
3.68e-03 |
|
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: 40.82 E-value: 3.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 34784298 672 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKS 713
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKS 50
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
143-248 |
3.72e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 143 PHGDQtQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYL 221
Cdd:PRK10762 387 PSMEQ-AIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ--LINQFKAEGLSIILVSSEMpEVL 459
|
90 100
....*....|....*....|....*..
gi 34784298 222 PHADWIIAMKDGTIQREgtlkdFQRSE 248
Cdd:PRK10762 460 GMSDRILVMHEGRISGE-----FTREQ 481
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
694-849 |
4.18e-03 |
|
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: 39.59 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 694 ALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRI--------IIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIR 764
Cdd:cd03297 18 DFDLNEEVTGIFGASGAGKSTL----LRCIAGLEKPDggtivlngTVLFDSRKKINLPPQQRKIGLVFQQYALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 765 FNLD-PEKKCSDSTLW----EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASI 839
Cdd:cd03297 94 ENLAfGLKRKRNREDRisvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170
....*....|
gi 34784298 840 DMATENILQK 849
Cdd:cd03297 163 DRALRLQLLP 172
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
352-632 |
4.21e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 40.19 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 352 MVLVAIdyWLAKW-TDSALVLSPAARNCSLSQECALDqSVYAMVFTVLCSLGIALC-----LVTSVTVEWTGLKVAKRLH 425
Cdd:cd18564 14 LRLLEP--WPLKVvIDDVLGDKPLPGLLGLAPLLGPD-PLALLLLAAAALVGIALLrglasYAGTYLTALVGQRVVLDLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 426 RSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLeclsrsTLLCVSALTVISYVTPVF-------LVALLPL 498
Cdd:cd18564 91 RDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGV------LPLLTNLLTLVGMLGVMFwldwqlaLIALAVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 499 AVVCYFIQKY---FRVASRDLQQLDdttqlpllSHFAETV-EGLTTIR---AFRYEARFQQKLLEYTDSNNIASLFLTAA 571
Cdd:cd18564 165 PLLLLAARRFsrrIKEASREQRRRE--------GALASVAqESLSAIRvvqAFGREEHEERRFARENRKSLRAGLRAARL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 572 NRWLEVRMEYIGA---CVVLIAAATSIsnsLHRELSAGlvGLgltyaLMVSNYLNWM---VRNLADM 632
Cdd:cd18564 237 QALLSPVVDVLVAvgtALVLWFGAWLV---LAGRLTPG--DL-----LVFLAYLKNLykpVRDLAKL 293
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
672-718 |
4.69e-03 |
|
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: 39.43 E-value: 4.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLA 718
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKT 45
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
672-886 |
4.94e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.17 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 672 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLP---L 742
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLLERptsgRVLVDGQDLTALSekeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 743 HTLRSRLSIILQdpvlfsgtiRFNLdpekkCSDSTLWE----ALEIAQ-------------LKLVvkalpgGLDAIITEG 805
Cdd:PRK11153 78 RKARRQIGMIFQ---------HFNL-----LSSRTVFDnvalPLELAGtpkaeikarvtelLELV------GLSDKADRY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 806 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvvMTAFADR----TVVTIAHRVHTILS-ADLVMVL 879
Cdd:PRK11153 138 PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAtTRSILE---LLKDINRelglTIVLITHEMDVVKRiCDRVAVI 214
|
....*..
gi 34784298 880 KRGAILE 886
Cdd:PRK11153 215 DAGRLVE 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
780-882 |
5.10e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 780 EALEIAQLKLVVKALPGgldaiITeggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM-TAFADR 858
Cdd:PLN03140 1000 ELVELDNLKDAIVGLPG-----VT----GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGR 1070
|
90 100
....*....|....*....|....*.
gi 34784298 859 TVVTIAHR--VHTILSADLVMVLKRG 882
Cdd:PLN03140 1071 TVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
391-553 |
5.43e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 39.74 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 391 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFF---ETTPlGSILNRFSSDCNTI----DQHI 463
Cdd:cd18578 54 WALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddpENST-GALTSRLSTDASDVrglvGDRL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 464 PSTLECLSrstlLCVSALtVISYV-----TPVfLVALLPLAVVCYFIQKYF--RVASRDLQQLDDTTQLpllshFAETVE 536
Cdd:cd18578 133 GLILQAIV----TLVAGL-IIAFVygwklALV-GLATVPLLLLAGYLRMRLlsGFEEKNKKAYEESSKI-----ASEAVS 201
|
170
....*....|....*..
gi 34784298 537 GLTTIRAFRYEARFQQK 553
Cdd:cd18578 202 NIRTVASLTLEDYFLEK 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
390-560 |
5.67e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 39.88 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 390 VYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTI-----DQHIP 464
Cdd:cd18782 43 VIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIrgfltGTALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 465 STLECLsrSTLLCVSALTVISYVTPVFLVALLPLAVVCYF---------IQKYFRVASRdlqqlddtTQlpllSHFAETV 535
Cdd:cd18782 122 TLLDVL--FSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFlfgpilrrqIRRRAEASAK--------TQ----SYLVESL 187
|
170 180
....*....|....*....|....*.
gi 34784298 536 EGLTTIRAFRYEARFQQKLLE-YTDS 560
Cdd:cd18782 188 TGIQTVKAQNAELKARWRWQNrYARS 213
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
394-589 |
6.01e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 39.77 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 394 VFTVLCSLGIALCLVTSVT--VE-----WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPST 466
Cdd:cd18550 37 LLVLLALGMVAVAVASALLgvVQtylsaRIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 467 LECLSRSTLLCVSALTVISYVTP---VFLVALLPLAVV-CYFIQKYFRVASRDLQQLDDTtqlpLLSHFAET--VEGLTT 540
Cdd:cd18550 117 LTSVVSNVVTLVATLVAMLALDWrlaLLSLVLLPLFVLpTRRVGRRRRKLTREQQEKLAE----LNSIMQETlsVSGALL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34784298 541 IRAFRYEARFQQKLLEytDSNNIASLFLTAA--NRWLEVRMEYIGACVVLI 589
Cdd:cd18550 193 VKLFGREDDEAARFAR--RSRELRDLGVRQAlaGRWFFAALGLFTAIGPAL 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
152-218 |
6.45e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 6.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 152 ERGI-NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH--LSdhlMQAGILELLRDdkRTVVLVTHKL 218
Cdd:PRK13409 207 DRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrLN---VARLIRELAEG--KYVLVVEHDL 271
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
423-594 |
7.41e-03 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); 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: 350033 [Multi-domain] Cd Length: 289 Bit Score: 39.38 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 423 RLHRSLLNRIILAPMR----FFETTPLGSILNRFSSDCNTIDQHIPSTLECL----SRSTLLCVSALTVISYVTPVFLVA 494
Cdd:cd18589 66 RIHSRLQGLVFAAVLRqeiaFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLmwylARGLFLFIFMLWLSPKLALLTALG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 495 LLPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAFRYE----ARFQQKlLEYTDSNNIASLFLT 569
Cdd:cd18589 146 LPLLLLVPKFVGKFQQSLAVQVQKsLARANQVAV-----ETFSAMKTVRSFANEegeaQRYRQR-LQKTYRLNKKEAAAY 219
|
170 180 190
....*....|....*....|....*....|...
gi 34784298 570 AANRW--------LEVRMEYIGACVVLIAAATS 594
Cdd:cd18589 220 AVSMWtssfsglaLKVGILYYGGQLVTAGTVSS 252
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
808-885 |
8.08e-03 |
|
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: 38.85 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784298 808 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRGAI 884
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
.
gi 34784298 885 L 885
Cdd:cd03267 233 L 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
156-227 |
9.05e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 9.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34784298 156 NLSGGQRQRISVARALYQHTNVVFLDDPFSALD---VH-LSDHlmqagilelLRDDKRTVVLVTHKLQYLPH-ADWI 227
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDaesVAwLEQF---------LHDYPGTVVAVTHDRYFLDNvAGWI 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
672-716 |
9.12e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 9.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 34784298 672 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFS 716
Cdd:CHL00131 8 LEIKNLHASVNE--NEILKGLNLSINKGEIHAIMGPNGSGKSTLS 50
|
|
| |
