|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-787 |
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: 1660.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKNK 80
Cdd:TIGR00957 734 LEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNK 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 81 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLASEDD---SVSGSGKESKPVENGM 157
Cdd:TIGR00957 814 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSwtaLVSGEGKEAKLIENGM 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 158 LVTDTVGKHLQRHLSNSSSHSGDTSQQHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVYWNYMKAIGLFITFLSIFL 237
Cdd:TIGR00957 894 LVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFL 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 238 FLCNHVSALASNYWLSLWTDDPpVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSP 317
Cdd:TIGR00957 974 FVCNHVSALASNYWLSLWTDDP-MVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSP 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 318 MSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQL 397
Cdd:TIGR00957 1053 MSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQL 1132
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 398 KRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI 477
Cdd:TIGR00957 1133 KRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI 1212
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 478 SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCL 557
Cdd:TIGR00957 1213 SRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCL 1292
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 558 RYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLF 637
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLF 1372
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 SGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 717
Cdd:TIGR00957 1373 SGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 718 DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAKDAGL 787
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-786 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 693.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpMGLLKNK 80
Cdd:PLN03130 714 IDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGK 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 81 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLdRDGAFAEFLRTYANAEQDLASEDDSVSGSGKESKPVENGmlvt 160
Cdd:PLN03130 792 TRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS-NNGPLFQKLMENAGKMEEYVEENGEEEDDQTSSKPVANG---- 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 161 dtVGKHLQRhlsNSSShsgdtsqqhssiaelqKAGAKEETWKLMEADKAQTGQVQLSVYWNYMKAIGLFitFLSIFLFLC 240
Cdd:PLN03130 867 --NANNLKK---DSSS----------------KKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGA--WVVMILFLC 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 241 ---NHVSALASNYWLSLWTDDppvvNGTQANR-NFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRS 316
Cdd:PLN03130 924 yvlTEVFRVSSSTWLSEWTDQ----GTPKTHGpLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRA 999
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 317 PMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQ 396
Cdd:PLN03130 1000 PMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTARE 1079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 397 LKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAV 476
Cdd:PLN03130 1080 VKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAV 1159
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 477 I-----SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSTWPHSGRVE 551
Cdd:PLN03130 1160 MqngraENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIK 1239
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 552 FRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIP 631
Cdd:PLN03130 1240 FEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIP 1319
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 632 QDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 711
Cdd:PLN03130 1320 QAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 712 EATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQ-QRGIFYSMAKDAG 786
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-786 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 633.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMglLKNK 80
Cdd:PLN03232 714 IDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGK 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 81 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYA--NAEQDLASEDDSVSGSGkeskpvengml 158
Cdd:PLN03232 792 TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGkmDATQEVNTNDENILKLG----------- 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 159 vtdtvgkhlqrhlsnsSSHSGDTSQQhsSIAELQKAgaKEETWKLMEADKAQTGQVQLSVYWNYMKAIG-LFITFLSIFL 237
Cdd:PLN03232 861 ----------------PTVTIDVSER--NLGSTKQG--KRGRSVLVKQEERETGIISWNVLMRYNKAVGgLWVVMILLVC 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 238 FLCNHVSALASNYWLSLWTDDPPVVNGTQAnrnFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSP 317
Cdd:PLN03232 921 YLTTEVLRVSSSTWLSIWTDQSTPKSYSPG---FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAP 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 318 MSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQL 397
Cdd:PLN03232 998 MLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREV 1077
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 398 KRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI 477
Cdd:PLN03232 1078 RRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVL 1157
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 478 -----SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSTWPHSGRVEF 552
Cdd:PLN03232 1158 rngnaENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKF 1237
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 553 RDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQ 632
Cdd:PLN03232 1238 EDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ 1317
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 633 DPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 712
Cdd:PLN03232 1318 SPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 713 ATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRG-IFYSMAKDAG 786
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-786 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 586.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 4 CALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpMGLLKNKTRI 83
Cdd:PTZ00243 759 SQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRV 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 84 LVTHGISYLPQVDVIIVMSGGKISEMGSYqelldrdgafAEFLRTyaNAEQDLASED-DSVSGSGKESKPVENGMLVTDT 162
Cdd:PTZ00243 837 LATHQVHVVPRADYVVALGDGRVEFSGSS----------ADFMRT--SLYATLAAELkENKDSKEGDADAEVAEVDAAPG 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 163 VGKHlqrhlsnsssHSGDTSQQHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVYWNYMKAIG-LFITFLSIFLFLCN 241
Cdd:PTZ00243 905 GAVD----------HEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVT 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 242 HVSALASNYWLSLWTddppvvngtqaNRNFRLS------VYgaLGI-LQGAAIFGYSMAVSIGGI-FASRRLHLDLLYNV 313
Cdd:PTZ00243 975 ELVTVSSGVWLSMWS-----------TRSFKLSaatylyVY--LGIvLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSV 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 314 LRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVAS 393
Cdd:PTZ00243 1042 SRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 394 SRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAAL 473
Cdd:PTZ00243 1122 NREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIAL 1201
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 474 FAVI------SRHSLsaGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS-ETEKEAPWQ------------ 534
Cdd:PTZ00243 1202 IGVIgtmlraTSQEI--GLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDMPEldeevdalerrt 1279
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 535 -----------IQETAPPSTWPH---SGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRI 600
Cdd:PTZ00243 1280 gmaadvtgtvvIEPASPTSAAPHpvqAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM 1359
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 601 NESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHEC 680
Cdd:PTZ00243 1360 VEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRV 1439
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 681 AEGGENLSVGQRQLVCLARALLRK-TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDK 759
Cdd:PTZ00243 1440 LEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDH 1519
|
810 820
....*....|....*....|....*...
gi 1907116879 760 GEVRECGAPSELLQQR-GIFYSMAKDAG 786
Cdd:PTZ00243 1520 GAVAEMGSPRELVMNRqSIFHSMVEALG 1547
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
231-525 |
2.38e-178 |
|
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: 512.79 E-value: 2.38e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 231 TFLSIFLFLCNHVSALASNYWLSLWTDDPPV-VNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDL 309
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALnGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 310 LYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRF 389
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 390 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVL 469
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 470 FAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
548-768 |
1.19e-137 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 405.72 E-value: 1.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 548 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 627
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 707
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 708 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAP 768
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
232-783 |
8.42e-129 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 396.07 E-value: 8.42e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 232 FLSIFLFLCNHVSALASNYWLSLWTDDppVVNGTQANRNFRLS-VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLL 310
Cdd:COG1132 24 ILALLLLLLSALLELLLPLLLGRIIDA--LLAGGDLSALLLLLlLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 311 YNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFY 390
Cdd:COG1132 102 EHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 391 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 470
Cdd:COG1132 182 GRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 471 AALFAV--ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPstwPHSG 548
Cdd:COG1132 262 VLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLP---PVRG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 549 RVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGVNIAKIGLHNLRF 625
Cdd:COG1132 339 EIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVnllLRFYDPTS---GRILIDGVDIRDLTLESLRR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALL 702
Cdd:COG1132 415 QIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 703 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMA 782
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLY 572
|
.
gi 1907116879 783 K 783
Cdd:COG1132 573 R 573
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
232-525 |
1.70e-124 |
|
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: 374.63 E-value: 1.70e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 232 FLSIFLFLCNHVSALASNYWLSLWTDDPpvVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLY 311
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDP--VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 312 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIpPLGLVYFFVQRFYV 391
Cdd:cd18559 80 KALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI-PLGLLYVPVNRVYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 392 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFA 471
Cdd:cd18559 159 ASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 472 ALFAVISRHSLsAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18559 238 SFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
232-525 |
6.66e-122 |
|
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: 367.98 E-value: 6.66e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 232 FLSIFLFLCNHVSALASNYWLSLWTDDppVVNGTQANRNFRLSVYGALGILQGAA-IFGYSMAVSIGGIFASRRLHLDLL 310
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD--WSSSPNSSSGYYLGVYAALLVLASVLlVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 311 YNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFY 390
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 391 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 470
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 471 AALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18580 240 VALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-778 |
3.65e-116 |
|
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: 383.88 E-value: 3.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpMGLLKNK 80
Cdd:TIGR01271 522 IKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL--CKLMSNK 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 81 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLAS---------------EDDSVSG 145
Cdd:TIGR01271 600 TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAErrnsiltetlrrvsiDGDSTVF 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 146 SGKESK-------PVE------------------------------NGMLVTDTVGKHLQRHLS--------------NS 174
Cdd:TIGR01271 680 SGPETIkqsfkqpPPEfaekrkqsiilnpiasarkfsfvqmgpqkaQATTIEDAVREPSERKFSlvpedeqgeeslprGN 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 175 SSHSGDTSQ-----------QHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVY------------------------ 219
Cdd:TIGR01271 760 QYHHGLQHQaqrrqsvlqlmTHSNRGENRREQLQTSFRKKSSITQQNELASELDIYsrrlskdsvyeiseeineedlkec 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 220 -------------WN-YMKAIGLF--ITFLSIFLFLCNHVSALASNYWLSLWTDDPPVVN---GTQANRNFRLSVYGALg 280
Cdd:TIGR01271 840 faderenvfetttWNtYLRYITTNrnLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNyvdQQHANASSPDVQKPVI- 918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 281 ILQGAAIFGYSMAVSIG------GIF-----------ASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSM 343
Cdd:TIGR01271 919 ITPTSAYYIFYIYVGTAdsvlalGFFrglplvhtlltVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDM 998
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 344 IPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIR 423
Cdd:TIGR01271 999 LPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIR 1078
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 424 AFEEQ---ERFIHQSdlkVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQIT 498
Cdd:TIGR01271 1079 AFGRQsyfETLFHKA---LNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGIILTLAMNIL 1152
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 499 AYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP--PST------------WPHSGRVEFRDYCLRYREDLD 564
Cdd:TIGR01271 1153 STLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKyqLSTvlvienphaqkcWPSGGQMDVQGLTAKYTEAGR 1232
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 565 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMN 644
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 645 LDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 724
Cdd:TIGR01271 1312 LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 725 IQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIF 778
Cdd:TIGR01271 1392 IRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
232-525 |
1.99e-115 |
|
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: 351.01 E-value: 1.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 232 FLSIFLFLCNHVSALASNYWLSLWTDDPPvvngtQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLY 311
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDFF-----GLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 312 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYV 391
Cdd:cd18606 77 RVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 392 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFA 471
Cdd:cd18606 157 ASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 472 ALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18606 237 ALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
277-783 |
2.88e-102 |
|
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: 331.03 E-value: 2.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 277 GALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMFMGSL 355
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTALLDLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 356 FSVIGAVIIILLATPIAAV---IIPPLGLVYFFVQRFYVASSRQlkrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFI 432
Cdd:COG2274 282 FVLIFLIVLFFYSPPLALVvllLIPLYVLLGLLFQPRLRRLSRE----ESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 433 HQSDLKVDE----NQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVISRHsLSAG-LVGlSVSYSLQITAYLNWLVRM 507
Cdd:COG2274 358 RRWENLLAKylnaRFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVIDGQ-LTLGqLIA-FNILSGRFLAPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 508 SSEMETNIVAVERLKEYSETEKEAPWQIQETAPPstwPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTG 587
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP---RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 588 AGKSSLT---LGLFRINEsaeGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALE 661
Cdd:COG2274 512 SGKSTLLkllLGLYEPTS---GRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 662 LAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTI 741
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907116879 742 AHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAK 783
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
544-768 |
9.86e-100 |
|
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: 307.03 E-value: 9.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 544 WPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL 623
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 624 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELahlkgfvsalpdklnhecAEGGENLSVGQRQLVCLARALLR 703
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 704 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAP 768
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
232-525 |
4.08e-97 |
|
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: 303.62 E-value: 4.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 232 FLSIFLFLCNHVSALASNYWLSLWT---DDPPVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLD 308
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWAsayETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 309 LLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQR 388
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 389 FYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIV 468
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 469 LFAALFAViSRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18604 242 FATAALLV-YGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
231-525 |
3.92e-92 |
|
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: 291.04 E-value: 3.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 231 TFLSIFLFLCNHVSALASNYWLSLWTD------DPPVVNGTQANRN----FRLSVYGALGILQGAAIFGYSMAVSIGGIF 300
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEanhdvaSVVFNITSSSLEDdevsYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 301 ASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLG 380
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 381 LVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRL 460
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 461 ECVGNCIVLFAALFAVISRH--SLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18602 241 DYLGAVIVFLAALSSLTAALagYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
229-524 |
1.40e-89 |
|
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: 284.04 E-value: 1.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 229 FITFLsIFLFLCnHVSALASNYWLSLWTDD--PPVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLH 306
Cdd:cd18605 1 LILIL-LSLILM-QASRNLIDFWLSYWVSHsnNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 307 LDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFV 386
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 387 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 466
Cdd:cd18605 159 QRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 467 IVLFAALFAVISRH---SLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEY 524
Cdd:cd18605 239 IVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
548-783 |
4.20e-86 |
|
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: 273.32 E-value: 4.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 548 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 627
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 707
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 708 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELL-QQRGIFYSMAK 783
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVR 254
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
278-776 |
1.09e-77 |
|
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: 261.23 E-value: 1.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 278 ALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFskeLDTVDSM-------IPQVIKM 350
Cdd:COG4988 66 AVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEALdgyfaryLPQLFLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 351 FMGSLfsVIGAVI--------IILLATpiaAVIIPplgLVYFFVQRFY-VASSRQLKRLESVSrspvySHFNETLLGVSV 421
Cdd:COG4988 143 ALVPL--LILVAVfpldwlsgLILLVT---APLIP---LFMILVGKGAaKASRRQWRALARLS-----GHFLDRLRGLTT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 422 IRAF----EEQERFIHQSD---------LKVdenqkAYYPSIVanrwlavrLECVGnciVLFAALFAVISRHSLSAGLVG 488
Cdd:COG4988 210 LKLFgrakAEAERIAEASEdfrkrtmkvLRV-----AFLSSAV--------LEFFA---SLSIALVAVYIGFRLLGGSLT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 489 LSVSYSLQITA---YL-------NWLVRMSsemetNIVAVERLKEYSETEKEAPWQIQETAPpstWPHSGRVEFRDYCLR 558
Cdd:COG4988 274 LFAALFVLLLApefFLplrdlgsFYHARAN-----GIAAAEKIFALLDAPEPAAPAGTAPLP---AAGPPSIELEDVSFS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 559 YrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFS 638
Cdd:COG4988 346 Y-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 GSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 715
Cdd:COG4988 425 GTIRENLrlgRP--DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 716 AVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRG 776
Cdd:COG4988 503 HLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
227-525 |
1.91e-76 |
|
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: 249.79 E-value: 1.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 227 GLFITFLSIFLFLCNHVSALASNYWLSLWTDDPpvvNGTQANR-----------------NFRLSVYG--ALGILQGAAI 287
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQG---SGNTTNNvdnstvdsgnisdnpdlNFYQLVYGgsILVILLLSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 288 --FGYSMAVsiggIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIII 365
Cdd:cd18599 78 rgFVFVKVT----LRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 366 LLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKA 445
Cdd:cd18599 154 AIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 446 YYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18599 234 FFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
548-776 |
9.30e-75 |
|
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: 242.13 E-value: 9.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 548 GRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 627
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWM-ALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 706
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 707 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRG 776
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
279-781 |
1.20e-71 |
|
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: 245.01 E-value: 1.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 279 LGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSV 358
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 359 IGAVIIILLA----TPIAAVIIPPLGLVyffvqrfyvaSSRQLKRLESVSRSPVYSH------FNETLLGVSVIRAF--- 425
Cdd:TIGR02203 143 IGLFIVLLYYswqlTLIVVVMLPVLSIL----------MRRVSKRLRRISKEIQNSMgqvttvAEETLQGYRVVKLFggq 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 426 -EEQERFIHQSD------LKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFAVISRHSLSAGLVGLSVSySLQ 496
Cdd:TIGR02203 213 aYETRRFDAVSNrnrrlaMKMTSAGSISSPITqlIASLALAV---------VLFIALFQAQAGSLTAGDFTAFITA-MIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 497 ITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEApwQIQETAPPSTwphSGRVEFRDYCLRYREDLDLVLKHINVTIEG 576
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK--DTGTRAIERA---RGDVEFRNVTFRYPGRDRPALDSISLVIEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 577 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfSQYSD 653
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADR 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 654 EEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF 733
Cdd:TIGR02203 437 AEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 734 EDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIF---YSM 781
Cdd:TIGR02203 517 QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYaqlHNM 567
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
326-783 |
3.89e-71 |
|
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: 243.52 E-value: 3.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 326 SGNLVNRFSKELDTVDSMIPQVIkmfmgslFSVIGAVIIILLATPIAAVIIPPLGLVYF------------FVQRFYVAS 393
Cdd:COG4987 111 SGDLLNRLVADVDALDNLYLRVL-------LPLLVALLVILAAVAFLAFFSPALALVLAlglllaglllplLAARLGRRA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 394 SRQLKRLesvsRSPVYSHFNETLLGVSVIRAFEEQERFIHQsdlkVDENQKAYypsiVANRWLAVRLECVGNCIVLFAAL 473
Cdd:COG4987 184 GRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALAR----LDAAEARL----AAAQRRLARLSALAQALLQLAAG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 474 FAVI----------SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqIQETAPPST 543
Cdd:COG4987 252 LAVVavlwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPA----VTEPAEPAP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 544 WPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL 623
Cdd:COG4987 328 APGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 624 RFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARA 700
Cdd:COG4987 408 RRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARA 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 701 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYS 780
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
...
gi 1907116879 781 MAK 783
Cdd:COG4987 566 LYQ 568
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
227-525 |
2.08e-67 |
|
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: 225.66 E-value: 2.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 227 GLFITFLSIFLFLCNHVSALASNYWLSLW----------TDDPPVVNGTQA-----NRNFRLSVYGalGILQGAAIFGYS 291
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndtTDRVQGENSTNVdiedlDRDFNLGIYA--GLTAATFVFGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 292 MAVSI--GGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLAT 369
Cdd:cd18601 79 RSLLFfhVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 370 PIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS 449
Cdd:cd18601 159 PWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 450 IVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 525
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
303-781 |
3.62e-65 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 228.06 E-value: 3.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 303 RRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLfSVIGAVIIILLATP-----IAAVIIP 377
Cdd:PRK10790 98 QQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA-ALIGAMLVAMFSLDwrmalVAIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 378 PLGLVYFFVQRFyvaSSRQLKRLESVsRSPVYSHFNETLLGVSVIRAFEEQERFihqsDLKVDENQKAYYPSivanRWLA 457
Cdd:PRK10790 177 AVLVVMVIYQRY---STPIVRRVRAY-LADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSHYMA----RMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 458 VRLE--CVGNCIVLFAALF--AVISRHSLSA-GLVGLSVSYslqitAYLNWLVRMS----------SEMETNIVAVERLK 522
Cdd:PRK10790 245 LRLDgfLLRPLLSLFSALIlcGLLMLFGFSAsGTIEVGVLY-----AFISYLGRLNeplielttqqSMLQQAVVAGERVF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 523 EYSETEKeapwqiQETAPPSTWPHSGRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE 602
Cdd:PRK10790 320 ELMDGPR------QQYGNDDRPLQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 603 SAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAE 682
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 683 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 762
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
490
....*....|....*....
gi 1907116879 763 RECGAPSELLQQRGIFYSM 781
Cdd:PRK10790 553 VEQGTHQQLLAAQGRYWQM 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
550-781 |
2.30e-64 |
|
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: 214.79 E-value: 2.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 704
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 705 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
550-781 |
4.58e-63 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 211.32 E-value: 4.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 704
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 705 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-105 |
2.21e-62 |
|
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: 208.09 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMgLLKNK 80
Cdd:cd03250 101 IKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGL-LLNNK 179
|
90 100
....*....|....*....|....*
gi 1907116879 81 TRILVTHGISYLPQVDVIIVMSGGK 105
Cdd:cd03250 180 TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
550-761 |
2.31e-62 |
|
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: 206.85 E-value: 2.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILV 709
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 710 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 761
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
297-781 |
2.70e-62 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 222.68 E-value: 2.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 297 GGIF------ASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP 370
Cdd:TIGR00958 222 GGSFnytmarINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 371 IAAVI----IPPLGLVYFFVQRFYVASSRQLKrlESVSRSPVYSHfnETLLGVSVIRAF--EEQE--RFIHQSDLKVDEN 442
Cdd:TIGR00958 302 RLTMVtlinLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGEasRFKEALEETLQLN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 443 QK---AYYPSIVANRWLAVRLECvgncIVLFAALFAVISRHSLSAGLVGLsVSYSLQITAYLNWLVRMSSEMETNIVAVE 519
Cdd:TIGR00958 378 KRkalAYAGYLWTTSVLGMLIQV----LVLYYGGQLVLTGKVSSGNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 520 RLKEYSETEKEAPwQIQETAPPstwPHSGRVEFRDYCLRY--REDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGL 597
Cdd:TIGR00958 453 KVFEYLDRKPNIP-LTGTLAPL---NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 598 FRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWMALELAHLKGFVSALPDKL 676
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 677 NHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYTRVIV 756
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILV 685
|
490 500
....*....|....*....|....*
gi 1907116879 757 LDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
550-783 |
1.64e-60 |
|
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: 204.31 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRY--REDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 627
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALL 702
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 703 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMA 782
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 1907116879 783 K 783
Cdd:cd03249 236 K 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
477-781 |
3.49e-60 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 214.30 E-value: 3.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 477 ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqIQET--APPSTwPHSGRVEFRD 554
Cdd:COG5265 288 VVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE----VADApdAPPLV-VGGGEVRFEN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 555 YCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDP 634
Cdd:COG5265 363 VSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 635 VLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILV 709
Cdd:COG5265 442 VLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 710 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
548-778 |
1.41e-57 |
|
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: 197.77 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 548 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGVNIAKIGLHNLRFKI 627
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 707
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 708 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIF 778
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
317-778 |
1.68e-55 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 201.02 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 317 PMSFFERTPSGNLVNRFskeldTVDSmiPQVIKMFMGSLFSVI--GAVIIILLA----------------TPIAAVIIpp 378
Cdd:PRK11176 112 PVSFFDKQSTGTLLSRI-----TYDS--EQVASSSSGALITVVreGASIIGLFImmfyyswqlsliliviAPIVSIAI-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 379 lGLVyffVQRFyvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERF------IHQSDLKVDENQKAYYP 448
Cdd:PRK11176 183 -RVV---SKRF-----RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFggqeVETKRFdkvsnrMRQQGMKMVSASSISDP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 449 SI--VANRWLAVrlecvgnciVLFAALFAVIsRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEY-- 524
Cdd:PRK11176 254 IIqlIASLALAF---------VLYAASFPSV-MDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAIld 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 525 SETEKEAPWQIQETAppstwphSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESA 604
Cdd:PRK11176 324 LEQEKDEGKRVIERA-------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 605 EGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFS--QYSDEEVWMALELAHLKGFVSALPDKLNHECAE 682
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 683 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 762
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
490
....*....|....*.
gi 1907116879 763 RECGAPSELLQQRGIF 778
Cdd:PRK11176 557 VERGTHAELLAQNGVY 572
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
550-781 |
1.23e-53 |
|
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: 185.77 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 706
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 707 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
548-762 |
2.11e-51 |
|
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: 178.94 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 548 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIGLHNLR 624
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLkllAGLYK---PTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 625 FKITIIPQDPVLFSGSLRMNLDPFSQY-SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLR 703
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 704 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 762
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
232-501 |
3.07e-51 |
|
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: 180.15 E-value: 3.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 232 FLSIFLFLCNHVSALASNYWLSLWTDDPPVVNGTQANR-NFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLL 310
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAlNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 311 YNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFY 390
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 391 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 470
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1907116879 471 AALFAV--ISRHSLSAGLVGLSVSYSLQITAYL 501
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-781 |
3.84e-49 |
|
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: 184.94 E-value: 3.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 277 GALGILQGAAIFGY------SMAVSIGGIFASRRLHLDLLYN----VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQ 346
Cdd:TIGR01193 193 GTLGIISIGLIIAYiiqqilSYIQIFLLNVLGQRLSIDIILSyikhLFELPMSFFSTRRTGEIVSRFTDASSIIDALAST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 347 VIKMFMG-SLFSVIGAVI---------IILLATPIAAVIIpplglvYFFVQRFYVASSRQLKrlesvSRSPVYSHFNETL 416
Cdd:TIGR01193 273 ILSLFLDmWILVIVGLFLvrqnmllflLSLLSIPVYAVII------ILFKRTFNKLNHDAMQ-----ANAVLNSSIIEDL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 417 LGVSVIRAF-EEQERFIHQSDLKVDENQKA--YYPSIVANRWLAVRLECVGNCIVLFAALFAVIsRHSLSAGLVglsVSY 493
Cdd:TIGR01193 342 NGIETIKSLtSEAERYSKIDSEFGDYLNKSfkYQKADQGQQAIKAVTKLILNVVILWTGAYLVM-RGKLTLGQL---ITF 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 494 SLQITAYLNWL---VRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAppSTWPHsGRVEFRDYCLRYREDlDLVLKHI 570
Cdd:TIGR01193 418 NALLSYFLTPLeniINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTE--LNNLN-GDIVINDVSYSYGYG-SNILSDI 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 571 NVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQ 650
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 651 --YSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 728
Cdd:TIGR01193 574 enVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNN 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 729 IrTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:TIGR01193 654 L-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
314-783 |
3.94e-49 |
|
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: 184.77 E-value: 3.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 314 LRSPMSFFERTPSGNLVNRfskeLDTVDSMIPQ----VIKMFMGSLFSVIGAVII-------ILLATPIAAVIIpplgLV 382
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR----AMGISQIRRIlsgsTLTTLLSGIFALLNLGLMfyyswklALVAVALALVAI----AV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 383 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLec 462
Cdd:TIGR03797 292 TLVLGLLQVRKERRLLELSGKISGLTVQLIN----GISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFN-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 463 VGNCIVLFAALFAVISRHSLSAGL-VGLSVSYSLQITAYLNWLVRMSSEMeTNIVAV----ERLKEYSETEKEAPwqiQE 537
Cdd:TIGR03797 366 AVLPVLTSAALFAAAISLLGGAGLsLGSFLAFNTAFGSFSGAVTQLSNTL-ISILAViplwERAKPILEALPEVD---EA 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 538 TAPPStwPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGlFRINESaeGEIIIDGVN 614
Cdd:TIGR03797 442 KTDPG--KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLlrlLLG-FETPES--GSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 615 IAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQL 694
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 695 VCLARALLRKTKILVLDEATAAVDLETDNLI-QSTIRTQfedCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQ 773
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVsESLERLK---VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|
gi 1907116879 774 QRGIFYSMAK 783
Cdd:TIGR03797 674 REGLFAQLAR 683
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
313-788 |
3.02e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 180.16 E-value: 3.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 313 VLRSPMSFFERTPSGNLVNRFskeLDTVDSMIpQVIKMFMGSLFSVIGAVIIILlatPIA-------AVIIPPLGLVYFF 385
Cdd:PRK13657 99 IIQLPLAWHSQRGSGRALHTL---LRGTDALF-GLWLEFMREHLATLVALVVLL---PLAlfmnwrlSLVLVVLGIVYTL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 386 VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF---EEQERFIHQSdlkVDENQKAYYPsiVANRW-LAVRLE 461
Cdd:PRK13657 172 ITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnriEAETQALRDI---ADNLLAAQMP--VLSWWaLASVLN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 462 CVGNCIVLFAALF---AVISRHSLSAGLVGLSVSYSlqiTAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQEt 538
Cdd:PRK13657 247 RAASTITMLAILVlgaALVQKGQLRVGEVVAFVGFA---TLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVP-DVRD- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 539 aPPSTWPH---SGRVEFRDYCLRY---REDLDlvlkHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG 612
Cdd:PRK13657 322 -PPGAIDLgrvKGAVEFDDVSFSYdnsRQGVE----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 613 VNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENL 687
Cdd:PRK13657 397 TDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 688 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGA 767
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
490 500
....*....|....*....|.
gi 1907116879 768 PSELLQQRGIFYSMAKDAGLV 788
Cdd:PRK13657 553 FDELVARGGRFAALLRAQGML 573
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
277-757 |
1.71e-44 |
|
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: 168.23 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 277 GALGILQGAAIFGYSMAVSiggifasRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDS----MIPQVIKMFM 352
Cdd:TIGR02857 58 ALLGWLQERAAARAAAAVK-------SQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGyfarYLPQLVLAVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 353 GSLfsVIGAVIiiLLATPIAAVII---PPLgLVYFFVQRFYVASSRQLKRLESVSRspVYSHFNETLLGVSVIRAF---- 425
Cdd:TIGR02857 131 VPL--AILAAV--FPQDWISGLILlltAPL-IPIFMILIGWAAQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFgrak 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 426 EEQERFIHQSD---------LKVdenqkAYYPSIVanrwlavrLEcvgncivLFA----ALFAVISRHSLSAGLVGLSVS 492
Cdd:TIGR02857 204 AQAAAIRRSSEeyrertmrvLRI-----AFLSSAV--------LE-------LFAtlsvALVAVYIGFRLLAGDLDLATG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 493 YSLQITA---YLNwLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPpSTWPHSGRVEFRDYCLRYrEDLDLVLKH 569
Cdd:TIGR02857 264 LFVLLLApefYLP-LRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAP-VTAAPASSLEFSGVSVAY-PGRRPALRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---D 646
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 647 PFSqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 726
Cdd:TIGR02857 421 PDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
490 500 510
....*....|....*....|....*....|.
gi 1907116879 727 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVL 757
Cdd:TIGR02857 499 EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
233-745 |
3.16e-44 |
|
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: 167.54 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 233 LSIFLFLCNHVSALA----SNYWLSLWTDDPPVVNGTQANRNFRlsvygALGILQGAA-----IFGYSMAVSIGGifasr 303
Cdd:TIGR02868 17 LAVLLGALALGSAVAllgvSAWLISRAAEMPPVLYLSVAAVAVR-----AFGIGRAVFrylerLVGHDAALRSLG----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 304 RLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIkmfmgslFSVIGAVIIILLATPIAAVIIPPLGLV- 382
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI-------VPAGVALVVGAAAVAAIAVLSVPAALIl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 383 -------YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRW 455
Cdd:TIGR02868 160 aaglllaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 456 LAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPW 533
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGpaVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 534 QIQETAPPSTwPHSGRVEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV 613
Cdd:TIGR02868 320 GSAPAAGAVG-LGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 614 NIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVG 690
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 691 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 745
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
548-762 |
5.19e-44 |
|
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: 158.40 E-value: 5.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 548 GRVEFRDYCLRYREDLD-LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFK 626
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 627 ITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKT 705
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 706 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 762
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
570-781 |
2.66e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 165.79 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLT---LGLFrineSAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL- 645
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLnalLGFL----PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 --DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 723
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 724 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
515-781 |
5.68e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.83 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 515 IVAVERLKEYSETEKEAPWQIQETAPPStwphSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT 594
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAAD----QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 595 LGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSA 671
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 672 lPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI--M 749
Cdd:PRK11160 462 -DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqF 540
|
250 260 270
....*....|....*....|....*....|..
gi 1907116879 750 DytRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:PRK11160 541 D--RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
550-775 |
5.48e-38 |
|
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: 141.32 E-value: 5.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINEsaeGEIIIDGVNIAKIGLHNLRFK 626
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRllnGLLKPTS---GEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 627 ITIIPQDPV--LFSGSLR-------MNLdpfsQYSDEE----VWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQ 693
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEedvafgpENL----GLPREEirerVEEALELVGLEHL-------ADRPPHE----LSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 694 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 771
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREV 221
|
....
gi 1907116879 772 LQQR 775
Cdd:COG1122 222 FSDY 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-785 |
4.17e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 144.40 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDaHVGKHIFEKVVGPMGLLKNKTRILVTHGISYL 92
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 93 PQVDVIIVMS-----------------------------------------------GGKISEMGSYQELL-DRDGAFAE 124
Cdd:PTZ00265 644 RYANTIFVLSnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnaGSYIIEQGTHDALMkNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 125 FLRTyanaeQDLASEDDSVSGSGKES-------KPVENGMLVTDTVGKHLQRHLSNSSSHSGDTSQQHSSIAElqkAGAK 197
Cdd:PTZ00265 724 MINN-----QKVSSKKSSNNDNDKDSdmkssayKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASENN---AGGK 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 198 EETWKLMEADKAQTGQVQLSVY---WNYMKAIGlfITFLSIFLF--LCNHVSALASNYWLSLWTddppvVNGTQANRNfR 272
Cdd:PTZ00265 796 LPFLRNLFKRKPKAPNNLRIVYreiFSYKKDVT--IIALSILVAggLYPVFALLYAKYVSTLFD-----FANLEANSN-K 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 273 LSVYG---ALGILQGAAIFGYSMAVSigGIFASRRLHLDLLYNVLRSPMSFFER---TPsGNLVNRFSKELDTVDSMIPQ 346
Cdd:PTZ00265 868 YSLYIlviAIAMFISETLKNYYNNVI--GEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVN 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 347 VIKMFMGSLFSVIGAVIIILLATPIAAVIippLGLVYFFVQRFYVASSR-------QLKRLESVSRSPVYSH-------- 411
Cdd:PTZ00265 945 NIVIFTHFIVLFLVSMVMSFYFCPIVAAV---LTGTYFIFMRVFAIRARltankdvEKKEINQPGTVFAYNSddeifkdp 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 412 ---FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFA--VISRHSLSAGL 486
Cdd:PTZ00265 1022 sflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGsfLIRRGTILVDD 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 487 VGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLkeYSETEKEAPWQIQETAP---PSTWPHSGRVEFRDYCLRYREDL 563
Cdd:PTZ00265 1102 FMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKY--YPLIIRKSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRYISRP 1179
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 564 DL-VLKHINVTIEGGEKVGIVGRTGAGKSSL--------------------------------------TLGLFRINESA 604
Cdd:PTZ00265 1180 NVpIYKDLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivfknehtndmtneqdyqgdeeqNVGMKNVNEFS 1259
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 605 ----------------EGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDpFSQ--YSDEEVWMALELAHLK 666
Cdd:PTZ00265 1260 ltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFAAID 1338
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 667 GFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHR 744
Cdd:PTZ00265 1339 EFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHR 1418
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1907116879 745 LNTIMDYTRVIVLDKGE-----VRECGAPSELLQ-QRGIFYSMAKDA 785
Cdd:PTZ00265 1419 IASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQDGVYKKYVKLA 1465
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
550-766 |
3.34e-33 |
|
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: 125.89 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGVNIAKIGlHNLRFKIT 628
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTGDLKPqQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 629 IIPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKIL 708
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 709 VLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECG 766
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
551-761 |
5.39e-33 |
|
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: 126.43 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 551 EFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITII 630
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 631 PQDP------------VLFsgSLRmNLdpfsQYSDEEVWMALELAhLKGFvsALPDKLNHECAEggenLSVGQRQLVCLA 698
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 699 RALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGE 761
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
551-762 |
8.24e-33 |
|
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: 124.64 E-value: 8.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 551 EFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIGLHNLRFKI 627
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArliLGLLR---PTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKI 707
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 708 LVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 762
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1-104 |
1.13e-32 |
|
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: 125.91 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvGPMGLLKN- 79
Cdd:cd03290 114 TDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQE--GILKFLQDd 191
|
90 100
....*....|....*....|....*.
gi 1907116879 80 -KTRILVTHGISYLPQVDVIIVMSGG 104
Cdd:cd03290 192 kRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
566-766 |
1.02e-31 |
|
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: 123.38 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvlfSGSL- 641
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP---MSSLn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 642 -RMN-----LDPF------SQYSDEEVWMALELAHLkGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 709
Cdd:cd03257 97 pRMTigeqiAEPLrihgklSKKEARKEAVLLLLVGV-GLPEEVLNRYPHE-------LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 710 LDEATAAVDLETD----NLIQsTIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECG 766
Cdd:cd03257 169 ADEPTSALDVSVQaqilDLLK-KLQEEL-GLTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
551-761 |
2.40e-31 |
|
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: 120.04 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 551 EFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITII 630
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 631 PQdpvlfsgslrmnldpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVL 710
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 711 DEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGE 761
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
549-772 |
4.56e-31 |
|
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: 122.46 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 549 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKIT 628
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 629 IIPQDPVL-FSGSLR----M----NLDPFSQYSDEE---VWMALELAHLkgfvSALPDKLNHEcaeggenLSVGQRQLVC 696
Cdd:COG1120 79 YVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGL----EHLADRPVDE-------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 697 LARALLRKTKILVLDEATAAVDL----ETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSEL 771
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
.
gi 1907116879 772 L 772
Cdd:COG1120 226 L 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-133 |
6.08e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 128.74 E-value: 6.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYL 92
Cdd:COG1132 462 LPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTI 538
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAE 133
Cdd:COG1132 539 RNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
550-774 |
1.99e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.17 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGVNIAKIGLHNLRFK 626
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 627 ITIIPQDP------------VLFsgSLRMNLDPFSQySDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQL 694
Cdd:COG1123 85 IGMVFQDPmtqlnpvtvgdqIAE--ALENLGLSRAE-ARARVLELLEAVGLERRLDRYP----HQ-------LSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 695 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 771
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEI 230
|
...
gi 1907116879 772 LQQ 774
Cdd:COG1123 231 LAA 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
567-715 |
2.86e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 116.59 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGS-----L 641
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 642 RMNLDPFSQYSDE-EVWMALELAHLKgfvsaLPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 715
Cdd:pfam00005 81 RLGLLLKGLSKREkDARAEEALEKLG-----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-127 |
3.89e-30 |
|
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: 127.26 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEAC---ALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLL 77
Cdd:COG2274 582 IEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLL 658
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907116879 78 KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLR 127
Cdd:COG2274 659 KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
550-781 |
1.00e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.82 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYClrYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 706
Cdd:PRK10789 394 VSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 707 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-124 |
6.53e-29 |
|
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: 115.79 E-value: 6.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYL 92
Cdd:cd03253 123 FPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTI 199
|
90 100 110
....*....|....*....|....*....|..
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 124
Cdd:cd03253 200 VNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
220-521 |
8.79e-29 |
|
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: 117.60 E-value: 8.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 220 WN-YMKAIG-----LFITFLSIFLFLcnhVSALASNYWLSLWTDDPPVVNGTQANrnfrlSVYGALGILQGAAIFGYSMA 293
Cdd:cd18600 3 WNtYLRYITshkslIFVLILCLVIFA---IEVAASLVGLWLLRSQADRVNTTRPE-----SSSNTYAVIVTFTSSYYVFY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 294 VSIG--------GIF-----------ASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 354
Cdd:cd18600 75 IYVGvadsllamGFFrglplvhtlitVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 355 LFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERF--- 431
Cdd:cd18600 155 FLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFetl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 432 IHQSdlkVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSS 509
Cdd:cd18600 235 FHKA---LNLHTANWFLYLSTLRWFQMRIEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSI 308
|
330
....*....|..
gi 1907116879 510 EMETNIVAVERL 521
Cdd:cd18600 309 DVDSLMRSVSRI 320
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
566-774 |
1.47e-28 |
|
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: 120.78 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvlfSGSL- 641
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDP---YSSLn 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 642 -RMN--------LDPFSQYSDEEVW-MALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLD 711
Cdd:COG1123 357 pRMTvgdiiaepLRLHGLLSRAERReRVAELLERVGLPPDLADRYPHE-------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 712 EATAAVDLetdnLIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG1123 430 EPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIAdRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
550-761 |
1.76e-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: 113.33 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRY---REDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLfrINESA--EGEIIIDGvniakiglhnlr 624
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEklSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 625 fKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 704
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 705 TKILVLDEATAAVDLETDNLIqstirtqFEDC---------TVLTIAHRLNTIMDYTRVIVLDKGE 761
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
518-760 |
6.77e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.14 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 518 VERLKEYSETEKEAPwQIQETAPPSTWPHSGRVEFRDYCLRyREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtlgl 597
Cdd:COG4178 332 VDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 598 FR----INESAEGEIII-DGVNIAkiglhnlrfkitIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWMALELAHLkgfv 669
Cdd:COG4178 406 LRaiagLWPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL---- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 670 SALPDKLnHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRlNTIM 749
Cdd:COG4178 470 GHLAERL-DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLA 547
|
250
....*....|..
gi 1907116879 750 DY-TRVIVLDKG 760
Cdd:COG4178 548 AFhDRVLELTGD 559
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
550-771 |
7.41e-28 |
|
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: 112.27 E-value: 7.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDGVNIAKIGLH--N 622
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 623 LRFKITIIPQDPVLFSGSLRMNLDpfsqYS------------DEEVWMALELAHLKGFVSalpDKLNhecaegGENLSVG 690
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVK---DRLH------ALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 691 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYTrvIVLDKGEVRECGA 767
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRT--AFLLNGRLVEFGP 223
|
....
gi 1907116879 768 PSEL 771
Cdd:cd03260 224 TEQI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
550-774 |
2.05e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.72 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGVNIAK----IG--- 619
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLlkaILGLLPP---TSGTVRLFGKPPRRarrrIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 620 ---LHNLRFKITIipQDPVLfsgslrMNLDP----FSQYSDEE---VWMALELAHLKGF----VSALpdklnhecaegge 685
Cdd:COG1121 82 qraEVDWDFPITV--RDVVL------MGRYGrrglFRRPSRADreaVDEALERVGLEDLadrpIGEL------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 686 nlSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVR 763
Cdd:COG1121 141 --SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRGLVA 218
|
250
....*....|.
gi 1907116879 764 eCGAPSELLQQ 774
Cdd:COG1121 219 -HGPPEEVLTP 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
566-773 |
8.47e-27 |
|
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: 109.89 E-value: 8.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPvlfSGSL--RM 643
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP---YASLhpRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLD-----PFS----QYSDEEVWMALELAHLKgfvSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 714
Cdd:COG1124 97 TVDrilaePLRihglPDREERIAELLEQVGLP---PSFLDRYPHQ-------LSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 715 AAVDL----ETDNLIQStIRTQfEDCTVLTIAHRLNTImDY--TRVIVLDKGEVRECGAPSELLQ 773
Cdd:COG1124 167 SALDVsvqaEILNLLKD-LREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIVEELTVADLLA 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
566-774 |
1.07e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 115.14 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 645
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPFSQYSD-EEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN- 723
Cdd:TIGR01842 413 ARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQa 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 724 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQ 774
Cdd:TIGR01842 493 LANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
566-776 |
1.50e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 109.18 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRfKITIIPQDPVLFSG-SLRMN 644
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 645 LD---PFSQYSDEEVWMALE-LAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 720
Cdd:COG4555 95 IRyfaELYGLFDEELKKRIEeLIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 721 TDNLIQSTIRTQF-EDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQRG 776
Cdd:COG4555 167 ARRLLREILRALKkEGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
566-774 |
1.56e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 114.85 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRineSAEGEIIIDGVNIA-----KIGLHnlrfkITIIPQDPVLF 637
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLarlLVGVWP---PTAGSVRLDGADLSqwdreELGRH-----IGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 SGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 717
Cdd:COG4618 419 DGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 718 DLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG4618 499 DDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
543-761 |
1.74e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 116.67 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 543 TWPHSGRVEFRDYCLRY--REDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGVNIAKIG 619
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 620 LHNLRFKITIIPQDPVLFSGSLRMNL-------------------DPFSQYSDEEVWMAL------------------EL 662
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQENKNKRNSCrakcagdlndmsnttdsnEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 663 AHLK---------------------GFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 721
Cdd:PTZ00265 535 IEMRknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907116879 722 DNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 761
Cdd:PTZ00265 615 EYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
566-766 |
2.03e-26 |
|
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: 106.75 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQdpvlfsgSLRmnl 645
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------ALE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 dpfsqysdeevwmALELAHLKgfvsalpDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL----ET 721
Cdd:cd03214 84 -------------LLGLAHLA-------DRPFNE-------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907116879 722 DNLIQSTIRTqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECG 766
Cdd:cd03214 137 LELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
550-773 |
2.36e-26 |
|
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: 108.36 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAK---IGLHNL 623
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLrliVGLLR---PDSGEVLIDGEDISGlseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 624 RFKITIIPQDPVLFSG-SLRMN----LDPFSQYSDEE----VWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQL 694
Cdd:cd03261 76 RRRMGMLFQSGALFDSlTVFENvafpLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 695 VCLARALLRKTKILVLDEATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIM---DytRVIVLDKGEVRECGA 767
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFaiaD--RIAVLYDGKIVAEGT 220
|
....*.
gi 1907116879 768 PSELLQ 773
Cdd:cd03261 221 PEELRA 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-143 |
9.19e-26 |
|
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: 108.02 E-value: 9.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpMGLLKNK 80
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCV--CKLMANK 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 81 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLASEDDSV 143
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFSAERRNSI 273
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
551-760 |
2.20e-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: 104.54 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 551 EFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIglhnlRFKI 627
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLkaiLGLLK---PTSGSIRVFGKPLEKE-----RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQD-------PVLFSGSLRMNLDP----FSQYSDEE---VWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQ 693
Cdd:cd03235 71 GYVPQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEL-------ADRQIGE----LSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 694 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 760
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-120 |
3.10e-25 |
|
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: 111.00 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 2 EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKT 81
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRT 524
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907116879 82 RILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDG 120
Cdd:COG4988 525 VILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
566-775 |
3.13e-25 |
|
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: 104.96 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDP-------- 634
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFnlierlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 635 ---VLfSGSL-RMNLDP--FSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKIL 708
Cdd:cd03256 96 lenVL-SGRLgRRSTWRslFGLFPKEEKQRALAALERVG----LLDKAYQRADQ----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 709 VLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 775
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYAdRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
566-772 |
6.03e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 104.20 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFKITIIPQDPVLFSgslr 642
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLS---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 mnldpfSQYSDEEVWMALELAHLKG------------FVsALPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVL 710
Cdd:cd03258 96 ------SRTVFENVALPLEIAGVPKaeieervlelleLV-GLEDKADAYPA----QLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 711 DEATAAVDLE-TDNLIQ--STIRTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 772
Cdd:cd03258 165 DEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
550-762 |
1.19e-24 |
|
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: 102.57 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLfrINESAEGEIIIDGVNIAKIGLHNL-- 623
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVRVDGTDISKLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 624 --RFKITIIPQDPvlfsgslrmNLDP-FSQYsdEEVWMALELAHLKGFVSA-----------LPDKLNHECAEggenLSV 689
Cdd:cd03255 79 frRRHIGFVFQSF---------NLLPdLTAL--ENVELPLLLAGVPKKERReraeellervgLGDRLNHYPSE----LSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 690 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 762
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-127 |
2.00e-24 |
|
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: 102.62 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTHGISYL 92
Cdd:cd03249 125 LPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM---KGRTTIVIAHRLSTI 201
|
90 100 110
....*....|....*....|....*....|....*
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLR 127
Cdd:cd03249 202 RNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
566-762 |
5.08e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 99.39 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGVNIAKIGlHNLRFKITIIPQDPVLFSgslr 642
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIkiiLGLLKPDS---GEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYE---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 mnldpfsqysdeevwmalelaHLKGFvsalpdklnhecaeggENL--SVGQRQLVCLARALLRKTKILVLDEATAAVDLE 720
Cdd:cd03230 87 ---------------------NLTVR----------------ENLklSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907116879 721 TDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEV 762
Cdd:cd03230 130 SRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-124 |
7.38e-24 |
|
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: 100.77 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKvvgpmgLLKNKTRILVTHGI 89
Cdd:cd03251 124 LPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVqaaLER------LMKNRTTFVIAHRL 197
|
90 100 110
....*....|....*....|....*....|....*
gi 1907116879 90 SYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 124
Cdd:cd03251 198 STIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
566-761 |
1.38e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 98.41 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN--LRFKITIIPQDPVLFSG-SLR 642
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 MNLdpfsqysdeevwmalelahlkgfvsALPdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 722
Cdd:cd03229 95 ENI-------------------------ALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907116879 723 NLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGE 761
Cdd:cd03229 137 REVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-127 |
1.96e-23 |
|
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: 105.23 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 6 LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILV 85
Cdd:COG4987 450 LGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL---LEALAGRTVLLI 526
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907116879 86 THGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLR 127
Cdd:COG4987 527 THRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
550-784 |
4.88e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.68 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDP-VLFSGSLRMNLDPFS----QYSDEEVW-MALELAHLKGfvsaLPDKLNHEcaegGENLSVGQRQLVCLARALLR 703
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGlenkKVPPKKMKdIIDDLAKKVG----MEDYLDKE----PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 704 KTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
...
gi 1907116879 782 AKD 784
Cdd:PRK13632 240 KID 242
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
550-766 |
7.81e-23 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 97.20 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDGVNIAKIGLHnlRF 625
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTL-LrliaGLERP---DSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDPVLF----------SGsLRMNLDPFSQySDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLV 695
Cdd:cd03259 73 NIGMVFQDYALFphltvaeniaFG-LKLRGVPKAE-IRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 696 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECG 766
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
550-770 |
7.83e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.43 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFK 626
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 627 ITIIPQDP-----------VLFsgSLR-MNLDPfsQYSDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQL 694
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVAL--PLRvTGKSR--KEIRRRVREVLDLVGLSDKAKALP----HE-------LSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 695 VCLARALLRKTKILVLDEATAAVDLET-DNLIQstirtQFED-----CTVLtIA-HRLNTIMDY-TRVIVLDKGEVRECG 766
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETsWEIME-----LLEEinrrgTTVL-IAtHDLELVDRMpKRVLELEDGRLVRDE 219
|
....
gi 1907116879 767 APSE 770
Cdd:COG2884 220 ARGV 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
567-774 |
2.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.81 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA--KIGLHNLRFKITIIPQDP--VLFS---- 638
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 -----GSLRMNLdpfsqySDEEVWM----ALELAHLKgfVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 709
Cdd:PRK13637 103 kdiafGPINLGL------SEEEIENrvkrAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 710 LDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
550-775 |
8.35e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.46 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGLHNLRFKI 627
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDP--VLFSGSLR-------MNLdpfsQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLA 698
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 699 RALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 775
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCdNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
550-743 |
1.49e-21 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 93.69 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGVNIAKIGLHnlr 624
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLlriIAGLERP---TSGEVLVDGEPVTGPGPD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 625 fkITIIPQDPVLF---------SGSLRMNLDPFSQySDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLV 695
Cdd:cd03293 75 --RGYVFQQDALLpwltvldnvALGLELQGVPKAE-ARERAEELLELVGLSGFENAYP----HQ-------LSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 696 CLARALLRKTKILVLDEATAAVDLETDNLIQSTI-----RTQFedcTVLTIAH 743
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTH 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-124 |
1.79e-21 |
|
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: 99.81 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 9 DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmglLKNKTRILVTHG 88
Cdd:TIGR01193 593 DIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHR 668
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907116879 89 ISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 124
Cdd:TIGR01193 669 LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
567-775 |
2.49e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.67 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLtLGL---FRinESAEGEIIIDGVNIAKIGLHNlRfKITIIPQDPVLFSG-SLR 642
Cdd:COG3840 15 PLRFDLTIAAGERVAILGPSGAGKSTL-LNLiagFL--PPDSGRILWNGQDLTALPPAE-R-PVSMLFQENNLFPHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 MN----LDPFSQYSDEE---VWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATA 715
Cdd:COG3840 90 QNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 716 AVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 775
Cdd:COG3840 159 ALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIAdRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-127 |
3.04e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 10 LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTHGI 89
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS---RRQTTLMVTHQL 544
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907116879 90 SYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLR 127
Cdd:PRK11174 545 EDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
549-774 |
3.13e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.31 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 549 RVEFRDYclRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIGLHNLRF 625
Cdd:PRK13635 7 RVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL---PEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDP------------VLFSgsLRMNLDPFSQYSdEEVWMALELAHLKGFvsalpdkLNHECAeggeNLSVGQRQ 693
Cdd:PRK13635 82 QVGMVFQNPdnqfvgatvqddVAFG--LENIGVPREEMV-ERVDQALRQVGMEDF-------LNREPH----RLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 694 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSEL 771
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 1907116879 772 LQQ 774
Cdd:PRK13635 228 FKS 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
28-105 |
3.28e-21 |
|
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: 91.29 E-value: 3.28e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGK 105
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-123 |
4.31e-21 |
|
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: 92.93 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYL 92
Cdd:cd03252 124 LPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTV 200
|
90 100 110
....*....|....*....|....*....|.
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELLDRDGAFA 123
Cdd:cd03252 201 KNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
550-762 |
4.93e-21 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 92.09 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFK 626
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 627 ITIIPQDPVLFSG---------SLRMNLDPfSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCL 697
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 698 ARALLRKTKILVLDEATAAVDLETDNLIqSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEV 762
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-120 |
9.67e-21 |
|
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: 91.90 E-value: 9.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYL 92
Cdd:cd03254 125 LPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTI 201
|
90 100
....*....|....*....|....*...
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELLDRDG 120
Cdd:cd03254 202 KNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
261-521 |
4.39e-20 |
|
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: 91.46 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 261 VVNGTQANRNFRLSVYGALGILqgaAIFGYSMAVSIGGIFASRRLHLDLLYN--------VLRSPMSFFERTPSGNLVNR 332
Cdd:cd07346 25 LIDDVIPAGDLSLLLWIALLLL---LLALLRALLSYLRRYLAARLGQRVVFDlrrdlfrhLQRLSLSFFDRNRTGDLMSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 333 FSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKrlESVSRspV 408
Cdd:cd07346 102 LTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRRRIRKASREVR--ESLAE--L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 409 YSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSA 484
Cdd:cd07346 178 SAFLQESLSGIRVVKAFaaeeREIERFREANRDLRDANLRAARLSALFSPLIGL-LTALGTALVLLYGGYLVL-QGSLTI 255
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907116879 485 GLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERL 521
Cdd:cd07346 256 GELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
566-762 |
5.19e-20 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 87.48 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGlHNLRFKITIIPQdpvlfsgslrm 643
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPR-DARRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 nldpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL-ETD 722
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907116879 723 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 762
Cdd:cd03216 120 RLFKVIRRLRAQGVAVIFISHRLDEVFEIAdRVTVLRDGRV 160
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
357-778 |
5.39e-20 |
|
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: 95.78 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 357 SVIGAVIIILLATPIAAViipplglVYFFVQRFYVAssrQLKrlesvSRSPVYSHFNETLLGVSVIR------AFEEQER 430
Cdd:TIGR00957 459 SVLAGVAVMVLMVPLNAV-------MAMKTKTYQVA---HMK-----SKDNRIKLMNEILNGIKVLKlyawelAFLDKVE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 431 FIHQSDLKVDEnQKAYYPSIVANRWLavrleCVGNCIVL--FAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMS 508
Cdd:TIGR00957 524 GIRQEELKVLK-KSAYLHAVGTFTWV-----CTPFLVALitFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 509 SEMETNIVAVERLKEYSETEKEAPWQIQETAPPSTWPHSgrVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGA 588
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNS--ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGC 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 589 GKSSLTLGLFRINESAEGEIIIDGvniakiglhnlrfKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGF 668
Cdd:TIGR00957 676 GKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPD 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 669 VSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI---RTQFEDCTVLTIAHRL 745
Cdd:TIGR00957 743 LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGI 822
|
410 420 430
....*....|....*....|....*....|...
gi 1907116879 746 NTIMDYTRVIVLDKGEVRECGAPSELLQQRGIF 778
Cdd:TIGR00957 823 SYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-106 |
8.92e-20 |
|
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: 88.80 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 14 PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLP 93
Cdd:cd03245 127 PNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLD 203
|
90
....*....|...
gi 1907116879 94 QVDVIIVMSGGKI 106
Cdd:cd03245 204 LVDRIIVMDSGRI 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-145 |
1.34e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 93.24 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpmglLKN-------KTRILV 85
Cdd:PRK10789 437 LPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI----------LHNlrqwgegRTVIIS 506
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 86 THGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRtYANAEQDLASEDDSVSG 145
Cdd:PRK10789 507 AHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR-YQQLEAALDDAPEIREE 565
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
567-760 |
1.53e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 88.16 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL----RFKITIIPQDPVLFSGSLR 642
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 MNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-T 721
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907116879 722 DNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKG 760
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
566-774 |
1.89e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSltlgLFR-IN--ESA-EGEIIIDGVNIAKI---GLHNLRFKITIIPQDpvlFs 638
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRcINllERPtSGSVLVDGVDLTALserELRAARRKIGMIFQH---F- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 gslrmNLdpFSQYSDEE-VWMALELAHLKG------------FVSaLPDKLNHECAEggenLSVGQRQLVCLARALLRKT 705
Cdd:COG1135 92 -----NL--LSSRTVAEnVALPLEIAGVPKaeirkrvaelleLVG-LSDKADAYPSQ----LSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 706 KILVLDEATAAVDLETD----NLIQStIRTQFeDCTVLTIAHRLN---TIMDytRVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG1135 160 KVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDvvrRICD--RVAVLENGRIVEQGPVLDVFAN 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
550-771 |
2.30e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.65 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPV-LFSGSL-----RMNLDPFSQYSDEevwMALELAHLKGFVSALpDKLNHEcaegGENLSVGQRQLVCLARALLR 703
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDE---MHRRVSEALKQVDML-ERADYE----PNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 704 KTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSEL 771
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
549-730 |
3.71e-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: 86.38 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 549 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGVNIAKIGLHnLRF 625
Cdd:COG4133 2 MLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLlrILaGLLPP---SAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDPVLFSG-SLRMNLDpFSQ------YSDEEVWMALELAHLKGFvsalpdkLNHECAeggeNLSVGQRQLVCLA 698
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FWAalyglrADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|..
gi 1907116879 699 RALLRKTKILVLDEATAAVDLETDNLIQSTIR 730
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
567-774 |
3.93e-19 |
|
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: 91.67 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvlFsGSL-- 641
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 642 RMN-----------LDPfsQYSDEE----VWMALELAHLKgfvsalPDKLN---HEcaeggenLSVGQRQLVCLARALLR 703
Cdd:COG4172 378 RMTvgqiiaeglrvHGP--GLSAAErrarVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 704 KTKILVLDEATAAVDLetdnliqsTIRTQfedctVLT---------------IAHRLN---TIMDytRVIVLDKGEVREC 765
Cdd:COG4172 443 EPKLLVLDEPTSALDV--------SVQAQ-----ILDllrdlqrehglaylfISHDLAvvrALAH--RVMVMKDGKVVEQ 507
|
....*....
gi 1907116879 766 GAPSELLQQ 774
Cdd:COG4172 508 GPTEQVFDA 516
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
566-773 |
4.30e-19 |
|
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: 86.72 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN-LRFKITIIPQDPVLFSG----- 639
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPEltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 SLRMNLDPFSQYSDEEVW-MALELahlkgFvSALPDKLNHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAvd 718
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRVYEL-----F-PRLKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 719 letdnlIQSTIRTQFEDC---------TVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQ 773
Cdd:cd03224 163 ------LAPKIVEEIFEAirelrdegvTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
545-764 |
1.55e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.91 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 545 PHSGRVEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGVNIAKI 618
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLiaglEKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 619 GLhnlrfKITIIPQDPVLF----------SGsLRMNLDPFSQYsDEEVWMALELAHLKGFVSALPdklnHEcaeggenLS 688
Cdd:COG1116 79 GP-----DRGVVFQEPALLpwltvldnvaLG-LELRGVPKAER-RERARELLELVGLAGFEDAYP----HQ-------LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 689 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAH------RLNtimdyTRVIVLDK- 759
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLA-----DRVVVLSAr 215
|
....*.
gi 1907116879 760 -GEVRE 764
Cdd:COG1116 216 pGRIVE 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
550-787 |
1.60e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.78 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFK 626
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 627 ITIIPQDP-VLFSGSLRMNLDPFS----QYSDEE----VWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCL 697
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGlenrAVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 698 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQR 775
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
250
....*....|..
gi 1907116879 776 gifySMAKDAGL 787
Cdd:PRK13640 235 ----EMLKEIGL 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
550-772 |
2.09e-18 |
|
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: 85.52 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLF--RINESAEGEIII-----DGVNI----AKI 618
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTL-LSLItgDLPPTYGNDVRLfgerrGGEDVwelrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 619 GL------HNLRFKITIIpqDPVL--FSGSLrmnlDPFSQYSDEEV-----WMA-LELAHLKgfvsalpDKLNHEcaegg 684
Cdd:COG1119 81 GLvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQRerareLLElLGLAHLA-------DRPFGT----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 685 enLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMD-YTRVIVLDKGE 761
Cdd:COG1119 143 --LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGR 220
|
250
....*....|.
gi 1907116879 762 VRECGAPSELL 772
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
566-764 |
2.14e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.71 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFrinESA-EGEIIIDGVNIAKIG---LHNLRF-KITIIPQDPvlfs 638
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGGL---DRPtSGEVLIDGQDISSLSereLARLRRrHIGFVFQFF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 gslrmNLDPFsqYSDEE-VWMALELAHLKGFVSA-----------LPDKLNHECAEggenLSVGQRQLVCLARALLRKTK 706
Cdd:COG1136 96 -----NLLPE--LTALEnVALPLLLAGVSRKERRerarellervgLGDRLDHRPSQ----LSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 707 ILVLDEATAAVDLETD----NLIQSTIRTQfeDCTVLTIAH--RLNTIMDytRVIVLDKGEVRE 764
Cdd:COG1136 165 LILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHdpELAARAD--RVIRLRDGRIVS 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-127 |
2.15e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKvvgpmgLLKNKTRILVTHGI 89
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDE------LQKNRTSLVIAHRL 539
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907116879 90 SYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLR 127
Cdd:PRK11176 540 STIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHK 577
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
550-773 |
2.16e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.14 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGLHNLRFKI 627
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPVLFS----------GSLRMNldpfSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCL 697
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR----GASKEEAEKQARELLAKVG----LAERAHHYPSE----LSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 698 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQ 773
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
567-770 |
2.24e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.16 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFKITIIPQDPVLFSgslrm 643
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKARRQIGMIFQHFNLLS----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 nldpfSQYSDEEVWMALELAHL-KGFVSA----------LPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVLDE 712
Cdd:PRK11153 96 -----SRTVFDNVALPLELAGTpKAEIKArvtellelvgLSDKADRYPA----QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 713 ATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRlntiMDYT-----RVIVLDKGEVRECGAPSE 770
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRElgLTIVLITHE----MDVVkricdRVAVIDAGRLVEQGTVSE 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
564-744 |
3.73e-18 |
|
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: 82.59 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 564 DLVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFR-INE---SAEGEIIIDGVNiakiglhnlrfKITIIPQDPVLFSG 639
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRaLAGlwpWGSGRIGMPEGE-----------DLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 SLRmnldpfsqysdEEV---WMalelahlkgfvsalpdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:cd03223 79 TLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*...
gi 1907116879 717 VDLETDNLIQSTIRTQFedCTVLTIAHR 744
Cdd:cd03223 122 LDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-152 |
3.87e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.86 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 14 PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGkhifEKVVGPM-GLLKNKTRILVTHGISYL 92
Cdd:PRK13657 458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE----AKVKAALdELMKGRTTFIIAHRLSTV 533
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTyanaeQDLASEDDSVSGSGKESKP 152
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVARGGRFAALLRA-----QGMLQEDERRKQPAAEGAN 588
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
550-772 |
7.45e-18 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 83.50 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDLVlKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLFSG-SLRMN--LDP-FSQYSDEEV-WMALELAHLKGFVSA-LPDKLNHEcaeggenLSVGQRQLVCLARALLR 703
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLALVGLDPAeFADRYPHE-------LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 704 KTKILVLDEATAAVDLET-DNLIQSTIRTQFE-DCTVLTIAHRLN-TIMDYTRVIVLDKGEVRECGAPSELL 772
Cdd:cd03295 153 DPPLLLMDEPFGALDPITrDQLQEEFKRLQQElGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
275-453 |
7.65e-18 |
|
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: 84.75 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 275 VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 354
Cdd:cd18544 46 LYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 355 LFSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAFEEQE 429
Cdd:cd18544 126 LLLLIGILIAMFllnwrLAL-ISLLVLPLLLLATYLFRKKSRKAYREVR--EKLSR--LNAFLQESISGMSVIQLFNREK 200
|
170 180
....*....|....*....|....
gi 1907116879 430 RFIHQSDLKVDENQKAYYPSIVAN 453
Cdd:cd18544 201 REFEEFDEINQEYRKANLKSIKLF 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-124 |
8.60e-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: 87.57 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFE--KVVGpmgllKNKTRILVTHGIS 90
Cdd:COG5265 480 LPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAalREVA-----RGRTTLVIAHRLS 554
|
90 100 110
....*....|....*....|....*....|....
gi 1907116879 91 YLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 124
Cdd:COG5265 555 TIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
566-771 |
9.56e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGvniAKIGLHN----LRFKITIIPQDPVL 636
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS--TLmkilsGVYQPDS---GEILLDG---EPVRFRSprdaQAAGIAIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 FSgslrmNLdpfsqySDEE-VWMALELAHlKGFVSalPDKLNHECAE-----G--------GENLSVGQRQLVCLARALL 702
Cdd:COG1129 91 VP-----NL------SVAEnIFLGREPRR-GGLID--WRAMRRRAREllarlGldidpdtpVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 703 RKTKILVLDEATAAVDL-ETDNLIQsTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 771
Cdd:COG1129 157 RDARVLILDEPTASLTErEVERLFR-IIRRlKAQGVAIIYISHRLDEVFEIAdRVTVLRDGRLVGTGPVAEL 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
566-774 |
1.00e-17 |
|
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: 85.10 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDGVNIAKIG---LHNLRFK-ITIIPQDPvlfs 638
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLAraiLGLLPPPGITSGEILFDGEDLLKLSekeLRKIRGReIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 gslrMN-LDP--------------FSQYSDEEVW-MALELAHLKGFVSAlPDKLN---HEcaeggenLSVGQRQLVCLAR 699
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIELLERVGLPDP-ERRLDrypHE-------LSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 700 ALLRKTKILVLDEATAAVD-------LetdNLIQStIRTQFeDCTVLTIAHRLNT---IMDytRVIVLDKGEVRECGAPS 769
Cdd:COG0444 164 ALALEPKLLIADEPTTALDvtiqaqiL---NLLKD-LQREL-GLAILFITHDLGVvaeIAD--RVAVMYAGRIVEEGPVE 236
|
....*
gi 1907116879 770 ELLQQ 774
Cdd:COG0444 237 ELFEN 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
567-786 |
1.07e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 88.49 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdgvniakiglhnLRFKITIIPQDPVLFSGSLRMNLD 646
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 647 PFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-TDNLI 725
Cdd:PLN03232 701 FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVF 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 726 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAKDAG 786
Cdd:PLN03232 781 DSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAG 841
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
566-762 |
2.94e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGVNIAKIGLHNlRFK-ITIIPQDPVL---F 637
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL-LnaiaGSLPPDS---GSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMgtaP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 SGSLRMNLDpfsqysdeevwMALELAHLKGFVSALPDKLNHECAE-------GGEN--------LSVGQRQLVCLARALL 702
Cdd:COG1101 96 SMTIEENLA-----------LAYRRGKRRGLRRGLTKKRRELFREllatlglGLENrldtkvglLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 703 RKTKILVLDEATAAVD-------LE-TDNLIQStirtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEV 762
Cdd:COG1101 165 TKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
573-756 |
3.78e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 573 TIEGGEKVGIVGRTGAGKSslTLG--LFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvlfSGSL--RMN- 644
Cdd:COG4608 40 DIRRGETLGLVGESGCGKS--TLGrlLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRMTv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 645 -------LDPFSQYS----DEEVWMALELAHLKgfvsalPDKLN---HEcaeggenLSVGQRQLVCLARALLRKTKILVL 710
Cdd:COG4608 115 gdiiaepLRIHGLASkaerRERVAELLELVGLR------PEHADrypHE-------FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 711 DEATAAVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIV 756
Cdd:COG4608 182 DEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAV 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
549-772 |
4.03e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 549 RVEFRDYCLryrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-LHNLRFKI 627
Cdd:PRK13644 3 RLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDPV-----------LFSGSLRMNLDPFSqySDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVC 696
Cdd:PRK13644 80 GIVFQNPEtqfvgrtveedLAFGPENLCLPPIE--IRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 697 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELL 772
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-123 |
4.21e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVgkhifEKVVGPMGLLKNKTRILVTHGISYL 92
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTV 677
|
90 100 110
....*....|....*....|....*....|.
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELLDRDGAFA 123
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
566-762 |
4.27e-17 |
|
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: 80.65 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLFSgslRM 643
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 N------LDP---FSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 714
Cdd:cd03262 92 TvlenitLAPikvKGMSKAEAEERALELLEKVG----LADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 715 AAVDLETDNLIQSTIRTQFED-CTVLTIAHRlntiMDY-----TRVIVLDKGEV 762
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEgMTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
567-762 |
6.68e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDG--VNI--------AKIGLhnlrfkitiIP 631
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKS--TLmkilyGLYQPDS---GEILIDGkpVRIrsprdaiaLGIGM---------VH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 632 QDPVLFsgslrmnlDPFSQYsdEEVWMALElaHLKGFVSALpDKLNHE----CAEGG---------ENLSVGQRQLVCLA 698
Cdd:COG3845 87 QHFMLV--------PNLTVA--ENIVLGLE--PTKGGRLDR-KAARARirelSERYGldvdpdakvEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 699 RALLRKTKILVLDEATaAV--DLETDNLIQsTIRtQF--EDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 762
Cdd:COG3845 154 KALYRGARILILDEPT-AVltPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIAdRVTVLRRGKV 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-127 |
7.11e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 7.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 21 IGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLL----KNKTRILVTHGISYLPQVD 96
Cdd:PRK11160 469 LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFD 541
|
90 100 110
....*....|....*....|....*....|.
gi 1907116879 97 VIIVMSGGKISEMGSYQELLDRDGAFAEFLR 127
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
566-771 |
8.13e-17 |
|
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: 84.47 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE---GEII--------------------------------- 609
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 610 IDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLR-----MNLDPFSQYS-DEEVWMALELAHLKgfvsalpdKLNHECAEG 683
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIEMV--------QLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 684 GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 760
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDLSdKAIWLENG 245
|
250
....*....|.
gi 1907116879 761 EVRECGAPSEL 771
Cdd:TIGR03269 246 EIKEEGTPDEV 256
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
550-771 |
8.26e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.32 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLD-LVLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGVNIAKIGLHNLRF 625
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDP-VLFSGSLRMNLDPFS--------QYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVC 696
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGlenkgiphEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 697 LARALLRKTKILVLDEATAAVD----LETDNLIQStIRTQFeDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSEL 771
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDpegrLELIKTIKG-IRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
550-772 |
1.27e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 80.07 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREdldLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAkiGLHNLRFKITI 629
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLF---------SGSLRMNLDPFSQySDEEVwmaLELAHLKGFVSALPDKlnhecaegGENLSVGQRQLVCLARA 700
Cdd:cd03299 76 VPQNYALFphmtvykniAYGLKKRKVDKKE-IERKV---LEIAEMLGIDHLLNRK--------PETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 701 LLRKTKILVLDEATAAVDLET-DNLIQ--STIRTQFeDCTVLTIAHRLNTI-MDYTRVIVLDKGEVRECGAPSELL 772
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
563-772 |
1.27e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 563 LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFK--------ITIIP 631
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 632 QDPVLFSGSLRMNLDPF-SQYSDEEVWMALELAHLKGFVSALPDKlnhecaeggenLSVGQRQLVCLARALLRKTKILVL 710
Cdd:PRK10070 120 HMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 711 DEATAAVDletdnliqSTIRTQFED----------CTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 772
Cdd:PRK10070 189 DEAFSALD--------PLIRTEMQDelvklqakhqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
275-521 |
1.55e-16 |
|
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: 80.68 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 275 VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 354
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 355 LFSVIGAVIIILLA----TPIAAVIIPPLGLVYFFVQRFYVASSRQLkrLESVSRSPvySHFNETLLGVSVIRAFEEQER 430
Cdd:cd18557 121 ILQVIGGLIILFILswklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAEESLSNIRTVRSFSAEEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 431 FIHQSDLKVDENQKAYYPSIVAN---RWLAVRLECVGNCIVLFAALFAVISRHsLSAGLVGLSVSYSLQITAYLNWLVRM 507
Cdd:cd18557 197 EIRRYSEALDRSYRLARKKALANalfQGITSLLIYLSLLLVLWYGGYLVLSGQ-LTVGELTSFILYTIMVASSVGGLSSL 275
|
250
....*....|....
gi 1907116879 508 SSEMETNIVAVERL 521
Cdd:cd18557 276 LADIMKALGASERV 289
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
566-770 |
2.58e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 79.02 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGVNI--------AKIGLHnlR-FKITIIPQD 633
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFnliSGFLRPTS---GSVLFDGEDItglppheiARLGIG--RtFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 634 ---------PVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAeggeNLSVGQRQLVCLARALLRK 704
Cdd:cd03219 90 ltvlenvmvAAQARTGSGLLLARARREEREARERAEELLERVG----LADLADRPAG----ELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 705 TKILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSE 770
Cdd:cd03219 162 PKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
566-772 |
3.67e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtlgLFRINES---AEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVL---FSG 639
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTL---LRAINGTltpTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 S--LRMNLDP----FSQYSDEEVwMALELAHLKGFVSALPDKlnhecaeGGENLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:PRK09536 95 RqvVEMGRTPhrsrFDTWTETDR-AAVERAMERTGVAQFADR-------PVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 714 TAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGkTAVAAIHDLDLAARYCdELVLLADGRVRAAGPPADVL 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
549-771 |
4.05e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.93 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 549 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNI--AKIGLH 621
Cdd:COG1117 11 KIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 622 NLRFKITIIPQDPVLFSGS--------LRMNLDPFSQYSDEEVWMALELAHL----KgfvsalpDKLNhecaEGGENLSV 689
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALwdevK-------DRLK----KSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 690 GQRQLVCLARALLRKTKILVLDEATAAVD-LETDNlIQSTIRTQFEDCTVLTIAHRLNT---IMDYTrvIVLDKGEVREC 765
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHNMQQaarVSDYT--AFFYLGELVEF 234
|
....*.
gi 1907116879 766 GAPSEL 771
Cdd:COG1117 235 GPTEQI 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-101 |
4.43e-16 |
|
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: 81.95 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 2 EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKT 81
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRT 509
|
90 100
....*....|....*....|
gi 1907116879 82 RILVTHGISYLPQVDVIIVM 101
Cdd:TIGR02857 510 VLLVTHRLALAALADRIVVL 529
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
566-770 |
4.80e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.54 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL----TlGLFRINEsaeGEIIIDGVNI--------AKIGLhnLR-FKIT-IIP 631
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnliT-GFYRPTS---GRILFDGRDItglpphriARLGI--ARtFQNPrLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 632 QDPVL----------FSGSLRMNLDPFSQYSDEEVWM---ALELAHLKGfvsaLPDKLNHECAeggeNLSVGQRQLVCLA 698
Cdd:COG0411 93 ELTVLenvlvaaharLGRGLLAALLRLPRARREEREArerAEELLERVG----LADRADEPAG----NLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 699 RALLRKTKILVLDEATAAVDL-ETDNLIQsTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSE 770
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLAdRIVVLDFGRVIAEGTPAE 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
566-780 |
6.09e-16 |
|
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: 79.13 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGvniakiglhnlrfKITIIPQDPVLFSGSLRMNL 645
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 725
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 726 qstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYS 780
Cdd:cd03291 199 -------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSS 254
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
550-774 |
8.83e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.20 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA--KIGLHNLRFKI 627
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 628 TIIPQDP--VLFSGSLR-------MNLDPFSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLA 698
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 699 RALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
569-762 |
9.84e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 76.76 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 569 HINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGVNIAkiGLHNLRFKITIIPQDPVLFSG-------- 639
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL-LNLIAGFETPQsGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHltveqnvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 ---SLRMNLDPFSQysdEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:cd03298 93 lglSPGLKLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907116879 717 VD--LETDNL-IQSTIRTQfEDCTVLTIAHRLNTIMD-YTRVIVLDKGEV 762
Cdd:cd03298 159 LDpaLRAEMLdLVLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
567-774 |
1.34e-15 |
|
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: 77.68 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFK--------ITIIPQDPV 635
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 636 LFSGSLRMNLDPFSQYSDEEVWM-ALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 714
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAeALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 715 AAVDletdnliqSTIRTQFEDC----------TVLTIAHRLNTIM---DytRVIVLDKGEVRECGAPSELLQQ 774
Cdd:cd03294 189 SALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALrlgD--RIAIMKDGRLVQVGTPEEILTN 251
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
566-774 |
2.89e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFrineSAE-----GEIIIDGVNIAKIGLHNLRFKITIIPQDPVL-FSG 639
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTL-LRAL----SGElspdsGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 S----LRMNLDPFSQYSDE-----EVWMAL-ELAHLKGfvsalpdKLNHEcaeggenLSVGQRQLVCLARALLR------ 703
Cdd:PRK13548 92 TveevVAMGRAPHGLSRAEddalvAAALAQvDLAHLAG-------RDYPQ-------LSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 704 KTKILVLDEATAAVDL----ETDNLIQStiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13548 158 PPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNLAARYAdRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
566-766 |
3.55e-15 |
|
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: 74.92 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIaKIGLHNLRFKITIIPQDpvlFSGSLRMNL 645
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQE---FGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPFSQY-----------SDEEVWMALELAHLKGFVSalpDKLNhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEAT 714
Cdd:cd03264 90 REFLDYiawlkgipskeVKARVDEVLELVNLGDRAK---KKIG--------SLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 715 AAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMD-YTRVIVLDKGEVRECG 766
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
566-775 |
3.62e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSG-SLR-- 642
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 --------MNL-DPFSQYSDEEVWMALELAHlkgfVSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:PRK11231 97 vaygrspwLSLwGRLSAEDNARVNQAMEQTR----INHLADRR-------LTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 714 TAAVDL----ETDNLIQstiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 775
Cdd:PRK11231 166 TTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYCdHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
550-771 |
4.65e-15 |
|
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: 75.35 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYreDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHnlRFKITI 629
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLF---------SGSLRMNLDPfSQYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARA 700
Cdd:cd03300 77 VFQNYALFphltvfeniAFGLRLKKLP-KAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 701 LLRKTKILVLDEATAAVD--------LETDNLIQSTirtqfeDCTVLTIAHRLN---TIMDytRVIVLDKGEVRECGAPS 769
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDlklrkdmqLELKRLQKEL------GITFVFVTHDQEealTMSD--RIAVMNKGKIQQIGTPE 216
|
..
gi 1907116879 770 EL 771
Cdd:cd03300 217 EI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
566-774 |
5.00e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.45 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGVNIAKIGLHNlRfKITIIPQDPVLFS--- 638
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL-LrmiaGFETPDS---GRILLDGRDVTGLPPEK-R-NVGMVFQDYALFPhlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 -------GsLRM-NLDPfsQYSDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARALLRKTKILVL 710
Cdd:COG3842 94 vaenvafG-LRMrGVPK--AEIRARVAELLELVGLEGLADRYP----HQ-------LSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 711 DEATAAVDLETdnliqsTIRTQFEdctVLTIAHRLN--TIM------------DytRVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG3842 160 DEPLSALDAKL------REEMREE---LRRLQRELGitFIYvthdqeealalaD--RIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
260-436 |
6.22e-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: 75.92 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 260 PVVNGTQANRNFRLSVYGALGI-----LQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFS 334
Cdd:cd18552 24 PLLDDIFVEKDLEALLLVPLAIiglflLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRIT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 335 KELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLA----TPIAAVIIPPLGL-VYFFVQRFYVASSRQLKRLESVSrspvy 409
Cdd:cd18552 104 NDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdwklTLIALVVLPLAALpIRRIGKRLRKISRRSQESMGDLT----- 178
|
170 180 190
....*....|....*....|....*....|.
gi 1907116879 410 SHFNETLLGVSVIRAF----EEQERFIHQSD 436
Cdd:cd18552 179 SVLQETLSGIRVVKAFgaedYEIKRFRKANE 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
27-118 |
2.00e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.57 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfEKVVgpMGLLK--NKTRILVTH------GISylpqvDVI 98
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL-RRWL--RRLHDelGGTTVFVTHdqeealELA-----DRV 204
|
90 100
....*....|....*....|
gi 1907116879 99 IVMSGGKISEMGSYQELLDR 118
Cdd:COG1118 205 VVMNQGRIEQVGTPDEVYDR 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
566-772 |
2.56e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.41 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNIAKIGLHNLRFKITIIPQDP------ 634
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 635 -VLFSGSLRMNLDPFSQYSDE---EVWMALELAHLKGFVSalpDKLNhecAEGGEnLSVGQRQLVCLARALLRKTKILVL 710
Cdd:PRK14247 98 sIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVK---DRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 711 DEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEVRECGAPSELL 772
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREVF 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-106 |
3.01e-14 |
|
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: 72.89 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVgpMGLLKNKTRILVTHGISYL 92
Cdd:cd03248 136 LASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTV 212
|
90
....*....|....
gi 1907116879 93 PQVDVIIVMSGGKI 106
Cdd:cd03248 213 ERADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-118 |
4.17e-14 |
|
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: 75.94 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhvgkhifekvVGPMGLL--------KNKTRIL 84
Cdd:COG4618 453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD----------EGEAALAaairalkaRGATVVV 522
|
90 100 110
....*....|....*....|....*....|....
gi 1907116879 85 VTHGISYLPQVDVIIVMSGGKISEMGSYQELLDR 118
Cdd:COG4618 523 ITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
550-787 |
4.52e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLD----LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-LHNLR 624
Cdd:PRK13633 5 IKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 625 FKITIIPQDP------------VLFsGSLRMNLDPfsqysdEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQR 692
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAF-GPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHL-------LSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 693 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSE 770
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
250
....*....|....*..
gi 1907116879 771 LLQQrgifYSMAKDAGL 787
Cdd:PRK13633 231 IFKE----VEMMKKIGL 243
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-111 |
4.86e-14 |
|
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: 72.14 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 2 EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKT 81
Cdd:cd03244 114 ERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI---REAFKDCT 190
|
90 100 110
....*....|....*....|....*....|
gi 1907116879 82 RILVTHGISYLPQVDVIIVMSGGKISEMGS 111
Cdd:cd03244 191 VLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
566-781 |
6.10e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 76.10 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGvniakiglhnlrfKITIIPQDPVLFSGSLRMNL 645
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 725
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 726 qstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 781
Cdd:TIGR01271 588 -------FESClcklmsnkTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
28-110 |
7.40e-14 |
|
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: 71.40 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpmGLLKN--KTRILVTHGIS-YLPQVDVIIVMSGG 104
Cdd:cd03259 131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELK---ELQRElgITTIYVTHDQEeALALADRIAVMNEG 207
|
....*.
gi 1907116879 105 KISEMG 110
Cdd:cd03259 208 RIVQVG 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
566-771 |
7.49e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-LHNLRFKITIIPQDPVLFSG-SLRM 643
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLD---PFSQYSDEEvwmalelahLKGFVSALPDKLNHECAEGgeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD-L 719
Cdd:PRK15439 106 NILfglPKRQASMQK---------MKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 720 ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 771
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
566-774 |
7.51e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.60 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLfriNESAEGEIIIDGVNIAKIGLHNLrfKITIIPQDPVLFSG--- 639
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTvlrLVAGL---EKPTEGQIFIDGEDVTHRSIQQR--DICMVFQSYALFPHmsl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 ------SLRMNLDPFSQYSdEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:PRK11432 96 genvgyGLKMLGVPKEERK-QRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 714 TAAVDLETDNLIQSTIR---TQFeDCTVLTIAHrlntimDYTR-------VIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK11432 164 LSNLDANLRRSMREKIRelqQQF-NITSLYVTH------DQSEafavsdtVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
550-772 |
8.15e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDL-VLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGVNIAKIGLHNLRF 625
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLF---EEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDP-VLFSGSLRMNLDPFSQYSD----EEVWMALELAHLKgfVSALPDKLNHECaeggeNLSVGQRQLVCLARA 700
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA--VNMLDFKTREPA-----RLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 701 LLRKTKILVLDEATAAVDLETDNLIQSTIRtQFED---CTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELL 772
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
566-763 |
1.01e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSltlgLFRI----NESAEGEIIIDGvniakiglhnlRFKITIIPQDPVLFSG-S 640
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKIlageLEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRmnldpfsqysdEEVWMAL-----------ELAHLKGFVSALPDK---LNHECAEGGE--------------------- 685
Cdd:COG0488 78 VL-----------DTVLDGDaelraleaeleELEAKLAEPDEDLERlaeLQEEFEALGGweaearaeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 686 -----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqfEDCTVLTIAH-R--LNTIMdyTRVIVL 757
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRVA--TRILEL 222
|
....*.
gi 1907116879 758 DKGEVR 763
Cdd:COG0488 223 DRGKLT 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
304-712 |
1.11e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 74.45 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 304 RLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVdSMIPQVIKMFMGSLFSVIGAVI-IILLATPIAAVIIPPLGLV 382
Cdd:COG4615 82 RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAyLAWLSPPLFLLTLVLLGLG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 383 yFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllgvSVIRAFEE----QER--FIHQSDLKV------DENQKAYYPSI 450
Cdd:COG4615 161 -VAGYRLLVRRARRHLRRAREAEDRLFKHFR------ALLEGFKElklnRRRrrAFFDEDLQPtaeryrDLRIRADTIFA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 451 VANRWlavrlecvGNCIVLFA---ALFAVISRHSLSAGLVglsVSYSL----------QITAYLNWLVRMSsemetniVA 517
Cdd:COG4615 234 LANNW--------GNLLFFALiglILFLLPALGWADPAVL---SGFVLvllflrgplsQLVGALPTLSRAN-------VA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 518 VERLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLD---LVLKHINVTIEGGEKVGIVGRTGAGKSSLT 594
Cdd:COG4615 296 LRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 595 ---LGLFRineSAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGslrmNLDPFSQYSDEEV--WMA-LELAHLKGF 668
Cdd:COG4615 376 kllTGLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARAreLLErLELDHKVSV 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907116879 669 vsalpdklnhecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDE 712
Cdd:COG4615 449 -------------EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
27-118 |
1.15e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.18 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvgkhifekvvgpmglLKNKTR--------------ILVTHGisyl 92
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK---------------LRVEMRaeikrlhrrlgtttIYVTHD---- 193
|
90 100 110
....*....|....*....|....*....|..
gi 1907116879 93 pQV------DVIIVMSGGKISEMGSYQELLDR 118
Cdd:COG3839 194 -QVeamtlaDRIAVMNDGRIQQVGTPEELYDR 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
225-521 |
1.19e-13 |
|
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: 72.08 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 225 AIGLFITFLSIFLFLcnhvsalaSNYWLSLWT-DDppVVNGTQANRNFRLSV-YGALGILQGAAIFGYSMAVSIGGIFAS 302
Cdd:cd18542 2 LLAILALLLATALNL--------LIPLLIRRIiDS--VIGGGLRELLWLLALlILGVALLRGVFRYLQGYLAEKASQKVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 303 RRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIIL-----LATpIAAVIIP 377
Cdd:cd18542 72 YDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFsinwkLTL-ISLAIIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 378 PLGLV-YFF---VQRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA---- 445
Cdd:cd18542 151 FIALFsYVFfkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFaredYEIEKFDKENEEYRDLNIKLakll 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 446 --YYPSIVAnrwlavrLECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYslqiTAYLNWLVRMS----SEMETNIVAV 518
Cdd:cd18542 223 akYWPLMDF-------LSGLQIVLVLWVGGYLVI-NGEITLGeLVAFI-SY----LWMLIWPVRQLgrliNDMSRASASA 289
|
...
gi 1907116879 519 ERL 521
Cdd:cd18542 290 ERI 292
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
566-772 |
1.22e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV------NIAKIGLHNLRFKITIIPQDPVLFSG 639
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 -SLRMNLD-PFSQY---SDEEVWMALELAHLK-GFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRKvGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 714 TAAVDLETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEVRECGAPSELL 772
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEWGSSNEIF 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
567-786 |
1.42e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSL-TLGLFRINESAEGEIIIDGvniakiglhnlrfKITIIPQDPVLFSGSLRMNL 645
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET-DNL 724
Cdd:PLN03130 700 LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQV 779
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 725 IQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAKDAG 786
Cdd:PLN03130 780 FDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAG 841
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
232-520 |
1.70e-13 |
|
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: 72.05 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 232 FLSIFLFLCNHVSALASNYWLSLWTDDPPVVNGTQANRNFRlSVYGALGILQG----AAIFGYSMAVSIGGI--FASRRL 305
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFS-GLLRILLLLLGlyllSALFSYLQNRLMARVsqRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 306 HLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGL 381
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPlltlIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 382 VYFFV----QRFYVASSRQLKRLEsvsrspvySHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWL- 456
Cdd:cd18547 161 VTKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLm 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 457 -AVRLecVGN----CIVLFAALFAVisRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVER 520
Cdd:cd18547 233 pIMNF--INNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
550-772 |
3.38e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDP--VLFS---------GSLRMNLDPfsQYSDEEVWMALELAHLKgfvsALPDKLNHecaeggeNLSVGQRQLVCLA 698
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMW----DFRDKPPY-------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 699 RALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRgQETLMEILDRLHNQGKTVIVATHDVDLAAEWAdQVIVLKEGRVLAEGDKSLLT 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
565-766 |
3.59e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 69.32 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 565 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRfKITIIPQDPVLFSG-SLRM 643
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLDPFSQYsdeevwMALELAHLKGFVSALPDKL--NHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 721
Cdd:cd03266 98 NLEYFAGL------YGLKGDELTARLEELADRLgmEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907116879 722 DNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVRECG 766
Cdd:cd03266 172 TRALREFIRQLRALgKCILFSTHIMQEVERLCdRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
566-772 |
3.60e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAK--------------------IGLHNLRF 625
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiqmvfqdsISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDPvlfsgsLR--MNLDPFSQYSdeevwMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLR 703
Cdd:PRK10419 107 TVREIIREP------LRhlLSLDKAERLA-----RASEMLRAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 704 KTKILVLDEATAAVDLetdnLIQSTI-------RTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 772
Cdd:PRK10419 169 EPKLLILDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKL 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
532-766 |
3.75e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 532 PWQIQETAPPSTWPHSGRVEF--RDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEII 609
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFpiRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 610 IDGVNiakigLHNL--------RFKITIIPQDPvlfSGSL--RMNLDPF-------------SQYSDEEVWMALELAHLK 666
Cdd:PRK15134 344 FDGQP-----LHNLnrrqllpvRHRIQVVFQDP---NSSLnpRLNVLQIieeglrvhqptlsAAQREQQVIAVMEEVGLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 667 gfvsalPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHR 744
Cdd:PRK15134 416 ------PETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHD 485
|
250 260
....*....|....*....|...
gi 1907116879 745 LNTIMDYT-RVIVLDKGEVRECG 766
Cdd:PRK15134 486 LHVVRALChQVIVLRQGEVVEQG 508
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
28-105 |
4.30e-13 |
|
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: 67.66 E-value: 4.30e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMgLLKNKTRILVTHGISYLPQV-DVIIVMSGGK 105
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLREL-AEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
566-762 |
4.32e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 68.73 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGVNIakiGLHNLRFKITIIPQDPVLFSgslrm 643
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLDPFsqysdEEVWMAlelAHLKGfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 723
Cdd:cd03213 96 TLTVR-----ETLMFA---AKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907116879 724 LIQSTIRtQFED--CTVLTIAHRLNTIMDYT--RVIVLDKGEV 762
Cdd:cd03213 149 QVMSLLR-RLADtgRTIICSIHQPSSEIFELfdKLLLLSQGRV 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
567-745 |
4.79e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLFSG 639
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 S--------LRMNLDPFSQYSDEEVWMALELAHLKGFVSalpDKLnHECAEGgenLSVGQRQLVCLARALLRKTKILVLD 711
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVK---DRL-HDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 1907116879 712 EATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 745
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
566-766 |
6.07e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.71 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLhNLRFKITIIPQDPVLFSGSLrMNL 645
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-GGGFNPELTGRENIYLNGRL-LGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPfsQYSDEEVWMALELAHLKGFVSaLPDKlnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 725
Cdd:cd03220 115 SR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907116879 726 QSTIRTQFEDC-TVLTIAHRLNTIMDY-TRVIVLDKGEVRECG 766
Cdd:cd03220 182 QRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
557-752 |
6.62e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 557 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIIIDG--------VNIAKIGLHNLRFKIT 628
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 629 IIPQDPVLFsgslrmnldPFSQYSDEEVWMALELAH----LKGFVSA------LPDKLNHECAEGGENLSVGQRQLVCLA 698
Cdd:PRK14258 92 MVHPKPNLF---------PMSVYDNVAYGVKIVGWRpkleIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 699 RALLRKTKILVLDEATAAVD----LETDNLIQS-TIRTQFEDCTVLTIAHRLNTIMDYT 752
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFT 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
567-718 |
6.86e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.28 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRINESAEGEIIIDGVNIAKIGLHnlRFKITIIPQDPVLFS----- 638
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLlaaIAGTLSPAFSASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 GSLRMNLDPFSQYSD--EEVWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:COG4136 95 ENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 1907116879 717 VD 718
Cdd:COG4136 164 LD 165
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
550-774 |
7.26e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.83 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 629
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDP--VLFSGSLRMNL--DPFSQYSDEEV--WMALELAHLKGfVSALPDKLNHecaeggeNLSVGQRQLVCLARALLR 703
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEETvaHRVSSALHMLG-LEELRDRVPH-------HLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 704 KTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTI---MDYtrVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpemADY--IYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
568-771 |
7.89e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 568 KHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvLFSGSLRMN 644
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 645 L-----DPFSQY----SDEEVWMALELAHLKgfVSALPDKLN---HEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 712
Cdd:PRK15079 117 IgeiiaEPLRTYhpklSRQEVKDRVKAMMLK--VGLLPNLINrypHE-------FSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 713 ATAAVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNT---IMDytRVIVLDKGEVRECGAPSEL 771
Cdd:PRK15079 188 PVSALDVSIQaqvvNLLQQLQREM--GLSLIFIAHDLAVvkhISD--RVLVMYLGHAVELGTYDEV 249
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
548-771 |
1.06e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.10 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 548 GRVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGVNIAkiGLHNL 623
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTL-LrmiaGLEDPTS---GEILIGGRDVT--DLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 624 RFKITIIPQDPVLF----------SGsLRMnldpfSQYSDEEV-----WMA--LELAHLkgfvsalpdkLNHECAEggen 686
Cdd:COG3839 74 DRNIAMVFQSYALYphmtvyeniaFP-LKL-----RKVPKAEIdrrvrEAAelLGLEDL----------LDRKPKQ---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 687 LSVGQRQLVCLARALLRKTKILVLDEATAAVD----LETdnliqstiRTQfedctvltIA---HRLNTIMDY-------- 751
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAE--------IKrlhRRLGTTTIYvthdqvea 197
|
250 260
....*....|....*....|....
gi 1907116879 752 ----TRVIVLDKGEVRECGAPSEL 771
Cdd:COG3839 198 mtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
557-730 |
1.10e-12 |
|
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: 67.38 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 557 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGVNIAKIglhnlrfkiTIIPQD 633
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLlrILaGLLR---PDSGEVRWNGTPLAEQ---------RDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 634 PVLFSG---------SLRMNLD---PFSQYSDEEVWMALELAHLKGFvSALPdklnheCAEggenLSVGQRQLVCLARAL 701
Cdd:TIGR01189 74 NILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLP------AAQ----LSAGQQRRLALARLW 142
|
170 180
....*....|....*....|....*....
gi 1907116879 702 LRKTKILVLDEATAAVDLETDNLIQSTIR 730
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
28-106 |
1.11e-12 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 67.90 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQVDVIIVM 101
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEV-------MELLRelnkeaGTTIVVVTHDPELAEYADRIIEL 213
|
....*
gi 1907116879 102 SGGKI 106
Cdd:cd03255 214 RDGKI 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
516-718 |
1.13e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 516 VAVERLKEYSETEKEAPWQIqeTAPPSTWPhsgRVEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL 595
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPR--PQAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 596 GLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSgslRMnLDPFSQYSDEEV---WmaleLAHLKgfvsaL 672
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW----LERLK-----M 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907116879 673 PDKLNHecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVD 718
Cdd:PRK10522 435 AHKLEL---EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
566-772 |
1.22e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 68.08 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL-RFKITIIPQDPVLFSG-SLRM 643
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLD--PFSQYSDEEVWMALELAH-----LKgfvsalpDKLNHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLK-------ERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 717 -----VDletdnLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:COG0410 167 lapliVE-----EIFEIIRRlNREGVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELL 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
569-774 |
1.69e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 569 HINVTIEGGEKVGIVGRTGAGKSSLtLGL---FRINESaeGEIIIDGVNiakiglHNL----RFKITIIPQDPVLFSG-S 640
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTL-LNLiagFLTPAS--GSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRMN----LDPFSQYSDEEVWMALELAHLKGfVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:PRK10771 88 VAQNiglgLNPGLKLNAAQREKLHAIARQMG-IEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 717 VD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK10771 160 LDpalrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLSG 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-129 |
2.01e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 67.81 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 21 IGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGISYLPQ- 94
Cdd:COG1121 137 IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREy 205
|
90 100 110
....*....|....*....|....*....|....*
gi 1907116879 95 VDVIIVMSGGKISEmGSYQELLDRDgafaEFLRTY 129
Cdd:COG1121 206 FDRVLLLNRGLVAH-GPPEEVLTPE----NLSRAY 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
570-780 |
2.03e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.48 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHnlRFKITIIPQDPVLF---------SGS 640
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFphmtveqniAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRMNLDPFSQYSDEEVWMaLELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 720
Cdd:PRK11607 116 LKQDKLPKAEIASRVNEM-LGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 721 TDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQRGIFYS 780
Cdd:PRK11607 184 LRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-106 |
2.07e-12 |
|
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: 66.09 E-value: 2.07e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDaHVGKHIFEKVVGPMGlLKNKTRILVTHGISYLPQVDVIIVMSGGKI 106
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERALNQAIAALK-AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
566-763 |
3.03e-12 |
|
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: 66.54 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRF---------KITIIPQdpVL 636
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYlpeerglypKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 FSGSLR-MNLDPFSQYSDEevWM-ALELAHLKGfvsalpDKLnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 714
Cdd:cd03269 93 YLAQLKgLKKEEARRRIDE--WLeRLELSEYAN------KRV--------EELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 715 AAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVR 763
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAV 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-105 |
3.10e-12 |
|
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: 66.34 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmglLKN--KTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK----LKAegKTIIIVTHDLDLLLELaDRVIVLED 209
|
..
gi 1907116879 104 GK 105
Cdd:cd03225 210 GK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
28-118 |
3.82e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.59 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVG-------KHIFEKVvgpmgllkNKTRILVTH------GISylpq 94
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLReemreelRRLQREL--------GITFIYVTHdqeealALA---- 203
|
90 100
....*....|....*....|....
gi 1907116879 95 vDVIIVMSGGKISEMGSYQELLDR 118
Cdd:COG3842 204 -DRIAVMNDGRIEQVGTPEEIYER 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-127 |
4.64e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 10 LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVTHGI 89
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI-EKTIVDIKDKADKTIITIAHRI 1419
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907116879 90 SYLPQVDVIIVM-----SGGKISEMGSYQELLD-RDGAFAEFLR 127
Cdd:PTZ00265 1420 ASIKRSDKIVVFnnpdrTGSFVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
27-116 |
5.07e-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: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHGISYLPQV-DVII 99
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILA-------LLRdiNRelglTIVLITHEMEVVKRIcDRVA 212
|
90
....*....|....*..
gi 1907116879 100 VMSGGKISEMGSYQELL 116
Cdd:cd03258 213 VMEKGEVVEEGTVEEVF 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
28-115 |
6.87e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.82 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKI 215
|
....*....
gi 1907116879 107 SEMGSYQEL 115
Cdd:PRK11432 216 MQIGSPQEL 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
566-773 |
6.92e-12 |
|
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: 66.03 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGVNIAKIGLHN-LRFKITIIPQDPVLFSG-S 640
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVKPDS---GKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRMNLDPF--SQYSDEEVWMA-----LELAHLkgfvSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:cd03218 92 VEENILAVleIRGLSKKEREEkleelLEEFHI----THLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 714 TAAVDLETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQ 773
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITdRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
566-772 |
7.00e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 645
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPFSQYSDEEVWMALELAHLKGFVSAL-PDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-- 722
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQid 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 723 --NLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 772
Cdd:PRK10253 182 llELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
567-771 |
7.19e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 66.21 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAK-------IGL---HNLRFK-ITIIpqDPV 635
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvqernVGFvfqHYALFRhMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 636 LFSgsLRM---NLDPFSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDE 712
Cdd:cd03296 96 AFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 713 ATAAVDLETDNLIQSTIRTQFEDCTVLTI--AHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 771
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
560-772 |
9.03e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 560 REDLDLVlKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGvniakiglHNLRF--------KITIIP 631
Cdd:PRK15112 23 RQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD--------HPLHFgdysyrsqRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 632 QDPV-----------LFSGSLRMNLDPFSQYSDEEVWMALELahlkgfVSALPDKLNHEcaegGENLSVGQRQLVCLARA 700
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQ------VGLLPDHASYY----PHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 701 LLRKTKILVLDEATAAVDLetdnliqsTIRTQFEDCTV-LTIAHRLNTI--------MDYT--RVIVLDKGEVRECGAPS 769
Cdd:PRK15112 164 LILRPKVIIADEALASLDM--------SMRSQLINLMLeLQEKQGISYIyvtqhlgmMKHIsdQVLVMHQGEVVERGSTA 235
|
...
gi 1907116879 770 ELL 772
Cdd:PRK15112 236 DVL 238
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-118 |
9.19e-12 |
|
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: 65.98 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHG---ISYLpqVDVI 98
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEI-------LNLLKdlreerGLTYLFVSHDlavVAHL--CDRV 209
|
90 100
....*....|....*....|
gi 1907116879 99 IVMSGGKISEMGSYQELLDR 118
Cdd:COG1124 210 AVMQNGRIVEELTVADLLAG 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-110 |
9.55e-12 |
|
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: 64.26 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 25 GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGG 104
Cdd:cd03247 96 GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI---FEVLKDKTLIWITHHLTGIEHMDKILFLENG 172
|
....*.
gi 1907116879 105 KISEMG 110
Cdd:cd03247 173 KIIMQG 178
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
566-766 |
1.16e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEgeiiidgVNIAkiglhNLRFKITIIPQDPVLFSgsLRM 643
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEMPRSGT-------LNIA-----GNHFDFSKTPSDKAIRE--LRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLD-PFSQYS-----------------------DEEVWMALELA---HLKGFVSALPdklnhecaeggENLSVGQRQLVC 696
Cdd:PRK11124 83 NVGmVFQQYNlwphltvqqnlieapcrvlglskDQALARAEKLLerlRLKPYADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 697 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECG 766
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
566-772 |
1.24e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAE---GEIIIDG---VNIAKIGLHNLRFKITIIPQDPVLF 637
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTirvGDITIDTarsLSQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 ----------SGSLRMNLDPfsqySDEEVWMALEL---AHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRK 704
Cdd:PRK11264 98 phrtvleniiEGPVIVKGEP----KEEATARARELlakVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 705 TKILVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
278-511 |
1.42e-11 |
|
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: 65.97 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 278 ALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVD---SMIPqvikMFMGS 354
Cdd:cd18543 47 ALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQrflAFGP----FLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 355 LFSVIGAVIIILLATP----IAAVIIPPLGLV-YFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF---- 425
Cdd:cd18543 123 LLTLVVGLVVMLVLSPplalVALASLPPLVLVaRRFRRRYFPASRRAQDQAGDLA-----TVVEESVTGIRVVKAFgrer 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 426 EEQERFIHQSD-LKVDENQKAyypSIVANRWLAVR-LECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYSLQitayLN 502
Cdd:cd18543 198 RELDRFEAAARrLRATRLRAA---RLRARFWPLLEaLPELGLAAVLALGGWLVA-NGSLTLGtLVAFS-AYLTM----LV 268
|
....*....
gi 1907116879 503 WLVRMSSEM 511
Cdd:cd18543 269 WPVRMLGWL 277
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
567-770 |
1.46e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLrfkITIIPQD-------PVLFSG 639
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 SLRMnldpfSQYSDEEvWMALELAHLKGFVS---ALPDKLNHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:PRK15056 100 VVMM-----GRYGHMG-WLRRAKKRDRQIVTaalARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 717 VDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGaPSE 770
Cdd:PRK15056 173 VDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTE 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
28-127 |
1.64e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVgKHIFEKVvgpMGLLKNK--TRILVTHGISYLPQVDV-IIVMSGG 104
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL-RHEVLKV---MQDLAEEgmTMVIVTHEIGFAEKVASrLIFIDKG 212
|
90 100
....*....|....*....|....*
gi 1907116879 105 KISEMGSYQELLDR--DGAFAEFLR 127
Cdd:PRK09493 213 RIAEDGDPQVLIKNppSQRLQEFLQ 237
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
566-774 |
1.74e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 66.32 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLfrinESA-EGEIIIDGVNiAKIGLHNLRFKITIIPQDPVLFS-- 638
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL-LriiaGL----ETPdSGRIVLNGRD-LFTNLPPRERRVGFVFQHYALFPhm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 --------GsLRMnLDPFSQYSDEEV--WmaLELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKIL 708
Cdd:COG1118 91 tvaeniafG-LRV-RPPSKAEIRARVeeL--LELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 709 VLDEATAAVD------LEtDNLIQSTIRTQFedcTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG1118 156 LLDEPFGALDakvrkeLR-RWLRRLHDELGG---TTVFVTHDQEEALELAdRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
28-124 |
2.09e-11 |
|
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: 67.24 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK------NKTRILVTHGISYLPQV-DVIIV 100
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILD-------LLRelqrerGTTVLLITHDLGVVAEIaDRVVV 215
|
90 100
....*....|....*....|....
gi 1907116879 101 MSGGKISEMGSYQELLDRDGAFAE 124
Cdd:COG1123 216 MDDGRIVEDGPPEEILAAPQALAA 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
28-110 |
2.60e-11 |
|
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: 64.06 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIV 100
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQI-------LDLLKklqeelGLTLLFITHDLGVVAKIaDRVAV 218
|
90
....*....|
gi 1907116879 101 MSGGKISEMG 110
Cdd:cd03257 219 MYAGKIVEEG 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
554-777 |
2.92e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 554 DYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGLHNLRFKITIIP 631
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 632 QDP---VLFSG-------SLRmNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHecaeggenlsvGQRQLVCLARAL 701
Cdd:PRK13638 84 QDPeqqIFYTDidsdiafSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 702 LRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAP------SELLQ 773
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISdAVYVLRQGQILTHGAPgevfacTEAME 231
|
....
gi 1907116879 774 QRGI 777
Cdd:PRK13638 232 QAGL 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
28-118 |
2.99e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 64.18 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKN--KTRILVTHGIS-YLPQVDVIIVMSGG 104
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL---KRLQKElgITFVFVTHDQEeALTMSDRIAVMNKG 207
|
90
....*....|....
gi 1907116879 105 KISEMGSYQELLDR 118
Cdd:cd03300 208 KIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
570-774 |
3.37e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG----LHNLRFKITIIPQDP--VLFSGSLRM 643
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NL----DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD- 718
Cdd:PRK13643 105 DVafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE-------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDp 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 719 ---LETDNLIQSTIRTqfeDCTVLTIAHRLNTIMDYTR-VIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13643 178 karIEMMQLFESIHQS---GQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSDVFQE 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
551-774 |
3.42e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 66.63 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 551 EFRDYCLRYREDLDL--VLKHINVTIEGGEKVGIVGRTGAGKS--SL-TLGLF-RINESAEGEIIIDGVNIAKIGLHNLR 624
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtALsILRLLpDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 625 ----FKITIIPQDPvlfsgslrMN-LDPF----SQ----------YSDEEVW-MALELAHLKGfvsaLPD---KLN---H 678
Cdd:COG4172 88 rirgNRIAMIFQEP--------MTsLNPLhtigKQiaevlrlhrgLSGAAARaRALELLERVG----IPDperRLDaypH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 679 EcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnliqsTIRTQF----------EDCTVLTIAHRLNTI 748
Cdd:COG4172 156 Q-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQAQIldllkdlqreLGMALLLITHDLGVV 220
|
250 260
....*....|....*....|....*..
gi 1907116879 749 MDYT-RVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG4172 221 RRFAdRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
559-757 |
3.51e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.58 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 559 YREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFS 638
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 GSLRMNLDPFSQYSDEEVWMALELAHLKGFvsALPDK-LNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 717
Cdd:PRK10247 95 DTVYDNLIFPWQIRNQQPDPAIFLDDLERF--ALPDTiLTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907116879 718 D----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVL 757
Cdd:PRK10247 169 DesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
28-118 |
3.54e-11 |
|
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: 66.47 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIV 100
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI-------LNLLRdlqrelGLTYLFISHDLAVVRYIaDRVAV 477
|
90
....*....|....*...
gi 1907116879 101 MSGGKISEMGSYQELLDR 118
Cdd:COG1123 478 MYDGRIVEDGPTEEVFAN 495
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
566-773 |
4.00e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.09 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLG---LFRINESA--EGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLF- 637
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 --------SGSLRMN-LDPFSQYSDEEVWMALELAhlkgfvsALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKIL 708
Cdd:PRK14267 99 hltiydnvAIGVKLNgLVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 709 VLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDYTRVIVLdkGEVRECGAPSELLQ 773
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVGPTRKVFE 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
566-773 |
4.58e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLH-NLRFKITIIPQDPVLFS------ 638
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 ---GSLRMNLDPFSQYSDEEVWMALELAHlkgfVSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATA 715
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFH----IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 716 AVD----LETDNLIQstiRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQ 773
Cdd:PRK10895 167 GVDpisvIDIKRIIE---HLRDSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-106 |
5.03e-11 |
|
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: 62.94 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 21 IGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGI-SYLPQ 94
Cdd:cd03235 130 IGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYE-------LLRelrreGMTILVVTHDLgLVLEY 198
|
90
....*....|..
gi 1907116879 95 VDVIIVMSGGKI 106
Cdd:cd03235 199 FDRVLLLNRTVV 210
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
278-520 |
5.45e-11 |
|
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: 64.10 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 278 ALGILQG--AAIFGYSMAvsiggiFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 355
Cdd:cd18572 48 LSGLFSGlrGGCFSYAGT------RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 356 FSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF--EEQE 429
Cdd:cd18572 122 VQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYY----RKLSKEIQDALAEANQVAEEALSNIRTVRSFatEERE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 430 --RFIHQSDLKVDENQK---AYypsiVANRWLAVRLECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNWL 504
Cdd:cd18572 198 arRYERALDKALKLSVRqalAY----AGYVAVNTLLQNGTQVLVLFYGGHLVLS-GRMSAGQLVTFMLYQQQLGEAFQSL 272
|
250
....*....|....*.
gi 1907116879 505 VRMSSEMETNIVAVER 520
Cdd:cd18572 273 GDVFSSLMQAVGAAEK 288
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-128 |
5.83e-11 |
|
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: 63.77 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 13 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVgKHIFEKVVgpMGLLKNKTRILVTHGISYL 92
Cdd:cd03288 142 LPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTI 218
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907116879 93 PQVDVIIVMSGGKISEMGSYQELL-DRDGAFAEFLRT 128
Cdd:cd03288 219 LDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
556-758 |
6.76e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 556 CLRyreDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGVNIAK-----------IG-- 619
Cdd:PRK13538 9 CER---DERILFSGLSFTLNAGELVQIEGPNGAGKTSLlrILaGLAR---PDAGEVLWQGEPIRRqrdeyhqdllyLGhq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 620 ---------LHNLRFkitiipqdpvlfsgSLRMNldpfSQYSDEEVWMALELAHLKGFVSALpdklnheCAeggeNLSVG 690
Cdd:PRK13538 83 pgikteltaLENLRF--------------YQRLH----GPGDDEALWEALAQVGLAGFEDVP-------VR----QLSAG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 691 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLD 758
Cdd:PRK13538 134 QQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
28-105 |
6.78e-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: 61.82 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKVVGPMGllknKTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVralLKSLQAQLG----ITVVLVTHDLDEAARLaDRVVVLRD 176
|
..
gi 1907116879 104 GK 105
Cdd:cd03229 177 GK 178
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
275-520 |
6.87e-11 |
|
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: 64.03 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 275 VYGALGILQGAAIFGYSMAVSIGG---IFASRRlhlDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF 351
Cdd:cd18545 45 LFLALNLVNWVASRLRIYLMAKVGqriLYDLRQ---DLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 352 MGSLFSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFyvasSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE 426
Cdd:cd18545 122 IPDLLTLVGIVIIMFslnvrLAL-VTLAVLPLLVLVVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 427 EQERFIHQSDLKVDENQKAYYPSIVANR--WLAVRL-ECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNW 503
Cdd:cd18545 197 REDENEEIFDELNRENRKANMRAVRLNAlfWPLVELiSALGTALVYWYGGKLVLG-GAITVGVLVAFIGYVGRFWQPIRN 275
|
250
....*....|....*..
gi 1907116879 504 LVRMSSEMETNIVAVER 520
Cdd:cd18545 276 LSNFYNQLQSAMASAER 292
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
567-775 |
7.92e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGVNIAKIG------------------LHNLRF 625
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVQREGrlardirksrantgyifqQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVsalpdklnHECAEGGENLSVGQRQLVCLARALLRKT 705
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMV--------HFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 706 KILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQR 775
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHVFYDGSSQQFDNER 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
565-773 |
8.26e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.89 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 565 LVLKHINVTIEGGEKVGIVGRTGAGKSSL----------TLGLFRINEsaegEIIIDGVNIAKigLHNLRFKITIIPQDP 634
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlngllqpTSGTVTIGE----RVITAGKKNKK--LKPLRKKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 635 --VLFSGSLR-------MNldpFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKT 705
Cdd:PRK13634 95 ehQLFEETVEkdicfgpMN---FGVSEEDAKQKAREMIELVGLPEELLARSPFE-------LSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 706 KILVLDEATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQ 773
Cdd:PRK13634 165 EVLVLDEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYAdQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
28-106 |
8.63e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 62.16 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKhifeKVVGPMGLL--KNKTRILVTHGISYLPQV-DVIIVMSGG 104
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG----EVLDVMKDLaeEGMTMVVVTHEMGFAREVaDRVIFMDDG 211
|
..
gi 1907116879 105 KI 106
Cdd:cd03262 212 RI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
28-108 |
1.10e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 62.80 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLK--NKTRILVTHGIS---YLpqVDVIIVMS 102
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDEL---LRLWQetGKTVLFVTHDVDeavFL--ADRVVVLS 213
|
....*...
gi 1907116879 103 G--GKISE 108
Cdd:COG1116 214 ArpGRIVE 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
566-773 |
1.11e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQD-PVLFSGSLRM- 643
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVREl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 ----------NLDPFSQYSDEEVWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:PRK10575 106 vaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 714 TAAVDL----ETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQ 773
Cdd:PRK10575 175 TSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCdYLVALRGGEMIAQGTPAELMR 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-87 |
1.14e-10 |
|
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: 64.69 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMgllKNK 80
Cdd:TIGR02868 445 LERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL---SGR 521
|
....*..
gi 1907116879 81 TRILVTH 87
Cdd:TIGR02868 522 TVVLITH 528
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
28-108 |
1.21e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 61.98 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK------NKTRILVTHGISYLPQVDVIIVM 101
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRL 217
|
....*..
gi 1907116879 102 SGGKISE 108
Cdd:COG1136 218 RDGRIVS 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-116 |
1.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKI 106
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
90
....*....|
gi 1907116879 107 SEMGSYQELL 116
Cdd:PRK13632 221 IAQGKPKEIL 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-106 |
1.32e-10 |
|
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: 60.91 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 23 EKGVN-LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpMGLLKNKTRILVTHGISYLPQV-DVIIV 100
Cdd:cd03214 92 DRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR-LARERGKTVVMVLHDLNLAARYaDRVIL 170
|
....*.
gi 1907116879 101 MSGGKI 106
Cdd:cd03214 171 LKDGRI 176
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
28-117 |
1.37e-10 |
|
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: 62.36 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELrrwLRRLHDELHV----TTVFVTHDQEEALEVaDRVVVMNK 212
|
90
....*....|....
gi 1907116879 104 GKISEMGSYQELLD 117
Cdd:cd03296 213 GRIEQVGTPDEVYD 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
566-762 |
1.44e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdgvniAKIGLHNLRFKITIIPQDPVLF-------- 637
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMFQDARLLpwkkvidn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 -SGSLRMNLDPFSQYSDEEVwmalelahlkgfvsALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:PRK11247 102 vGLGLKGQWRDAALQALAAV--------------GLADRANEWPAA----LSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 717 VD----LETDNLIQSTIRTQ-FedcTVLTIAHRLN---TIMDytRVIVLDKGEV 762
Cdd:PRK11247 164 LDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKI 212
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
276-447 |
1.65e-10 |
|
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: 62.88 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 276 YGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 355
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 356 FSVIGAVII----------ILLATpiaaviIPPLGLVYFFVQRFYV-ASSRQLKRLESVSrspvySHFNETLLGVSVIRA 424
Cdd:cd18577 133 STFIAGFIIafiyswkltlVLLAT------LPLIAIVGGIMGKLLSkYTKKEQEAYAKAG-----SIAEEALSSIRTVKA 201
|
170 180
....*....|....*....|...
gi 1907116879 425 FEEQERFIHQSDLKVDENQKAYY 447
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGI 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
570-779 |
1.78e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---VNIAKIGLHNLRF-KITIIPQDPVlfsgslr 642
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAfalMGLLAANGRIGGSATFNGreiLNLPEKELNKLRAeQISMIFQDPM------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 MNLDPFSQYSDE--EVWM-------------------ALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARAL 701
Cdd:PRK09473 108 TSLNPYMRVGEQlmEVLMlhkgmskaeafeesvrmldAVKMPEARKRMKMYP----HE-------FSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 702 LRKTKILVLDEATAAVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIVLDKGEVRECGapsell 772
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVvagICD--KVLVMYAGRTMEYG------ 244
|
....*..
gi 1907116879 773 QQRGIFY 779
Cdd:PRK09473 245 NARDVFY 251
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
520-764 |
1.90e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 520 RLKEYSETEKEAPWQIQETA----PPStwPHSGR--VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSl 593
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTVeirfPPP--ERLGKkvLELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 594 tlgLFRI----NESAEGEIiidgvniaKIGlHNLrfKITIIPQDPVLFSGSLRMnLDPFSQYSDEevwmaLELAHLKGFV 669
Cdd:COG0488 357 ---LLKLlageLEPDSGTV--------KLG-ETV--KIGYFDQHQEELDPDKTV-LDELRDGAPG-----GTEQEVRGYL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 670 SAL---PDKLNHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETdnliqstiRTQFEDC------TVLT 740
Cdd:COG0488 417 GRFlfsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLL 484
|
250 260
....*....|....*....|....*..
gi 1907116879 741 IAH-R--LNTIMDytRVIVLDKGEVRE 764
Cdd:COG0488 485 VSHdRyfLDRVAT--RILEFEDGGVRE 509
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
28-116 |
1.92e-10 |
|
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: 61.93 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIDEAFRLaDRIAIMKNGEI 214
|
90
....*....|
gi 1907116879 107 SEMGSYQELL 116
Cdd:cd03295 215 VQVGTPDEIL 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
27-120 |
1.93e-10 |
|
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: 61.80 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVvgpMGLLKN--KTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:COG4555 132 ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARRLLREI---LRALKKegKTVLFSSHIMQEVEALcDRVVILHK 207
|
90
....*....|....*..
gi 1907116879 104 GKISEMGSYQELLDRDG 120
Cdd:COG4555 208 GKVVAQGSLDELREEIG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
567-749 |
2.22e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGvniAKIGLHNLR----FKITIIPQDPVL---- 636
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEG---EELQASNIRdterAGIAIIHQELALvkel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 ------FSGSL-----RMNLDpfSQYSDEEVWMAlELahlkgfvsalpdKLNHECAEGGENLSVGQRQLVCLARALLRKT 705
Cdd:PRK13549 98 svleniFLGNEitpggIMDYD--AMYLRAQKLLA-QL------------KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907116879 706 KILVLDEATAAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM 749
Cdd:PRK13549 163 RLLILDEPTASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
28-110 |
2.28e-10 |
|
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: 61.12 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKnKTRILVTHG-ISYLPQVDVIIVMSGGKI 106
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLG-TTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
....
gi 1907116879 107 SEMG 110
Cdd:cd03301 210 QQIG 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
567-774 |
2.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI-AKIG---LHNLRFKITIIPQDP--VLFSGS 640
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 L-----------RMNLDPFSQYSDEevwMALELAHLKGFVSALPDKlnhecaeggenLSVGQRQLVCLARALLRKTKILV 709
Cdd:PRK13646 103 VereiifgpknfKMNLDEVKNYAHR---LLMDLGFSRDVMSQSPFQ-----------MSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 710 LDEATAAVDLETDNLIQSTIRT-QFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYAdEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
28-116 |
2.46e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH-VGkhifeKVVGPMGLL--KNKTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElVG-----EVLNTIRQLaqEKRTMVIVTHEMSFARDVaDRAIFMDQ 219
|
90
....*....|...
gi 1907116879 104 GKISEMGSYQELL 116
Cdd:PRK11264 220 GRIVEQGPAKALF 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
520-774 |
2.52e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 520 RLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFR 599
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 600 INESAEGEIIIDGVNI-AKIGLhnLRFKITIIPQ-DPVLFSGSLRMNLDPFSQY-------SDEEVWMALELAHLKgfvs 670
Cdd:PRK13536 90 MTSPDAGKITVLGVPVpARARL--ARARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARLE---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 671 alpDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF-EDCTVLTIAHrlntIM 749
Cdd:PRK13536 164 ---SKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FM 232
|
250 260 270
....*....|....*....|....*....|
gi 1907116879 750 DYT-----RVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13536 233 EEAerlcdRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-115 |
2.53e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.79 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKNkTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKF-TSVFVTHDQEEAMEVaDRVVVMSQGNI 215
|
....*....
gi 1907116879 107 SEMGSYQEL 115
Cdd:PRK10851 216 EQAGTPDQV 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
560-774 |
2.74e-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: 62.81 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 560 REDLDLvlkHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRineSAEGEIIIDG---VNIAKigLHNL---RFKITI 629
Cdd:COG4148 11 RGGFTL---DVDFTLPGRGVTALFGPSGSGKTTL-LraiaGLER---PDSGRIRLGGevlQDSAR--GIFLpphRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQDPVLFSG-SLRMNLD--------PFSQYSDEEVWMALELAHLkgfvsalpdkLNHecaeGGENLSVGQRQLVCLARA 700
Cdd:COG4148 82 VFQEARLFPHlSVRGNLLygrkraprAERRISFDEVVELLGIGHL----------LDR----RPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 701 LLRKTKILVLDEATAAVDLETDNLIQ---STIRTQFeDCTVLTIAHRLNTIM---DytRVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVArlaD--HVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-126 |
4.01e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 60.81 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhvgkHIFEKVVGPMGLLKNK---TRILVTHGIS-YLPQVDVIIVMSG 103
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDV----RTKEKLREELKKIRKEfgvTVLHVTHDFEeAWALADKVAIMLN 205
|
90 100
....*....|....*....|....*
gi 1907116879 104 GKISEMGSYQELLDR--DGAFAEFL 126
Cdd:cd03299 206 GKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
570-774 |
4.01e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.68 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG----LHNLRFKITIIPQDP--VLFSGSLRM 643
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPesQLFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NL----DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 719
Cdd:PRK13649 106 DVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFE-------LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 720 ETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK13649 179 KGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
275-485 |
4.40e-10 |
|
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: 61.35 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 275 VYGALGILQGAAIFGYsmAVSIGGIFASRRLHLDLLYN--------VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQ 346
Cdd:cd18546 38 LLLAAAAYLAVVLAGW--VAQRAQTRLTGRTGERLLYDlrlrvfahLQRLSLDFHERETSGRIMTRMTSDIDALSELLQT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 347 VIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRfyvASSRQLKRL-ESVSRspVYSHFNETLLGVSV 421
Cdd:cd18546 116 GLVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRWFRR---RSSRAYRRArERIAA--VNADLQETLAGIRV 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 422 IRAF----EEQERFIHQSDLKVDENQKA------YYPSIvanRWLAVrlecVGNCIVLFAALFAVIsRHSLSAG 485
Cdd:cd18546 191 VQAFrrerRNAERFAELSDDYRDARLRAqrlvaiYFPGV---ELLGN----LATAAVLLVGAWRVA-AGTLTVG 256
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
28-118 |
4.40e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 60.78 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH-VGkhifEkVVGPMGLLKNK--TRILVTHGISYLPQV-DVIIVMSG 103
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElVG----E-VLDVMRDLAKEgmTMVVVTHEMGFAREVaDRVVFMDG 211
|
90
....*....|....*
gi 1907116879 104 GKISEMGSYQELLDR 118
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
27-118 |
4.50e-10 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 60.46 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHgisYLPQV----DV 97
Cdd:COG1131 131 TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWE-------LLRelaaeGKTVLLSTH---YLEEAerlcDR 200
|
90 100
....*....|....*....|.
gi 1907116879 98 IIVMSGGKISEMGSYQELLDR 118
Cdd:COG1131 201 VAIIDKGRIVADGTPDELKAR 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
566-757 |
4.57e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.55 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVniAKIGLhnLRFKITIIPQDPVLFSGSLRMNL 645
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 ----DPFSQYSDE---EVWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 718
Cdd:NF040873 83 warrGLWRRLTRDdraAVDDALERVGLADL-------AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907116879 719 LETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVL 757
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
28-106 |
4.61e-10 |
|
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: 60.18 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvgpmgLLK-----NKTRILVTHGIS---YLPqvDVII 99
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE------LLDiwretGKTVLLVTHDIDeavFLA--DRVV 203
|
....*....
gi 1907116879 100 VMSG--GKI 106
Cdd:cd03293 204 VLSArpGRI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-116 |
4.93e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.75 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 17 DRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH-VGK--HIFEKVVGpmgllKNKTRILVTHGISYLP 93
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGFAR 216
|
90 100
....*....|....*....|....
gi 1907116879 94 QVDV-IIVMSGGKISEMGSYQELL 116
Cdd:PRK10619 217 HVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
27-124 |
5.17e-10 |
|
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: 60.42 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGISYLPQV-DVIIV 100
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE-------LLKrlnkeGKTVIIVTHDLDLVAELaDRVIV 206
|
90 100
....*....|....*....|....
gi 1907116879 101 MSGGKISEMGSYQELLDRDGAFAE 124
Cdd:COG1122 207 LDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
566-774 |
5.55e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.46 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGVNIAKIGLHNlRFK--ITIIPQDPVLFSGsl 641
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 642 rmnldpfsqysdeevwmaLELAHLKGFVsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 721
Cdd:cd03217 92 ------------------VKNADFLRYV--------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 722 DNLIQSTIRT-QFEDCTVLTIAHRLNtIMDY---TRVIVLDKGEVRECGaPSELLQQ 774
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
550-773 |
5.56e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGlHNLRFKITI 629
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQ----DPVLfsgSLRMNLDPFSQY-------SDEEVWMALELAHLKgfvsalpdklNHECAEGGEnLSVGQRQLVCLA 698
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLE----------NKADAKVGE-LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 699 RALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAH------RLntimdYTRVIVLDKGEVRECGAPSEL 771
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 1907116879 772 LQ 773
Cdd:PRK13537 226 IE 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
564-731 |
5.95e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 564 DLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGVNiakIGLHNLRFKITII-PQD---PVL 636
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrLIaGLLPP---AAGTIKLDGGD---IDDPDVAEACHYLgHRNamkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 fsgSLRMNLDPFSQY---SDEEVWMALE------LAHLKgfvsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKI 707
Cdd:PRK13539 89 ---TVAENLEFWAAFlggEELDIAAALEavglapLAHLP-----------------FGYLSAGQKRRVALARLLVSNRPI 148
|
170 180
....*....|....*....|....
gi 1907116879 708 LVLDEATAAVDLETDNLIQSTIRT 731
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRA 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
566-762 |
6.14e-10 |
|
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: 60.42 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV--------NIAKIGLHnLRFKITIIPQDPVLf 637
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 sGSLRMNLD----PFSQYSdeevwmalelAHLKGFVSALpdKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:cd03267 114 -DSFYLLAAiydlPPARFK----------KRLDELSELL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 714 TAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDY-TRVIVLDKGEV 762
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
27-111 |
6.50e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.63 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHgisylpQVDVI-- 98
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILD-------LLKdiNRelglTIVLITH------EMDVVrr 206
|
90
....*....|....*...
gi 1907116879 99 I-----VMSGGKISEMGS 111
Cdd:COG1135 207 IcdrvaVLENGRIVEQGP 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
570-774 |
6.69e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII----DGVNIAKIGLHNL-RFK--ITIIPQDPVLFSGslR 642
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRgRAKryIGILHQEYDLYPH--R 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 MNLDPFSQYSDEEvwMALELAHLK--------GF-----VSALpDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 709
Cdd:TIGR03269 381 TVLDNLTEAIGLE--LPDELARMKavitlkmvGFdeekaEEIL-DKYPDE-------LSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907116879 710 LDEATAAVDLETDNLIQSTI---RTQFEDcTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 774
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVCdRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-106 |
7.50e-10 |
|
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: 59.62 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVgKHIFEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDRAL-RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRL 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
577-766 |
7.77e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 577 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPVlfsgslrMNLDPFSQ--Y 651
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 652 SDEEVWM----------ALELAHLKGFVSALPD---KLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 718
Cdd:PRK10261 423 SIMEPLRvhgllpgkaaAARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 719 LETDNLIQSTIRTQFEDCTV--LTIAHRLNTIMDYT-RVIVLDKGEVRECG 766
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
565-752 |
7.88e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 565 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLF 637
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 SGSLRMNL------DPFSQYSDEEVWMALELAHLKGFVSalpDKLNhecaEGGENLSVGQRQLVCLARALLRKTKILVLD 711
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907116879 712 EATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYT 752
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMT 220
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
235-505 |
7.96e-10 |
|
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: 60.89 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 235 IFLFLCNhVSALASNYWLSLWTDDppVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGifASRRLHLDL---LY 311
Cdd:cd18541 6 LFLILVD-LLQLLIPRIIGRAIDA--LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFG--ASRRIEYDLrndLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 312 N-VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP---IAAVIIPPL--GLVYFF 385
Cdd:cd18541 81 AhLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPkltLIALLPLPLlaLLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 386 VQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQK------AYYPSIVanrw 455
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLS-----DRVQESFSGIRVIKAFvqeeAEIERFDKLNEEYVEKNLRlarvdaLFFPLIG---- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 456 LAVRLecvGNCIVLFAALFAVIsRHSLSAG-LVglsvsyslQITAYLNWLV 505
Cdd:cd18541 232 LLIGL---SFLIVLWYGGRLVI-RGTITLGdLV--------AFNSYLGMLI 270
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
566-752 |
8.44e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidgvniakiglHNLRFKITIIPQ----DPVL-FSGS 640
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRMNLDPFSQYSDeeVWMALELAHLKGFVSALPDKLNhecaeGGENlsvgqrQLVCLARALLRKTKILVLDEATAAVD-- 718
Cdd:PRK09544 88 RFLRLRPGTKKED--ILPALKRVQAGHLIDAPMQKLS-----GGET------QRVLLARALLNRPQLLVLDEPTQGVDvn 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907116879 719 --LETDNLIQStIRTQFeDCTVLTIAHRLNTIMDYT 752
Cdd:PRK09544 155 gqVALYDLIDQ-LRREL-DCAVLMVSHDLHLVMAKT 188
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
28-127 |
1.18e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFE--KVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGG 104
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEiiRELSQTGI----TQVIVTHEVEFARKVaSQVVYMEKG 217
|
90 100
....*....|....*....|....*
gi 1907116879 105 KISEMGSyQELLD--RDGAFAEFLR 127
Cdd:COG4161 218 RIIEQGD-ASHFTqpQTEAFAHYLS 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
566-774 |
1.27e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGlfRINESAEGEIIIDGvNIAKI-----GLH-------NLRFKITII- 630
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlkLIA--GILEPTSGRVEVNG-RVSALlelgaGFHpeltgreNIYLNGRLLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 631 --PQDP-------VLFSGsLRMNLD-PFSQYSDEevwMALELA-----HLKgfvsalPDklnhecaeggenlsvgqrqlv 695
Cdd:COG1134 118 lsRKEIdekfdeiVEFAE-LGDFIDqPVKTYSSG---MRARLAfavatAVD------PD--------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 696 clarallrktkILVLDEATAAVDLE----TDNLIQSTIRtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSE 770
Cdd:COG1134 167 -----------ILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
....
gi 1907116879 771 LLQQ 774
Cdd:COG1134 233 VIAA 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
566-773 |
1.46e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLF--RINESAE-------GEIIIDGVNIAKIGLHNLRFKITIIPQ--DP 634
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTL-LKALagDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 635 VL-FSGSLRMNLDPF---------SQYSDEEVWMALELAHLKGFVsalpdklnhecAEGGENLSVGQRQLVCLARAL--- 701
Cdd:PRK13547 95 AFaFSAREIVLLGRYpharragalTHRDGEIAWQALALAGATALV-----------GRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 702 ------LRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHAdRIAMLADGAIVAHGAPADVL 243
|
.
gi 1907116879 773 Q 773
Cdd:PRK13547 244 T 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
577-763 |
1.50e-09 |
|
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: 58.85 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 577 GEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGVNI----AKIGLHNLRFKITIIPQDPVLFSG-SLRMNL--- 645
Cdd:cd03297 23 EEVTGIFGASGAGKSTLlrcIAGLEKPDG---GTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLafg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 -----DPFSQYSDEEVWMALELAHLKGfvsALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 720
Cdd:cd03297 100 lkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907116879 721 TDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVR 763
Cdd:cd03297 166 LRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLAdRIVVMEDGRLQ 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
566-718 |
1.55e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.73 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGVNIAKIGLH----NLRFK-------ITIIpqD 633
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV-LRLIAGFETPdSGRIMLDGQDITHVPAEnrhvNTVFQsyalfphMTVF--E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 634 PVLFSgsLRMNLDPFSQYsDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:PRK09452 106 NVAFG--LRMQKTPAAEI-TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
....*
gi 1907116879 714 TAAVD 718
Cdd:PRK09452 172 LSALD 176
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
28-115 |
1.65e-09 |
|
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: 58.73 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVgpMGLLKNKTRILVTHGisyLPQV----DVIIVMSG 103
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDP-ISTAKIEELI--AELKKEYTIVIVTHN---MQQAarvaDRTAFLLN 215
|
90
....*....|..
gi 1907116879 104 GKISEMGSYQEL 115
Cdd:cd03260 216 GRLVEFGPTEQI 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
566-774 |
2.06e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.21 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA-------------KIGLHNLRFKITIIPQ 632
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 633 DPVLFSgslRMNLDPFSQYSDEEVwMALELAHLKGFVSALPDKLNHECAEGGE---NLSVGQRQLVCLARALLRKTKILV 709
Cdd:PRK10619 100 HFNLWS---HMTVLENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 710 LDEATAAVDLEtdnLIQSTIRTQF----EDCTVLTIAHRlntiMDYTR-----VIVLDKGEVRECGAPSELLQQ 774
Cdd:PRK10619 176 FDEPTSALDPE---LVGEVLRIMQqlaeEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
568-762 |
2.27e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 568 KHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN-LRFKITIIPQD---PVLF-SGSLR 642
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqsSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 MNLDPFSqYSDEEVWM--ALELAHLKGFVSALPDKLNHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 720
Cdd:PRK15439 360 WNVCALT-HNRRGFWIkpARENAVLERYRRALNIKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907116879 721 TDNLIQSTIRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGEV 762
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEI 481
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
26-106 |
2.46e-09 |
|
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: 57.02 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 26 VNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGISYLPQV-DVII 99
Cdd:cd03230 94 LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE-------LLRelkkeGKTILLSSHILEEAERLcDRVA 166
|
....*..
gi 1907116879 100 VMSGGKI 106
Cdd:cd03230 167 ILNNGRI 173
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
573-750 |
2.48e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 573 TIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA---KIGLHNLRFKITIIPQDPVlfsGS--------- 640
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY---GSlnprkkvgq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 -----LRMNLDPFSQYSDEEVWMALELAHLKgfvsalP---DKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 712
Cdd:PRK11308 114 ileepLLINTSLSAAERREKALAMMAKVGLR------PehyDRYPHM-------FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907116879 713 ATAAVDLetdnliqsTIRTQFedctvltiahrLNTIMD 750
Cdd:PRK11308 181 PVSALDV--------SVQAQV-----------LNLMMD 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
550-766 |
2.70e-09 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 58.04 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV----------NIAKI- 618
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrDIAMVf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 619 ----------GLHNLRF--KITIIPQDPVlfsgslrmnldpfsqysDEEVWMALELAHLKGFVSALPDKlnhecaeggen 686
Cdd:cd03301 79 qnyalyphmtVYDNIAFglKLRKVPKDEI-----------------DERVREVAELLQIEHLLDRKPKQ----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 687 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRTQFEdctvlTIAHRLNTIMDY------------TRV 754
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA----KLRVQMRAELK-----RLQQRLGTTTIYvthdqveamtmaDRI 201
|
250
....*....|..
gi 1907116879 755 IVLDKGEVRECG 766
Cdd:cd03301 202 AVMNDGQIQQIG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-119 |
2.79e-09 |
|
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: 58.28 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKI 215
|
90
....*....|...
gi 1907116879 107 SEMGSYQELLDRD 119
Cdd:cd03261 216 VAEGTPEELRASD 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
567-775 |
3.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.07 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI----AKIGLHNLRFKITIIPQDP--VLFSGS 640
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRMNLD--P--FSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:PRK13641 103 VLKDVEfgPknFGFSEDEAKEKALKWLKKVGLSEDLISKSPFE-------LSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 717 VDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTR-VIVLDKGEVRECGAPSELLQQR 775
Cdd:PRK13641 176 LDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
563-762 |
3.16e-09 |
|
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: 57.06 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 563 LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN-LRFKITIIPQDPvlfsgsL 641
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDR------K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 642 RMNLdpFSQYSdeeVWMALELAHLkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 721
Cdd:cd03215 86 REGL--VLDLS---VAENIALSSL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907116879 722 DNLIQSTIRTQFED-CTVLTIAHRLNTIM---DytRVIVLDKGEV 762
Cdd:cd03215 140 KAEIYRLIRELADAgKAVLLISSELDELLglcD--RILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
566-745 |
3.45e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-----EIIIDGVNIAKI-GLHNLRFKITIIPQDPVLFSG 639
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 SLRMN---------LDPFSQYSDEEVWMALELahlkGFVSALPDKLnhecAEGGENLSVGQRQLVCLARALLRKTKILVL 710
Cdd:PRK14271 116 SIMDNvlagvrahkLVPRKEFRGVAQARLTEV----GLWDAVKDRL----SDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190
....*....|....*....|....*....|....*
gi 1907116879 711 DEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 745
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
27-114 |
3.69e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.58 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHifekvvgpMGL-LK------NKTRILVTHGI-SYLPQVDVI 98
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ--------MQNeLKalqrklGITFVFVTHDQeEALTMSDRI 215
|
90
....*....|....*.
gi 1907116879 99 IVMSGGKISEMGSYQE 114
Cdd:PRK09452 216 VVMRDGRIEQDGTPRE 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-150 |
4.35e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 1 MEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpmGLLKNK 80
Cdd:PRK10790 450 LETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA---AVREHT 526
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 81 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGafaeflRTYANAEQDLASEDDSVSGSGKES 150
Cdd:PRK10790 527 TLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG------RYWQMYQLQLAGEELAASVREEES 590
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
27-111 |
4.54e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.04 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHgisylpQVDVI-- 98
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdiNRelglTIVLITH------EMDVVkr 206
|
90
....*....|....*...
gi 1907116879 99 -----IVMSGGKISEMGS 111
Cdd:PRK11153 207 icdrvAVIDAGRLVEQGT 224
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
280-507 |
5.33e-09 |
|
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: 58.18 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 280 GILQGAAIFGYSMAVsIGGIFAS-------RRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFM 352
Cdd:cd18548 43 LLMLLLALLGLIAGI-LAGYFAAkasqgfgRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 353 GSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRF-YVASSRQLKRLESVSRSpvyshFNETLLGVSVIRAF-- 425
Cdd:cd18548 122 RAPIMLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKaIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFnr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 426 --EEQERFIhqsdlkvDENQKAYYPSIVANRWLAVR---LECVGN----CIVLFAALFavISRHSLSAG-LVGLsVSYSL 495
Cdd:cd18548 197 edYEEERFD-------KANDDLTDTSLKAGRLMALLnplMMLIMNlaivAILWFGGHL--INAGSLQVGdLVAF-INYLM 266
|
250
....*....|..
gi 1907116879 496 QITAYLNWLVRM 507
Cdd:cd18548 267 QILMSLMMLSMV 278
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
261-485 |
5.35e-09 |
|
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: 58.21 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 261 VVNGTQANRNFRLSVYGALGILQGAAIFG----YSMAVSigGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKE 336
Cdd:cd18551 25 LIDALSAGGSSGGLLALLVALFLLQAVLSalssYLLGRT--GERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTND 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 337 LDTVDSMIPQVIKMFMGSLFSVIGAVI-----------IILLATPIAAVIIPPLGlvyffvQRFYVASSRQLKRLESVSr 405
Cdd:cd18551 103 TTLLRELITSGLPQLVTGVLTVVGAVVlmflldwvltlVTLAVVPLAFLIILPLG------RRIRKASKRAQDALGELS- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 406 spvySHFNETLLGVSVIRAF--EEQErfihqSDLKVDENQKAYYPSIVANRWLAVrLECVGNcIVLFAALFAVI------ 477
Cdd:cd18551 176 ----AALERALSAIRTVKASnaEERE-----TKRGGEAAERLYRAGLKAAKIEAL-IGPLMG-LAVQLALLVVLgvggar 244
|
....*....
gi 1907116879 478 -SRHSLSAG 485
Cdd:cd18551 245 vASGALTVG 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-124 |
6.21e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.72 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKhifEKVVGPMGLLKNKTRILV---THGISYLPQVDVIIVMSGG 104
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKG 216
|
90 100
....*....|....*....|
gi 1907116879 105 KISEMGSYQELLDRDGAFAE 124
Cdd:PRK13635 217 EILEEGTPEEIFKSGHMLQE 236
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
279-521 |
7.48e-09 |
|
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: 57.91 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 279 LGILQGAAIFGYS---MAVSIGGIFASRrLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 355
Cdd:cd18564 61 VGIALLRGLASYAgtyLTALVGQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 356 FSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF----E 426
Cdd:cd18564 140 LTLVGMLGVMFwldwqLAL-IALAVAPLLLLAARRFSRRIKEASREQRRREGA----LASVAQESLSAIRVVQAFgreeH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 427 EQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGlvGLSVsyslqITAYLNWL-- 504
Cdd:cd18564 215 EERRFARENRKSLRAGLRAARLQALLSPVVDV-LVAVGTALVLWFGAWLVL-AGRLTPG--DLLV-----FLAYLKNLyk 285
|
250 260
....*....|....*....|..
gi 1907116879 505 -VRMSSEMETNI----VAVERL 521
Cdd:cd18564 286 pVRDLAKLTGRIakasASAERV 307
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-116 |
8.27e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 57.27 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKnKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDLDEALRLgDRIAIMKDGRL 239
|
90
....*....|
gi 1907116879 107 SEMGSYQELL 116
Cdd:cd03294 240 VQVGTPEEIL 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-118 |
8.35e-09 |
|
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: 58.19 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKvvgpmglLKNKTRI---LVTHGisyLPQV----D 96
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIlpyLER-------LRDELDIpilYVSHS---LDEVarlaD 202
|
90 100
....*....|....*....|..
gi 1907116879 97 VIIVMSGGKISEMGSYQELLDR 118
Cdd:COG4148 203 HVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
225-520 |
8.47e-09 |
|
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: 57.52 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 225 AIGLFITFLSIFLflcnhvsALASNYWLSLWTDDppVVNGTQANRNFRLsVYGALGILQGAAIFGYSMAVSIG--GIFAS 302
Cdd:cd18563 2 ILGFLLMLLGTAL-------GLVPPYLTKILIDD--VLIQLGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGrlLARLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 303 RRLHLDL---LYNVL-RSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIIL-----LAtpiAA 373
Cdd:cd18563 72 ERITADLrrdLYEHLqRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFslnwkLA---LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 374 VIIP-PL--GLVYFFVQRFYVASSRQLKRlesvsRSPVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA- 445
Cdd:cd18563 149 VLIPvPLvvWGSYFFWKKIRRLFHRQWRR-----WSRLNSVLNDTLPGIRVVKAFgqekREIKRFDEANQELLDANIRAe 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 446 -----YYPSIVAnrwlavrLECVGNCIVLFAALFAVISRHsLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVER 520
Cdd:cd18563 224 klwatFFPLLTF-------LTSLGTLIVWYFGGRQVLSGT-MTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-106 |
9.23e-09 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 56.11 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH----VGKhIFEKVVGpmgllKNKTRILVTHGISYLPQV-DVIIVMS 102
Cdd:cd03226 127 LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLA 200
|
....
gi 1907116879 103 GGKI 106
Cdd:cd03226 201 NGAI 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
557-771 |
9.59e-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: 56.61 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 557 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKiGLHNLRFKITIIPQDPVL 636
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 fsgslrmnldpfsqysDEEV--WMALEL-AHLKGFVSALPDKLNHECAEGGE----------NLSVGQRQLVCLARALLR 703
Cdd:cd03265 85 ----------------DDELtgWENLYIhARLYGVPGAERRERIDELLDFVGlleaadrlvkTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 704 KTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRL---NTIMDytRVIVLDKGEVRECGAPSEL 771
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMeeaEQLCD--RVAIIDHGRIIAEGTPEEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
566-721 |
1.03e-08 |
|
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: 56.67 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGVNIAKI---GLHNLRF-KITIIPQDPVLFsGS 640
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPtSGTVRLAGQDLFALdedARARLRArHVGFVFQSFQLL-PT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRMnLdpfsqysdEEVWMALELA-HLKGFVSA--------LPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLD 711
Cdd:COG4181 105 LTA-L--------ENVMLPLELAgRRDARARArallervgLGHRLDHYPAQ----LSGGEQQRVALARAFATEPAILFAD 171
|
170
....*....|
gi 1907116879 712 EATAAVDLET 721
Cdd:COG4181 172 EPTGNLDAAT 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
566-757 |
1.15e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.96 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 645
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 646 DPFSQY-SDEEVWMALELAHLKGFVSALpdklnheCAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 724
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGFEDRP-------VAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1907116879 725 IQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVL 757
Cdd:cd03231 164 FAEAMAGHCARggMVVLTTHQDLGLSEAGARELDL 198
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-116 |
1.22e-08 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 56.67 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKhifEKVVGPMGLLK---NKTRILVTHGISYLPQVDVIIVMSG 103
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDP-KGR---KEVLETIRKLNkeeGITVISITHDMEEAVLADRVIVMNK 211
|
90
....*....|...
gi 1907116879 104 GKISEMGSYQELL 116
Cdd:TIGR04520 212 GKIVAEGTPREIF 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-118 |
1.23e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.55 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 10 LEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhvgkhifeKVVGPMGL-LK------NKTR 82
Cdd:PRK11650 122 LELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA--------KLRVQMRLeIQrlhrrlKTTS 188
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907116879 83 ILVTHGisylpQV------DVIIVMSGGKISEMGSYQELLDR 118
Cdd:PRK11650 189 LYVTHD-----QVeamtlaDRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-117 |
1.87e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.30 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 107
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVY 221
|
90
....*....|
gi 1907116879 108 EMGSYQELLD 117
Cdd:PRK13648 222 KEGTPTEIFD 231
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
275-520 |
1.92e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 56.72 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 275 VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 354
Cdd:cd18540 47 LYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 355 LFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF--EEQ 428
Cdd:cd18540 127 ITYMIGILIVMLILNWklalIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKTLvrEEK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 429 erfiHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLV---GLSV--SYSLQITAYLNW 503
Cdd:cd18540 203 ----NLREFKEL-TEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAItigTLVAfiSYATQFFEPIQQ 277
|
250
....*....|....*..
gi 1907116879 504 LVRMSSEMETNIVAVER 520
Cdd:cd18540 278 LARVLAELQSAQASAER 294
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-126 |
2.33e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD----AHVGKHIFEkvVGPMGLlknkTRILVTHgisylpQVDV------ 97
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRE--LAETGI----TQVIVTH------EVEVarktas 209
|
90 100 110
....*....|....*....|....*....|.
gi 1907116879 98 -IIVMSGGKISEMGSYQELLD-RDGAFAEFL 126
Cdd:PRK11124 210 rVVYMENGHIVEQGDASCFTQpQTEAFKNYL 240
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
28-127 |
2.76e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 55.58 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH-VGkhifeKVVGPMGLLKN--KTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPElVG-----EVLKVMRDLAEegRTMLVVTHEMGFARDVsSHVVFLHQ 229
|
90 100
....*....|....*....|....*.
gi 1907116879 104 GKISEMGSYQELLD--RDGAFAEFLR 127
Cdd:COG4598 230 GRIEEQGPPAEVFGnpKSERLRQFLS 255
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
27-106 |
3.11e-08 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 55.45 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHgisylpQVDV--- 97
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQV-------MDLLRriaredGITVVVNLH------QVDLarr 212
|
90
....*....|...
gi 1907116879 98 ----IIVMSGGKI 106
Cdd:COG3638 213 yadrIIGLRDGRV 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
565-761 |
3.13e-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: 53.22 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 565 LVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglfrinesaegeiiidgvniakiglhnlrfkITIIPQDPVLFSGSLRmn 644
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKLIAGELEPDEGIVT-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 645 ldpfsqysdeevWMA-LELAHLkgfvsalpdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 723
Cdd:cd03221 59 ------------WGStVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907116879 724 LIQSTIRTQfeDCTVLTIAH-R--LNTIMdyTRVIVLDKGE 761
Cdd:cd03221 108 ALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-111 |
3.59e-08 |
|
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: 54.34 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 20 EIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVgKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVII 99
Cdd:cd03369 118 RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKIL 194
|
90
....*....|..
gi 1907116879 100 VMSGGKISEMGS 111
Cdd:cd03369 195 VMDAGEVKEYDH 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
27-115 |
3.63e-08 |
|
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: 54.82 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpmGLLKNKTRILVTHG---ISYLpqVDVIIVMSG 103
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLIL---EVRKGRSIILTTHSmdeAEAL--CDRIAIMSD 207
|
90
....*....|..
gi 1907116879 104 GKISEMGSYQEL 115
Cdd:cd03263 208 GKLRCIGSPQEL 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
567-748 |
3.79e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGVNIAKIGLHNLRFK-ITIIPQDPVLFSgslrm 643
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLDPFsqysdEEVWMALELAHlKGFVSALPdKLNHECAEGGENLSV--------------GQRQLVCLARALLRKTKILV 709
Cdd:TIGR02633 92 ELSVA-----ENIFLGNEITL-PGGRMAYN-AMYLRAKNLLRELQLdadnvtrpvgdyggGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907116879 710 LDEATAAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 748
Cdd:TIGR02633 165 LDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEV 204
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
28-116 |
3.82e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 55.23 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIF-------EKvvgpMGLlknkTRILVTHG------ISylpq 94
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIInlmlelqEK----LGI----SYIYVSQHlgivkhIS---- 217
|
90 100
....*....|....*....|..
gi 1907116879 95 vDVIIVMSGGKISEMGSYQELL 116
Cdd:COG4167 218 -DKVLVMHQGEVVEYGKTAEVF 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
28-115 |
4.36e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA--HVGKHI----FEKVVGpmgllknKTRILVTHG-ISYLPQVDVIIV 100
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIeisrLHKRLG-------RTMIYVTHDqVEAMTLADKIVV 206
|
90
....*....|....*
gi 1907116879 101 MSGGKISEMGSYQEL 115
Cdd:PRK11000 207 LDAGRVAQVGKPLEL 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
566-718 |
4.44e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGvniakiglhnlrfKITIIPQDPVLFSGSLRMNL 645
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-------------SIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 646 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 718
Cdd:PTZ00243 742 LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
566-718 |
4.74e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 54.36 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID----GVNIAKIG---LHNLRfKITI--------- 629
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR-RRTIgyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 630 IPQ--------DPVLFSGslrmnldpfsqYSDEEvwmALE-----LAHLKgfvsaLPDKLNHecaeggenL-----SVGQ 691
Cdd:COG4778 105 IPRvsaldvvaEPLLERG-----------VDREE---ARArarelLARLN-----LPERLWD--------LppatfSGGE 157
|
170 180
....*....|....*....|....*..
gi 1907116879 692 RQLVCLARALLRKTKILVLDEATAAVD 718
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
273-424 |
5.17e-08 |
|
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: 55.29 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 273 LSVYGAlgILQGAAIF--GYSMAVSIGGIFASRRLHLDLLYNV----LRSPMSFFERTPSGNLVNRFSkELDTV-DSMIP 345
Cdd:cd18782 41 LYVIGV--VMLVAALLeaVLTALRTYLFTDTANRIDLELGGTIidhlLRLPLGFFDKRPVGELSTRIS-ELDTIrGFLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 346 QVIKMFMGSLFSVIGAVIIILLATPIAAVI---IPPLGLVYFFVQRFYvasSRQLKRLESvSRSPVYSHFNETLLGVSVI 422
Cdd:cd18782 118 TALTTLLDVLFSVIYIAVLFSYSPLLTLVVlatVPLQLLLTFLFGPIL---RRQIRRRAE-ASAKTQSYLVESLTGIQTV 193
|
..
gi 1907116879 423 RA 424
Cdd:cd18782 194 KA 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
28-106 |
5.30e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLKN-----KTRILVTHGISYLPQVDVIIVMS 102
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV-------MAILHQlrdrgHTVIIVTHDPQVAAQAERVIEIR 217
|
....
gi 1907116879 103 GGKI 106
Cdd:PRK10535 218 DGEI 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-118 |
5.56e-08 |
|
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: 55.44 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIV 100
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQI-------LNLLKdlqrelGLAILFITHDLGVVAEIaDRVAV 223
|
90
....*....|....*...
gi 1907116879 101 MSGGKISEMGSYQELLDR 118
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
28-119 |
5.92e-08 |
|
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: 54.66 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvgkHIFEkVvgpMGLLK------NKTRILVTHgisYLPQV----DV 97
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA---HQLE-V---LELLRrlarerGRTVVMVLH---DLNLAaryaDR 207
|
90 100
....*....|....*....|..
gi 1907116879 98 IIVMSGGKISEMGSYQELLDRD 119
Cdd:COG1120 208 LVLLKDGRIVAQGPPEEVLTPE 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-119 |
6.02e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.24 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFekvvgpMGLLK-----NKTRILVTHGISYLPQV-DVIIVM 101
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEM------MQLILdakanNKTVFVITHTMEHVLEVaDEVIVM 249
|
90
....*....|....*....
gi 1907116879 102 SGGKISEMGS-YQELLDRD 119
Cdd:PRK13631 250 DKGKILKTGTpYEIFTDQH 268
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
28-108 |
6.40e-08 |
|
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: 53.98 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLL--KNKTR----ILVTHGISYLPQVDVIIVM 101
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI-------IDLLfeLNRERgttlVLVTHDPALAARCDRVLRL 219
|
....*..
gi 1907116879 102 SGGKISE 108
Cdd:COG4181 220 RAGRLVE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
567-760 |
6.54e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGlHNLRFK--ITIIPQD-PVLFSGSLRM 643
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 644 NLdPFSQYSDEEVWMA--LELAHLKGFVSALPDK--LNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV-D 718
Cdd:PRK09700 100 NL-YIGRHLTKKVCGVniIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907116879 719 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKG 760
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-106 |
7.14e-08 |
|
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: 52.82 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvgpMGLLKN--KTRILVTHGISYLPQV-DVIIVMSGG 104
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV----IRRLRAqgVAVIFISHRLDEVFEIaDRVTVLRDG 158
|
..
gi 1907116879 105 KI 106
Cdd:cd03216 159 RV 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-118 |
7.71e-08 |
|
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: 55.12 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLKNKTR------ILVTHGISYLPQV-DVIIV 100
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI-------LPYLERLHAefgipiLYVSHSLQEVLRLaDRVVV 204
|
90
....*....|....*...
gi 1907116879 101 MSGGKISEMGSYQELLDR 118
Cdd:TIGR02142 205 LEDGRVAAAGPIAEVWAS 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-118 |
8.82e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.46 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLKnktRILVTHGISYL-----PQV-----DV 97
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD-------LLR---DLQREHGLAYLfishdLAVvralaHR 495
|
90 100
....*....|....*....|.
gi 1907116879 98 IIVMSGGKISEMGSYQELLDR 118
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
566-771 |
9.43e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.70 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGVNIA-------KIG--------------L 620
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiaglEHQTSGHIRFHGTDVSrlhardrKVGfvfqhyalfrhmtvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 621 HNLRFKITIIPQDPvlfsgslrmnlDPFSQYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARA 700
Cdd:PRK10851 93 DNIAFGLTVLPRRE-----------RPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 701 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 771
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
27-106 |
1.20e-07 |
|
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: 53.34 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHgisylpQVDV--- 97
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQV-------MDLLKrinreeGITVIVSLH------QVDLare 210
|
90
....*....|...
gi 1907116879 98 ----IIVMSGGKI 106
Cdd:cd03256 211 yadrIVGLKDGRI 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-56 |
1.21e-07 |
|
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: 51.88 E-value: 1.21e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1907116879 19 TEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLS 56
Cdd:pfam00005 113 RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
577-763 |
1.21e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 577 GEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDGvniAKIGLHN----LRFKITIIPQD-------PVLFSG--SLR 642
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDG---KPVKIRNpqqaIAQGIAMVPEDrkrdgivPVMGVGknITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 643 MNLDPFSQYS--DEevwmALELAHLKGFVSALPDKLNHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDL- 719
Cdd:PRK13549 365 AALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVg 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907116879 720 ---ETDNLIQSTIRtqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVR 763
Cdd:PRK13549 440 akyEIYKLINQLVQ---QGVAIIVISSELPEVLGLSdRVLVMHEGKLK 484
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
281-430 |
1.41e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 53.64 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 281 ILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIG 360
Cdd:cd18576 47 LLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIG 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 361 AVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQlkRLESVSRSPVysHFNETLLGVSVIRAF--EEQER 430
Cdd:cd18576 127 GVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKK--VQDELAEANT--IVEETLQGIRVVKAFtrEDYEI 198
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
274-429 |
1.84e-07 |
|
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: 53.67 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 274 SVYGALG---ILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKM 350
Cdd:cd18573 42 TFALALLgvfVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 351 FMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLkrLESVSRSpvySHF-NETLLGVSVIRAF 425
Cdd:cd18573 122 GLRSLVSGVGGIGMMLYISPkltlVMLLVVPPIAVGAVFYGRYVRKLSKQV--QDALADA---TKVaEERLSNIRTVRAF 196
|
....*.
gi 1907116879 426 --EEQE 429
Cdd:cd18573 197 aaERKE 202
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
27-117 |
2.36e-07 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 52.69 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLKnktRILVTHGISY---LPQVDV------ 97
Cdd:TIGR02315 145 QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQV-------MDYLK---RINKEDGITViinLHQVDLakkyad 214
|
90 100
....*....|....*....|.
gi 1907116879 98 -IIVMSGGKISEMGSYQELLD 117
Cdd:TIGR02315 215 rIVGLKAGEIVFDGAPSELDD 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
566-718 |
2.84e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.87 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNI--------AKIGL-------------HN 622
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIrsprdairAGIAYvpedrkgeglvldLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 623 LRFKITIipqdPVLFSGSLRMNLDPfsqysdeevwmALELAHLKGFVSAL---PDKLNHECAeggeNLSVGQRQLVCLAR 699
Cdd:COG1129 347 IRENITL----ASLDRLSRGGLLDR-----------RRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170
....*....|....*....
gi 1907116879 700 ALLRKTKILVLDEATAAVD 718
Cdd:COG1129 408 WLATDPKVLILDEPTRGID 426
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
566-772 |
3.01e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLT--LGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDP----VLFSG 639
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 640 SLRMNLD---PFSQY--------------------SDEEvwmALELAhlKGFVS--ALPDKLnheCAEGGENLSVGQRQL 694
Cdd:PRK13651 102 EIRRRVGvvfQFAEYqlfeqtiekdiifgpvsmgvSKEE---AKKRA--AKYIElvGLDESY---LQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 695 VCLARALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkRTIFFKDGKIIKDGDTYDIL 253
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-89 |
3.01e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.56 E-value: 3.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvgpmgLLK-----NKTRILVTHGI 89
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQEL------LLDvwqrtGKGVFLITHSV 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
566-762 |
3.07e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.96 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL----RFKITIIPQDPVLFSG-S 640
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 641 LRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 720
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ----LSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907116879 721 TDNLIQSTIRtQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEV 762
Cdd:PRK10535 179 SGEEVMAILH-QLRDrgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
556-725 |
3.24e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.13 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 556 CLRYRED--LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-------------- 619
Cdd:PRK11629 12 CKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaelrnqklgf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 620 ---LHNLRFKITIIPQD--PVLFSGSLRMNldpfSQYSDEEVWMALELAHlkgfvsalpdKLNHECAEggenLSVGQRQL 694
Cdd:PRK11629 92 iyqFHHLLPDFTALENVamPLLIGKKKPAE----INSRALEMLAAVGLEH----------RANHRPSE----LSGGERQR 153
|
170 180 190
....*....|....*....|....*....|.
gi 1907116879 695 VCLARALLRKTKILVLDEATAAVDLETDNLI 725
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
566-712 |
3.76e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.80 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI-----AKIglhnLRFKITIIPQDPVLFSgs 640
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 641 lRMNLDpfsqysdEEVWMALELAHLKGF------VSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 712
Cdd:PRK11614 94 -RMTVE-------ENLAMGGFFAERDQFqerikwVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
567-774 |
4.04e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSS----LTlGLfrINESAeGEIIIDGVNIAKIGLHNLRfKITII------------ 630
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLT-GI--LVPTS-GEVRVLGYVPFKRRKEFAR-RIGVVfgqrsqlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 631 PQDpvlfsgSLRMN-----LDP--FSQYSDEEVWMaLELAH-LKGFVsalpdklnhecaeggENLSVGQRQLVCLARALL 702
Cdd:COG4586 113 AID------SFRLLkaiyrIPDaeYKKRLDELVEL-LDLGElLDTPV---------------RQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 703 RKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 774
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
228-485 |
4.41e-07 |
|
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: 52.46 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 228 LFITFLSIFLFLCnhvsALASNYWLSLWTDDppVVngTQANRNFrLSV----YGALGILQGAAifgySMAVSIGGIFASR 303
Cdd:cd18567 5 LQILLLSLALELF----ALASPLYLQLVIDE--VI--VSGDRDL-LTVlaigFGLLLLLQALL----SALRSWLVLYLST 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 304 RLHLDLLYNV----LRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMFMGSLFSVIGAVIIILLATPIAAVIIPP 378
Cdd:cd18567 72 SLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFG-SLDEIQQTLTtGFVEALLDGLMAILTLVMMFLYSPKLALIVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 379 LgLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIHQSDLKVDE-NQkayypSIVANRWL 456
Cdd:cd18567 151 V-ALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFgREAEREARWLNLLVDAiNA-----DIRLQRLQ 224
|
250 260 270
....*....|....*....|....*....|....*
gi 1907116879 457 AVR------LECVGNCIVLFAALFAVISRHsLSAG 485
Cdd:cd18567 225 ILFsaanglLFGLENILVIYLGALLVLDGE-FTVG 258
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
567-748 |
4.46e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNiakiglhnLRFK---------ITIIPQDpvlf 637
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--------MRFAsttaalaagVAIIYQE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 638 sgslrMNLDPfsQYSDEEVWMALELAHLKGFV--SALPDKLNHECAEGGEN---------LSVGQRQLVCLARALLRKTK 706
Cdd:PRK11288 88 -----LHLVP--EMTVAENLYLGQLPHKGGIVnrRLLNYEAREQLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907116879 707 ILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTI 748
Cdd:PRK11288 161 VIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEI 203
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
272-451 |
4.76e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 52.15 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 272 RLSVYGALGILQGAAIFGYSMAVSIGGIFASR---RLHLDL---LYNVL-RSPMSFFERTPSGNLVNRFSKELDTVDSMI 344
Cdd:cd18778 35 SLGLLLGLALLLLGAYLLRALLNFLRIYLNHVaeqKVVADLrsdLYDKLqRLSLRYFDDRQTGDLMSRVINDVANVERLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 345 PQVIKMFMGSLFSVIGAVIIILLATPI-AAVIIPPLGLVYFFVqRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIR 423
Cdd:cd18778 115 ADGIPQGITNVLTLVGVAIILFSINPKlALLTLIPIPFLALGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQ 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907116879 424 AF----EEQERFIHQSDLKVDENQKA------YYPSIV 451
Cdd:cd18778 194 AFgreeEEAKRFEALSRRYRKAQLRAmklwaiFHPLME 231
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
281-444 |
4.97e-07 |
|
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: 52.16 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 281 ILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIG 360
Cdd:cd18574 53 LLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 361 AVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRspvySHFNETLLGVSVIRAF----EEQERFI 432
Cdd:cd18574 133 CVVSLYLISPkltlLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKAT----GVADEALGNIRTVRAFamedRELELYE 208
|
170
....*....|..
gi 1907116879 433 HQSDLKVDENQK 444
Cdd:cd18574 209 EEVEKAAKLNEK 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
27-87 |
5.64e-07 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 50.97 E-value: 5.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTH 87
Cdd:COG4619 130 RLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-NTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
28-106 |
5.85e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVG---KHIFEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiemQDLIESLWQQHGF----TVLLVTHDVSEAVAMaDRVLLIEE 209
|
...
gi 1907116879 104 GKI 106
Cdd:PRK11247 210 GKI 212
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
278-445 |
6.42e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 52.07 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 278 ALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTP--SGNLVNRFSKELDTVDSMIPQVIKMFMGSL 355
Cdd:cd18578 60 VLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 356 FSVIGAVIIILLA----TPIAAVIIPPLGLVYFFVQRFYVASSRQLKR-LESVSRspvysHFNETLLGVSVIRAFEEQER 430
Cdd:cd18578 140 VTLVAGLIIAFVYgwklALVGLATVPLLLLAGYLRMRLLSGFEEKNKKaYEESSK-----IASEAVSNIRTVASLTLEDY 214
|
170
....*....|....*
gi 1907116879 431 FIHQSDLKVDENQKA 445
Cdd:cd18578 215 FLEKYEEALEEPLKK 229
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
545-744 |
6.88e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 545 PHSGRVEFRDYCLRYrEDLDLV-------LKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRInesaEGEI--IIDGVnI 615
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSL----FRI----LGELwpVYGGR-L 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 616 AKiglhNLRFKITIIPQDPVLFSGSLR------MNLDPFSQ--YSDEEVWMALELAHLKGFVSAlpdklnhecaEGG--- 684
Cdd:TIGR00954 510 TK----PAKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQLTHILER----------EGGwsa 575
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 685 -----ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIqstirtqFEDC-----TVLTIAHR 744
Cdd:TIGR00954 576 vqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-116 |
7.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.53 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 7 LPDLEILPSGDRT--EIG-EK-----GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGllK 78
Cdd:PRK13644 108 LPPIEIRKRVDRAlaEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE--K 185
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907116879 79 NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 116
Cdd:PRK13644 186 GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-118 |
1.06e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKI 106
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
90
....*....|..
gi 1907116879 107 SEMGSYQELLDR 118
Cdd:PRK13640 222 LAQGSPVEIFSK 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-129 |
1.32e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.57 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEV 243
|
90 100
....*....|....*....|...
gi 1907116879 107 SEMGSYQELLDRDGafAEFLRTY 129
Cdd:PRK10070 244 VQVGTPDEILNNPA--NDYVRTF 264
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
687-771 |
1.34e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.00 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 687 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRE 764
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILK 256
|
....*..
gi 1907116879 765 CGAPSEL 771
Cdd:PRK13631 257 TGTPYEI 263
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-114 |
1.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKI 106
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK-IKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
....*...
gi 1907116879 107 SEMGSYQE 114
Cdd:PRK13637 224 ELQGTPRE 231
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
302-521 |
1.55e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 50.52 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 302 SRRLHLDLLYN----VLRSPMSFFERTPSGNLVNRFSkELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAA 373
Cdd:cd18570 70 SQKLDIRLILGyfkhLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWklflITL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 374 VIIPPLGLVYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS---I 450
Cdd:cd18570 149 LIIPLYILIILLFNKPF----KKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 451 VANRWLAVRLECVGNCIVLFAALFAVISrHSLSaglVGLSVSYsLQITAY----LNWLVRMSSEMETNIVAVERL 521
Cdd:cd18570 225 NLQSSIKGLISLIGSLLILWIGSYLVIK-GQLS---LGQLIAF-NALLGYflgpIENLINLQPKIQEAKVAADRL 294
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-137 |
1.68e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 14 PSGDRTeIGekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmglLKNKTR------ILVTh 87
Cdd:PRK10762 387 PSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ--------LINQFKaeglsiILVS- 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 88 giSYLPQV----DVIIVMSGGKISemgsyqelldrdgafAEFLRTYANAEQDLA 137
Cdd:PRK10762 453 --SEMPEVlgmsDRILVMHEGRIS---------------GEFTREQATQEKLMA 489
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
23-87 |
1.70e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.16 E-value: 1.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 23 EKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmglLKNK-TRILVTH 87
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG----LKDDyTMLLVTR 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-117 |
2.00e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGK 105
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELL--FELKKEYTIVLVTHSPAQAARVsDYVAFLYLGK 225
|
90
....*....|..
gi 1907116879 106 ISEMGSYQELLD 117
Cdd:PRK14267 226 LIEVGPTRKVFE 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-145 |
2.83e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.78 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 23 EKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvgpMGLLKNK-TRILVTHGISYLPQVDVIIVM 101
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEEL----MHELKEQyTIIIVTHNMQQAARVSDMTAF 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907116879 102 SGGKISEMGSyqelldRDGAFAEFLRTYA--NAEQDLASEdDSVSG 145
Cdd:PRK14243 223 FNVELTEGGG------RYGYLVEFDRTEKifNSPQQQATR-DYVSG 261
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-117 |
3.16e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.83 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPmgLLKNKTRILVTHGISYLPQV-DVIIVMSGG-K 105
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL--LARGKTILLTTHFMEEAERLcDRLCVLEAGrK 250
|
90
....*....|..
gi 1907116879 106 ISEmGSYQELLD 117
Cdd:PRK13536 251 IAE-GRPHALID 261
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
275-434 |
3.21e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 49.82 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 275 VYGALGILQGA--AIFGYSMAVSIGGIFASRRLHLdllynvlrsPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMF 351
Cdd:cd18555 54 LYGLFSFLRGYiiIKLQTKLDKSLMSDFFEHLLKL---------PYSFFENRSSGDLLFRAN-SNVYIRQILSnQVISLI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 352 MGSLFSVIGAVIIILLATPIAAVIIpPLGLVYFFvqrFYVASSRQLKRL---ESVSRSPVYSHFNETLLGVSVIRAFEEQ 428
Cdd:cd18555 124 IDLLLLVIYLIYMLYYSPLLTLIVL-LLGLLIVL---LLLLTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSLGSE 199
|
....*.
gi 1907116879 429 ERFIHQ 434
Cdd:cd18555 200 KNIYKK 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
567-773 |
3.29e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-------------IID-------------GVNIAKIgl 620
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIElseqsaaqmrhvrGADMAMI-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 621 hnlrFKITIIPQDPVLFSG-----SLRMNLDPFSQYSDEEVWMALELAHL---KGFVSALPdklnHEcaeggenLSVGQR 692
Cdd:PRK10261 110 ----FQEPMTSLNPVFTVGeqiaeSIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYP----HQ-------LSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 693 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT--VLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPS 769
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAdRVLVMYQGEAVETGSVE 254
|
....
gi 1907116879 770 ELLQ 773
Cdd:PRK10261 255 QIFH 258
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-115 |
3.50e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.32 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKhifEKVVGPMGLLKNK---TRILVTHGISYLPQVDVIIVMSGG 104
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP-SGR---REVVNTIKELNKKygiTIILITHYMEEAVEADRIIVMDSG 220
|
90
....*....|.
gi 1907116879 105 KISEMGSYQEL 115
Cdd:PRK13633 221 KVVMEGTPKEI 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
28-119 |
3.56e-06 |
|
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: 48.82 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFE---KVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDElirELRDELGL----TSVVVTHDLDSAFAIaDRVAVLAD 217
|
90
....*....|....*.
gi 1907116879 104 GKISEMGSYQELLDRD 119
Cdd:COG1127 218 GKIIAEGTPEELLASD 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
550-771 |
3.83e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.03 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-----VNIAKIGLHNLR 624
Cdd:PRK11000 4 VTLRNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 625 FKITIIPQDPVLFSGSLRMNLDPFS----QYSDEEVWMALELAHLkgfVSALPdklnhecaeggENLSVGQRQLVCLARA 700
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKkeeiNQRVNQVAEVLQLAHL---LDRKP-----------KALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 701 LLRKTKILVLDEATAAVD--LETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDytRVIVLDKGEVRECGAPSEL 771
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDaaLRVQMRIEISRLHKRLGRTMIYVTHdqvEAMTLAD--KIVVLDAGRVAQVGKPLEL 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-135 |
3.95e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.02 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 9 DLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDahVG-KH-IFEKVvgpMGLLKNKTRILVt 86
Cdd:COG1129 380 RLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID--VGaKAeIYRLI---RELAAEGKAVIV- 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 87 hgIS-YLPQV----DVIIVMSGGKISEMgsyqelLDRDGAFAEFLRTYANAEQD 135
Cdd:COG1129 450 --ISsELPELlglsDRILVMREGRIVGE------LDREEATEEAIMAAATGGAA 495
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
279-450 |
4.19e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 49.49 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 279 LGILQGAAIFGYSMAVSIGGiFASRRLH---LDLLYNVLRSPMSFFERTPSGNL-------VNRFSKELDTvdsMIPQVI 348
Cdd:cd18565 61 VAAFLLESLFQYLSGVLWRR-FAQRVQHdlrTDTYDHVQRLDMAFFEDRQTGDLmsvlnndVNQLERFLDD---GANSII 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 349 KMFmgSLFSVIGAVIIIL---LATpIAAVIIPPL-GLVYFFVQRfyvASSRQLKRLESVSRspVYSHFNETLLGVSVIRA 424
Cdd:cd18565 137 RVV--VTVLGIGAILFYLnwqLAL-VALLPVPLIiAGTYWFQRR---IEPRYRAVREAVGD--LNARLENNLSGIAVIKA 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907116879 425 F----EEQERFIHQSDLKVDENQKA------YYPSI 450
Cdd:cd18565 209 FtaedFERERVADASEEYRDANWRAirlraaFFPVI 244
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-118 |
4.44e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 2 EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKT 81
Cdd:PRK13645 125 EAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKR 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907116879 82 RILVTHGISYLPQV-DVIIVMSGGKISEMG------SYQELLDR 118
Cdd:PRK13645 204 IIMVTHNMDQVLRIaDEVIVMHEGKVISIGspfeifSNQELLTK 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-118 |
5.00e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHgisYLPQV----DVIIVMSG 103
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF---LELKKDMTIVLVTH---FPQQAarisDYVAFLYK 220
|
90
....*....|....*
gi 1907116879 104 GKISEMGSYQELLDR 118
Cdd:PRK14247 221 GQIVEWGPTREVFTN 235
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
299-521 |
5.96e-06 |
|
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: 48.71 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 299 IFASRRLHLDLL---YN-VLRSPMSFFERTPSGNLVNRFsKELDTVDSMI-PQVIKMFMGSLFSVIgaVIIILLA----- 368
Cdd:cd18568 67 DYFANRIDLSLLsdfYKhLLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFI--YLGLMFYynlql 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 369 TPIAAVIIPPLGLvyffvqrFYVASSRQLKRLES---VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKA 445
Cdd:cd18568 144 TLIVLAFIPLYVL-------LTLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 446 YYPSIVanrwLAVRLECV-------GNCIVLFAALFAVISrHSLSAG-LVGLSVSYSLQITAYLNwLVRMSSEMETNIVA 517
Cdd:cd18568 217 RFRGQK----LSIVLQLIsslinhlGTIAVLWYGAYLVIS-GQLTIGqLVAFNMLFGSVINPLLA-LVGLWDELQETRIS 290
|
....
gi 1907116879 518 VERL 521
Cdd:cd18568 291 VERL 294
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
27-61 |
6.07e-06 |
|
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: 47.86 E-value: 6.07e-06
10 20 30
....*....|....*....|....*....|....*
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 61
Cdd:COG4133 131 QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-126 |
6.43e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 48.21 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDahvgkhifekvvgP------MGLLK------NKTRILVTHGIS-YLPQ 94
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALD-------------PalrqemLDLVDelcrerGLTVLMVTHDPEdAARI 196
|
90 100 110
....*....|....*....|....*....|....
gi 1907116879 95 VDVIIVMSGGKISEMGSYQELLDRDG--AFAEFL 126
Cdd:COG3840 197 ADRVLLVADGRIAADGPTAALLDGEPppALAAYL 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-122 |
6.66e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGK---HIFEKVVgpmglLKNKTRILVTHGI-SYLPQVDVIIVMS 102
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeilEIFDNLN-----KQGKTIILVTHDLdNVLEWTKRTIFFK 239
|
90 100
....*....|....*....|
gi 1907116879 103 GGKISEMGSYQELLdRDGAF 122
Cdd:PRK13651 240 DGKIIKDGDTYDIL-SDNKF 258
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
304-424 |
8.31e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 48.35 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 304 RLHLDLLYNVLRSPMSFFERTPSGNLVNRFsKELDTV-DSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAViipPLGLV 382
Cdd:cd18566 76 RLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIrEFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLV---PLVLL 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907116879 383 YFFVQRFYVASSRQLKRLESVSRSPV--YSHFNETLLGVSVIRA 424
Cdd:cd18566 152 GLFVLVAILLGPILRRALKERSRADErrQNFLIETLTGIHTIKA 195
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-119 |
1.04e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 10 LEILPSGDRTEIGEKGV---NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVgKHIFEKVVGPMGLLKNKTRILVT 86
Cdd:PRK10522 429 LERLKMAHKLELEDGRIsnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVLLPLLQEMGKTIFAIS 507
|
90 100 110
....*....|....*....|....*....|....
gi 1907116879 87 HGISYLPQVDVIIVMSGGKISEM-GSYQELLDRD 119
Cdd:PRK10522 508 HDDHYFIHADRLLEMRNGQLSELtGEERDAASRD 541
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
687-761 |
1.21e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 1.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 687 LSVGQRQLVCLARALLRKTKILVLDEATAAV-DLETDNLIqSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE 761
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEICdDVTVFRDGQ 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
565-771 |
1.25e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.68 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 565 LVLKHINVTIEGGEKVGIVGRTGAGKSS----LTlGLFRineSAEGEIIIDGVN--------IAKIGL----HNLR-FK- 626
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTvfncLT-GFYK---PTGGTILLRGQHieglpghqIARMGVvrtfQHVRlFRe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 627 ITIIPQDPV---------LFSGSLRMnldPFSQYSDEEvwmALELAHLKGFVSALPDKLNHECAeggeNLSVGQRQLVCL 697
Cdd:PRK11300 95 MTVIENLLVaqhqqlktgLFSGLLKT---PAFRRAESE---ALDRAATWLERVGLLEHANRQAG----NLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 698 ARALLRKTKILVLDEATAAVD-LETDNLIQ--STIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 771
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEI 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
5-117 |
1.49e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.50 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 5 ALLPDLEILPSGDrTEIGEKGV--NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHifekVVGPMGLL--KNK 80
Cdd:TIGR00955 143 EVLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS----VVQVLKGLaqKGK 217
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907116879 81 TRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQELLD 117
Cdd:TIGR00955 218 TIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
567-762 |
1.50e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLfrinesaEGEIIIDG--VNIAKiglhnlRFKITIIPQDP------VLFS 638
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgrIIYEQ------DLIVARLQQDPprnvegTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 639 ---------GSL-----RMNLDPFSQYSDEevwMALELAHLKGFVS-----ALPDKLNHECAEGGEN-------LSVGQR 692
Cdd:PRK11147 86 fvaegieeqAEYlkryhDISHLVETDPSEK---NLNELAKLQEQLDhhnlwQLENRINEVLAQLGLDpdaalssLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 693 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqFEDCTVLtIAHRLNTI--MdYTRVIVLDKGEV 762
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHDRSFIrnM-ATRIVDLDRGKL 231
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-129 |
1.80e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 26 VNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGg 104
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEEGKKTALVVEHDLAVLDYLsDRIHVFEG- 147
|
90 100
....*....|....*....|....*...
gi 1907116879 105 kisEMGSYQELLDRDG---AFAEFLRTY 129
Cdd:cd03222 148 ---EPGVYGIASQPKGtreGINRFLRGY 172
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
567-772 |
1.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 567 LKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrINESaeGEIIIDG----VNIAKIG-LHNLRFKITIIPQDP--VL 636
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI-ISET--GQTIVGDyaipANLKKIKeVKRLRKEIGLVFQFPeyQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 FSGSLRMNL--DPFSQYSD-EEVWMalELAHLKGFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 713
Cdd:PRK13645 104 FQETIEKDIafGPVNLGENkQEAYK--KVPELLKLVQLPEDYVKRSPFE----LSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907116879 714 TAAVDL--ETD--NLIQSTIRTQFEdcTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:PRK13645 178 TGGLDPkgEEDfiNLFERLNKEYKK--RIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-116 |
2.31e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.58 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPmgLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVaDYVAFLYNGEL 230
|
90
....*....|
gi 1907116879 107 SEMGSYQELL 116
Cdd:PRK14246 231 VEWGSSNEIF 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-60 |
2.67e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.62 E-value: 2.67e-05
10 20 30
....*....|....*....|....*....|...
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 60
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-95 |
3.13e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.57 E-value: 3.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 18 RTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVTHGisyLPQV 95
Cdd:PRK14258 141 KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHN---LHQV 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
566-772 |
3.28e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGVNIAKIGLHNLRF----KITIIPQDPVL 636
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 fsgslrmNLDPFSQYSDE--EVW-----MALELAhlKGFVSALPDKLNHECAEGGEN-----LSVGQRQLVCLARALLRK 704
Cdd:PRK15134 104 -------SLNPLHTLEKQlyEVLslhrgMRREAA--RGEILNCLDRVGIRQAAKRLTdyphqLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 705 TKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 772
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLAdRVAVMQNGRCVEQNRAATLF 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-116 |
3.30e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 46.16 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 19 TEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvgkHIFEkVVGPMGLLKN--KTRILVTHGIS----Y 91
Cdd:PRK11231 129 NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN---HQVE-LMRLMRELNTqgKTVVTVLHDLNqasrY 204
|
90 100
....*....|....*....|....*
gi 1907116879 92 lpqVDVIIVMSGGKISEMGSYQELL 116
Cdd:PRK11231 205 ---CDHLVVLANGHVMAQGTPEEVM 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
28-118 |
3.35e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 46.65 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSG 103
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVlnlLEDLQDELGL----TYLFISHDLSVVRHIsDRVAVMYL 233
|
90
....*....|....*
gi 1907116879 104 GKISEMGSYQELLDR 118
Cdd:COG4608 234 GKIVEIAPRDELYAR 248
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-119 |
3.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKI 106
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSI 224
|
90
....*....|...
gi 1907116879 107 SEMGSYQELLDRD 119
Cdd:PRK13646 225 VSQTSPKELFKDK 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-59 |
3.50e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 3.50e-05
10 20 30
....*....|....*....|....*....|..
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
565-772 |
4.01e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 565 LVLKHINV---------TIEGGEKVGIVGRTGAGKSSL---TLGLFrineSAEGEIIIDGVNIAKIGLHNL-RFKITIIP 631
Cdd:PRK03695 1 MQLNDVAVstrlgplsaEVRAGEILHLVGPNGAGKSTLlarMAGLL----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 632 QDPVLFSgslrMnldPFSQYSD---------EEVWMAL-ELAHLKGfvsaLPDKLnHECAeggENLSVGQRQLVCLARAL 701
Cdd:PRK03695 77 QQTPPFA----M---PVFQYLTlhqpdktrtEAVASALnEVAEALG----LDDKL-GRSV---NQLSGGEWQRVRLAAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 702 LR-------KTKILVLDEATAAVDLETDNLIQSTIRtqfEDC----TVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPS 769
Cdd:PRK03695 142 LQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLS---ELCqqgiAVVMSSHDLNHTLRHaDRVWLLKQGKLLASGRRD 218
|
...
gi 1907116879 770 ELL 772
Cdd:PRK03695 219 EVL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-110 |
4.79e-05 |
|
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: 44.85 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK-----NKTRILVTHGISYL--PQVDVIIV 100
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV-------MSLLRrladtGRTIICSIHQPSSEifELFDKLLL 184
|
90
....*....|
gi 1907116879 101 MSGGKISEMG 110
Cdd:cd03213 185 LSQGRVIYFG 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-110 |
4.89e-05 |
|
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: 45.18 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKNkTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKM-TVLMVTHQPEDAKRLaQRVVFLDNGRI 207
|
....
gi 1907116879 107 SEMG 110
Cdd:cd03298 208 AAQG 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-118 |
4.93e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.11 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 29 SGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGG 104
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlMMDLQQELGL----SYVFISHDLSVVEHIaDEVMVMYLG 231
|
90
....*....|....
gi 1907116879 105 KISEMGSYQELLDR 118
Cdd:PRK11308 232 RCVEKGTKEQIFNN 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-115 |
5.31e-05 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 45.53 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNK--TRILVTHGI-SYLPQVDVIIVMSGG 104
Cdd:TIGR01184 115 LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL---MQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
90
....*....|.
gi 1907116879 105 KISEMGSYQEL 115
Cdd:TIGR01184 192 PAANIGQILEV 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
577-761 |
5.67e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 577 GEKVGIVGRTGAGKSSLTLGLFR-INESAEGEIIIDGVNIAKIGLHNLRFKITiipqdpvlfsgslrmnldpfsqysdee 655
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 656 vwmalelahlkgfvsalpdklnhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF-- 733
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907116879 734 -----EDCTVLTIAHRLNTIMD------YTRVIVLDKGE 761
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-118 |
5.80e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.88 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 107
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE-GRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
90
....*....|.
gi 1907116879 108 EMGSYQELLDR 118
Cdd:PRK13650 220 STSTPRELFSR 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-87 |
6.00e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 6.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907116879 25 GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD----AHVGKHIFEkvvgpmglLKNK-TRILVTH 87
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTH 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-115 |
6.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.45 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTHGISYLP-QVDVIIVM 101
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQI-------MKLLYdlNKegiTIIISTHDVDLVPvYADKVYVM 210
|
90
....*....|....
gi 1907116879 102 SGGKISEMGSYQEL 115
Cdd:PRK13639 211 SDGKIIKEGTPKEV 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-115 |
7.00e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 106
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL-ELQQKENMALVLITHDLALVAEAaHKIIVMYAGQV 232
|
....*....
gi 1907116879 107 SEMGSYQEL 115
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
573-761 |
7.93e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 573 TIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDgVNIAkiglhnlrFK---ITIIPQDPVlfSGSLRMNLDPF- 648
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS--------YKpqyIKPDYDGTV--EDLLRSITDDLg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 649 SQYSDEEVWMALELAHLkgfvsaLPDKLNhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 728
Cdd:PRK13409 430 SSYYKSEIIKPLQLERL------LDKNVK--------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907116879 729 IRTQFE--DCTVLTIAHRLnTIMDY--TRVIVLDkGE 761
Cdd:PRK13409 496 IRRIAEerEATALVVDHDI-YMIDYisDRLMVFE-GE 530
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-116 |
9.14e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.09 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 18 RTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQV-D 96
Cdd:PRK14271 154 KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVIIVTHNLAQAARIsD 230
|
90 100
....*....|....*....|
gi 1907116879 97 VIIVMSGGKISEMGSYQELL 116
Cdd:PRK14271 231 RAALFFDGRLVEEGPTEQLF 250
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-119 |
9.25e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.18 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGllKNKTRILVTHGISYLPQV--DVIIVMSGGK 105
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA--RGKTILLTTHFMEEAERLcdRLCVIEEGRK 216
|
90
....*....|....
gi 1907116879 106 ISEmGSYQELLDRD 119
Cdd:PRK13537 217 IAE-GAPHALIESE 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
686-749 |
9.94e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 9.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 686 NLSVGQRQLVCLARALLRKTKILVLDEATAAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM 749
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIR 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
566-771 |
1.04e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.22 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDG--VN--------IAKI------------- 618
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTL-LrmvaGLERI---TSGEIWIGGrvVNelepadrdIAMVfqnyalyphmsvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 619 -----GLHNLRFKITIIPQdpvlfsgslRMnldpfsqysdEEVWMALELAHLkgfvsalpdkLNHECAEggenLSVGQRQ 693
Cdd:PRK11650 95 enmayGLKIRGMPKAEIEE---------RV----------AEAARILELEPL----------LDRKPRE----LSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 694 LVCLARALLRKTKILVLDEATAAVD--------LETDNLiQSTIRT--------QFEdctVLTIAHRLntimdytrvIVL 757
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLEIQRL-HRRLKTtslyvthdQVE---AMTLADRV---------VVM 208
|
250
....*....|....
gi 1907116879 758 DKGEVRECGAPSEL 771
Cdd:PRK11650 209 NGGVAEQIGTPVEV 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-114 |
1.16e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.32 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 20 EIGEKGVN-LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVI 98
Cdd:PRK10247 129 TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKV 207
|
90
....*....|....*.
gi 1907116879 99 IVMSggkiSEMGSYQE 114
Cdd:PRK10247 208 ITLQ----PHAGEMQE 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-87 |
1.19e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.42 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTH 87
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ-LLGELNRLQGTAFLVVTH 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
564-763 |
1.36e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 564 DLVLKhINVTIEGGEKVGIVGRTGAGKSSLtlglfrINESA------EGEIIIDG---VNIAK-IGLHNLRFKITIIPQD 633
Cdd:PRK11144 12 DLCLT-VNLTLPAQGITAIFGRSGAGKTSL------INAISgltrpqKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 634 PVLF-----SGSLRMNLDPFSQ-YSDEEVWMaLELAHLkgfVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKI 707
Cdd:PRK11144 85 ARLFphykvRGNLRYGMAKSMVaQFDKIVAL-LGIEPL---LDRYP-----------GSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907116879 708 LVLDEATAAVDL----ETDNLIQSTIRTQfeDCTVLTIAHRLNTIM---DytRVIVLDKGEVR 763
Cdd:PRK11144 150 LLMDEPLASLDLprkrELLPYLERLAREI--NIPILYVSHSLDEILrlaD--RVVVLEQGKVK 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-135 |
1.44e-04 |
|
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: 45.18 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmGLLKNKTRILVThgiSYLPQV-----DVIIVM 101
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE--AVKASGISMVLT---SHWPEViedlsDKAIWL 242
|
90 100 110
....*....|....*....|....*....|....
gi 1907116879 102 SGGKISEMGSYQELLDRdgafaeFLRTYANAEQD 135
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV------FMEGVSEVEKE 270
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-141 |
1.50e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.49 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 20 EIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKhifeKVVGPMGLLKN--KTRILVTHGISYLPQVDV 97
Cdd:PRK15056 139 QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA----RIISLLRELRDegKTMLVSTHNLGSVTEFCD 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907116879 98 IIVMSGGKISEMGSYQ-----ELLDRdgAFAEFLR--TYANAEQDLASEDD 141
Cdd:PRK15056 211 YTVMVKGTVLASGPTEttftaENLEL--AFSGVLRhvALNGSEESIITDDE 259
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-117 |
1.55e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.70 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 29 SGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhvgkHIFEKVVgpmGLLKNKTR------ILVTHGISYLPQV-DVIIVM 101
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDV----SIQAQVV---NLLQQLQRemglslIFIAHDLAVVKHIsDRVLVM 235
|
90
....*....|....*.
gi 1907116879 102 SGGKISEMGSYQELLD 117
Cdd:PRK15079 236 YLGHAVELGTYDEVYH 251
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
28-115 |
1.56e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 44.83 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGI-SYLPQVDVIIVMSGGKI 106
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERV-GVTCVMVTHDQeEAMTMAGRIAIMNRGKF 228
|
....*....
gi 1907116879 107 SEMGSYQEL 115
Cdd:PRK11607 229 VQIGEPEEI 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-105 |
1.58e-04 |
|
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: 42.44 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 3 ACALLPDLEILPSGDRTEIG--EKgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEkvvgpmGLLKN- 79
Cdd:cd03221 47 AGELEPDEGIVTWGSTVKIGyfEQ---LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALE------EALKEy 116
|
90 100
....*....|....*....|....*...
gi 1907116879 80 -KTRILVTHGISYLPQV-DVIIVMSGGK 105
Cdd:cd03221 117 pGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-59 |
1.71e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 1.71e-04
10 20 30
....*....|....*....|....*....|..
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-103 |
1.93e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.94 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGI---SYLpqVDVIIVMSG 103
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAENNEKTAFVVEHDIimiDYL--ADRLIVFEG 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-106 |
2.01e-04 |
|
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: 42.80 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDahVG--KHIFEKVVgpmgLL--KNKTRILVThgiSYLPQV----DVII 99
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VGakAEIYRLIR----ELadAGKAVLLIS---SELDELlglcDRIL 175
|
....*..
gi 1907116879 100 VMSGGKI 106
Cdd:cd03215 176 VMYEGRI 182
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-108 |
2.37e-04 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 43.12 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTHGISYLPQVDV-IIVM 101
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEI-------MELLEeiNRrgtTVLIATHDLELVDRMPKrVLEL 210
|
....*..
gi 1907116879 102 SGGKISE 108
Cdd:COG2884 211 EDGRLVR 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-110 |
2.88e-04 |
|
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: 42.95 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 2 EACALLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMGllKNKT 81
Cdd:cd03264 110 RVDEVLELVNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EERIRFRNLLSELG--EDRI 181
|
90 100 110
....*....|....*....|....*....|....*
gi 1907116879 82 RILVTHGISylpqvDV------IIVMSGGKISEMG 110
Cdd:cd03264 182 VILSTHIVE-----DVeslcnqVAVLNKGKLVFEG 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-116 |
2.99e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIV 100
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQI-------LQLLRelqqelNMGLLFITHNLSIVRKLaDRVAV 229
|
90
....*....|....*.
gi 1907116879 101 MSGGKISEMGSYQELL 116
Cdd:PRK15134 230 MQNGRCVEQNRAATLF 245
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
320-521 |
3.00e-04 |
|
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: 43.56 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 320 FFERTPSGNLVNRFskeLDTVDSMIPQVIKMFMGSLFSVIGAVIII-------LLATPIAAVIIPPLGL-VYFFVQRFyv 391
Cdd:cd18554 96 YYANNRSGEIISRV---INDVEQTKDFITTGLMNIWLDMITIIIAIcimlvlnPKLTFVSLVIFPFYILaVKYFFGRL-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 392 assRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDlkvDENQKAYYPSIVANRWLAVRLECV------GN 465
Cdd:cd18554 171 ---RKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVntitdlAP 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 466 CIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERL 521
Cdd:cd18554 245 LLVIGFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
570-768 |
3.10e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 570 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIaKIGLHNLRFKITIIPQDPVLFSG-SLRMNLDPF 648
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 649 SQY---SDEEVWMALElahlkgfvSALPDK-LNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 724
Cdd:TIGR01257 1028 AQLkgrSWEEAQLEME--------AMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907116879 725 IQSTIRTQFEDCTVLTIAHRLNTI-MDYTRVIVLDKGEVRECGAP 768
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-115 |
3.52e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.47 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLL------KNKTRILVTHGISYLPQ-VDVIIV 100
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM-------MEMFyklhkeKGLTTVLVTHSMEDAARyADQIVV 218
|
90
....*....|....*
gi 1907116879 101 MSGGKISEMGSYQEL 115
Cdd:PRK13634 219 MHKGTVFLQGTPREI 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
312-430 |
3.93e-04 |
|
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: 43.24 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 312 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVI-----------IILLATPIaaVIIPplg 380
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVmlfitspkltlLVLLVIPL--VVLP--- 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907116879 381 lVYFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF--EEQER 430
Cdd:cd18575 153 -IILFGRRVRRLSRASQDRLADLS-----AFAEETLSAIKTVQAFtrEDAER 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-61 |
4.23e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 42.17 E-value: 4.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 3 ACAL-LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 61
Cdd:PRK13539 112 LEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-59 |
4.53e-04 |
|
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: 42.53 E-value: 4.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 5 ALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:cd03218 116 ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-87 |
4.64e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.46 E-value: 4.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTH 87
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD-LLFSLNREHGTTLILVTH 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-110 |
5.42e-04 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 42.13 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 19 TEIGEKG----VNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH----VGKHIFEKVvgpmglLKNKTRILVTHGIS 90
Cdd:cd03220 130 SELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELL------KQGKTVILVSHDPS 203
|
90 100
....*....|....*....|.
gi 1907116879 91 YLPQV-DVIIVMSGGKISEMG 110
Cdd:cd03220 204 SIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
28-116 |
5.69e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.47 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvVGPMGLLKNKtrilvtHGISYLPQV----------DV 97
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL----INLMLELQEK------QGISYIYVTqhlgmmkhisDQ 219
|
90
....*....|....*....
gi 1907116879 98 IIVMSGGKISEMGSYQELL 116
Cdd:PRK15112 220 VLVMHQGEVVERGSTADVL 238
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
285-431 |
5.92e-04 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 42.71 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 285 AAIFG---YSMAVSI-----GGIFA------SRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKM 350
Cdd:cd18590 37 SAIGLmclFSLGSSLsaglrGGLFMctlsrlNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 351 FMGSLFSVIGAVIIIL-----------LATPIAAVIipplglvyffvQRFYVASSRQLKR--LESVSRSPvySHFNETLL 417
Cdd:cd18590 117 LLRSLVKTLGMLGFMLslswqltlltlIEMPLTAIA-----------QKVYNTYHQKLSQavQDSIAKAG--ELAREAVS 183
|
170
....*....|....*...
gi 1907116879 418 GVSVIRAF----EEQERF 431
Cdd:cd18590 184 SIRTVRSFkaeeEEACRY 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
28-135 |
6.85e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.31 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTHGISY-LPQVDVIIVMSGGKI 106
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMD-TLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHV 231
|
90 100
....*....|....*....|....*....
gi 1907116879 107 SEMGSYQElLDRDgAFAEFLRTYANAEQD 135
Cdd:PRK09984 232 FYDGSSQQ-FDNE-RFDHLYRSINRVEEN 258
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
281-390 |
7.47e-04 |
|
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: 42.30 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 281 ILQGAAIFGYSMAVSI-GGIF--ASRRLHL---DLLY-NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMG 353
Cdd:cd18784 40 IIMGLLAIASSVAAGIrGGLFtlAMARLNIrirNLLFrSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907116879 354 SLFSVIGAVIIILLAT---PIAAVIIPPLGlvyFFVQRFY 390
Cdd:cd18784 120 SLVKAIGVIVFMFKLSwqlSLVTLIGLPLI---AIVSKVY 156
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
566-743 |
8.26e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.99 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 566 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFR-INESAEGEIIIDGVNIAKIGLHNlrfkiTIIPQDPVLFsgslrmn 644
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTL-LNLIAgFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 645 ldPFSQYSDEeVWMALELA---HLKGFVSALpDKLNHECAEGGEN-----LSVGQRQLVCLARALLRKTKILVLDEATAA 716
Cdd:PRK11248 83 --PWRNVQDN-VAFGLQLAgveKMQRLEIAH-QMLKKVGLEGAEKryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|....*....
gi 1907116879 717 VDLETDNLIQSTIRTQFEDC--TVLTIAH 743
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETgkQVLLITH 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-124 |
9.62e-04 |
|
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: 42.98 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 25 GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMglLKNKTRILVTHGISYLPQVDVIIVMSGG 104
Cdd:TIGR01271 1351 GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGS 1427
|
90 100
....*....|....*....|
gi 1907116879 105 KISEMGSYQELLDRDGAFAE 124
Cdd:TIGR01271 1428 SVKQYDSIQKLLNETSLFKQ 1447
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-108 |
1.03e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 42.48 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 26 VNLSGGQKQRVSLARAVYSNSDIYLFD------DPlsavdahVGKHIFEKVVGPMglLK--NKTRILVTHGISYLPQVDV 97
Cdd:COG4615 456 TDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVFYTELLPE--LKarGKTVIAISHDDRYFDLADR 526
|
90
....*....|.
gi 1907116879 98 IIVMSGGKISE 108
Cdd:COG4615 527 VLKMDYGKLVE 537
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-118 |
1.12e-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: 42.36 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLKNKTR------ILVTH--GIsylpqV---- 95
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHdlGV-----Vrrfa 224
|
90 100
....*....|....*....|...
gi 1907116879 96 DVIIVMSGGKISEMGSYQELLDR 118
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
286-381 |
1.14e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 41.85 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 286 AIFGYSMAVSIGGIFAS--------------RRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF 351
Cdd:cd18780 44 AVLILLGVVLIGSIATFlrswlftlagervvARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110
....*....|....*....|....*....|....
gi 1907116879 352 MGSLFSVIGAVIIILLA----TPIAAVIIPPLGL 381
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTswklTLVMLSVVPPLSI 157
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-59 |
1.19e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.58 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|...
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-116 |
1.43e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 41.23 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 107
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEII 219
|
....*....
gi 1907116879 108 EMGSYQELL 116
Cdd:PRK13642 220 KEAAPSELF 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
28-122 |
1.44e-03 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 41.75 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKN-KTRILVTHGISYLPQ-VDVIIVMSGGK 105
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV---RRLVDDgKTAVAAIHDLDLAARyCDELVLLADGR 216
|
90 100
....*....|....*....|
gi 1907116879 106 ISEMGSYQELLDRD---GAF 122
Cdd:PRK09536 217 VRAAGPPADVLTADtlrAAF 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-107 |
1.59e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 10 LEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH----VGKHIFEkvvgpmgLLKNKTRILV 85
Cdd:PRK13409 200 LGLENILDR-DISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlnVARLIRE-------LAEGKYVLVV 267
|
90 100 110
....*....|....*....|....*....|
gi 1907116879 86 THGIS---YLpqVDVIIVMSG-----GKIS 107
Cdd:PRK13409 268 EHDLAvldYL--ADNVHIAYGepgayGVVS 295
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-54 |
2.14e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.59 E-value: 2.14e-03
10 20
....*....|....*....|....*...
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDP 54
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-110 |
2.19e-03 |
|
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: 39.61 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 21 IGEKGVNLSGGQKQRVSLARAVYSNSD--IYLFDDPLSAVDaHVGKHIFEKVVGPMGLLKNkTRILVTHGISYLPQVDVI 98
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSSADWI 158
|
90
....*....|....*...
gi 1907116879 99 IVM------SGGKISEMG 110
Cdd:cd03238 159 IDFgpgsgkSGGKVVFSG 176
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
568-773 |
2.27e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.57 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 568 KHI--NVT--IEGGEKVGIVGRTGAGKSSLTLGL-FRINESAE--GEIIIDGVniaKIGLHNLRFKITIIPQDPVL---- 636
Cdd:TIGR00955 38 KHLlkNVSgvAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKgsGSVLLNGM---PIDAKEMRAISAYVQQDDLFiptl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 637 -------FSGSLRMnldPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGenLSVGQRQLVCLARALLRKTKILV 709
Cdd:TIGR00955 115 tvrehlmFQAHLRM---PRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVKG--LSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 710 LDEATAAVDletDNLIQSTIRTQFEDCT-----VLTIAHRLNTIMD-YTRVIVLDKGEVRECGAPSELLQ 773
Cdd:TIGR00955 190 CDEPTSGLD---SFMAYSVVQVLKGLAQkgktiICTIHQPSSELFElFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
27-119 |
2.28e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.56 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFeKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGK 105
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGR 215
|
90
....*....|....
gi 1907116879 106 ISEMGSYQELLDRD 119
Cdd:PRK13652 216 IVAYGTVEEIFLQP 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-118 |
2.30e-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: 40.20 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 25 GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLL-KNKTRILVTH--GISYLPQVDVIIVM 101
Cdd:cd03217 102 NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI---NKLReEGKSVLIITHyqRLLDYIKPDRVHVL 178
|
90
....*....|....*..
gi 1907116879 102 SGGKISEMGSyQELLDR 118
Cdd:cd03217 179 YDGRIVKSGD-KELALE 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-119 |
2.33e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.54 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD-AHVGKHIfeKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGG 104
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVL--ALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGG 224
|
90
....*....|....*
gi 1907116879 105 KISEMGSYQELLDRD 119
Cdd:PRK10575 225 EMIAQGTPAELMRGE 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
28-87 |
2.41e-03 |
|
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: 40.08 E-value: 2.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTH 87
Cdd:cd03292 137 LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI-------MNLLKkiNKagtTVVVATH 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-59 |
2.53e-03 |
|
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: 41.31 E-value: 2.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907116879 10 LEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:COG1245 200 LGLENILDR-DISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
550-712 |
2.54e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.52 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 550 VEFRDycLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGVNIAKI---GLHNLRF 625
Cdd:PRK11831 8 VDMRG--VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTL-LRLIGGQIAPDhGEILFDGENIPAMsrsRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 626 KITIIPQdpvlfSGSLRMNLDPF----------SQYSDE----EVWMALELAHLKGFVSALPDKlnhecaeggenLSVGQ 691
Cdd:PRK11831 85 RMSMLFQ-----SGALFTDMNVFdnvayplrehTQLPAPllhsTVMMKLEAVGLRGAAKLMPSE-----------LSGGM 148
|
170 180
....*....|....*....|.
gi 1907116879 692 RQLVCLARALLRKTKILVLDE 712
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDE 169
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-59 |
3.45e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.88 E-value: 3.45e-03
10 20 30
....*....|....*....|....*....|....*
gi 1907116879 25 GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
582-729 |
3.54e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 582 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGL-------HNLRFKITIIPQDpvlfsgslrmNLDPFSQYSDE 654
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLGLKLEMTVFE----------NLKFWSEIYNS 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 655 EVWMALELAHLKgfvsaLPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 729
Cdd:PRK13541 101 AETLYAAIHYFK-----LHDLLDEKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-115 |
4.16e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFE--KVVG---PMGLlknktrILVTHGISYLPQV-DVIIVM 101
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQkemSMGV------IFITHDMGVVAEIaDRVLVM 242
|
90
....*....|....
gi 1907116879 102 SGGKISEMGSYQEL 115
Cdd:PRK10261 243 YQGEAVETGSVEQI 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-127 |
4.28e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 39.72 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmglLKN--KTRILVTHGISYLPQ-VDVIIVMSGG 104
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDR----LHNqgKTVIVATHDVDLAAEwADQVIVLKEG 214
|
90 100
....*....|....*....|...
gi 1907116879 105 KISEMGSYQELLDRDGAFAEFLR 127
Cdd:PRK13647 215 RVLAEGDKSLLTDEDIVEQAGLR 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-59 |
4.78e-03 |
|
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: 38.67 E-value: 4.78e-03
10 20 30
....*....|....*....|....*....|..
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
28-156 |
5.59e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 39.45 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVG---PMGLlknkTRILVTHGISYLP-QVDVIIVMSG 103
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqkELGL----TIIIATHDIDIVPlYCDNVFVMKE 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907116879 104 GK------ISEMGSYQEL-------LDRDGAFAEFLRTYANAEQDlaSEDDSVSGSGKESKPVENG 156
Cdd:PRK13636 218 GRvilqgnPKEVFAEKEMlrkvnlrLPRIGHLMEILKEKDGFVFD--ELDLTISQARKTLNSWKNK 281
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-59 |
5.77e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 39.24 E-value: 5.77e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1907116879 24 KGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 59
Cdd:COG1137 133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-124 |
6.01e-03 |
|
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: 39.45 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 25 GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMglLKNKTRILVTHGISYLPQVDVIIVMSGG 104
Cdd:cd03289 136 GCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEEN 212
|
90 100
....*....|....*....|
gi 1907116879 105 KISEMGSYQELLDRDGAFAE 124
Cdd:cd03289 213 KVRQYDSIQKLLNEKSHFKQ 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-118 |
6.79e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.91 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIF---EKVV---GPmGLLknktriLVTHGISYLPQV-DVIIV 100
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILdllESIVqkrAL-GML------LVTHDMGVVARLaDDVAV 213
|
90
....*....|....*...
gi 1907116879 101 MSGGKISEMGSYQELLDR 118
Cdd:PRK10418 214 MSHGRIVEQGDVETLFNA 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-60 |
7.08e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 39.92 E-value: 7.08e-03
10 20 30
....*....|....*....|....*....|....
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 60
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-106 |
7.16e-03 |
|
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: 38.40 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvgpmglLKNKTRILVTHGISYLPQ--------VDVII 99
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-------IRTMADVLKTTTFVSLYQasdeiydlFDKVL 191
|
....*..
gi 1907116879 100 VMSGGKI 106
Cdd:cd03233 192 VLYEGRQ 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-61 |
8.46e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 38.25 E-value: 8.46e-03
10 20 30
....*....|....*....|....*....|....
gi 1907116879 28 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 61
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
687-743 |
8.70e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.55 E-value: 8.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907116879 687 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIrTQFEDcTVLTIAH 743
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSH 495
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-106 |
9.56e-03 |
|
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: 38.41 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907116879 27 NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK-----NKTRILVTH--GISYLPQVDVII 99
Cdd:cd03234 143 GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL-------VSTLSqlarrNRIVILTIHqpRSDLFRLFDRIL 215
|
....*..
gi 1907116879 100 VMSGGKI 106
Cdd:cd03234 216 LLSSGEI 222
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
28-87 |
9.71e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 9.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907116879 28 LSGGQKQRVSLARAV----YSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTR-ILVTH 87
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAI---LEHLVKGAQvIVITH 139
|
|
| |
