|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-827 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 671.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 6 GVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLA 85
Cdd:PLN03130 673 ASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMA 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGR 165
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPL 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 166 YAKLIHNLRGLQFKDPEHiyNVAMVETLKESPAQRDEDAVLA-SGDEKDEGKEPETeefvdtnapahQLIQTESPQEGIV 244
Cdd:PLN03130 833 FQKLMENAGKMEEYVEEN--GEEEDDQTSSKPVANGNANNLKkDSSSKKKSKEGKS-----------VLIKQEERETGVV 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 245 TWKTYHTYIKASGGYLVsflVLCLFFLMMGSSAF---STWWLGIWLDRGsqvvcasqnnktacnvdqTLQDTKHHMYQLV 321
Cdd:PLN03130 900 SWKVLERYKNALGGAWV---VMILFLCYVLTEVFrvsSSTWLSEWTDQG------------------TPKTHGPLFYNLI 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 322 YIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQF 401
Cdd:PLN03130 959 YALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQI 1038
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 402 FMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKF 481
Cdd:PLN03130 1039 FQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEIN 1118
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 482 KTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSK-----GLSLSYIIQLSGLLQVCVRTGTE 556
Cdd:PLN03130 1119 GRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAAfastmGLLLSYALNITSLLTAVLRLASL 1198
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 557 TQAKFTSAELLREYI-----LTCVPEHTHPfkvgtcPKDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVG 631
Cdd:PLN03130 1199 AENSLNAVERVGTYIdlpseAPLVIENNRP------PPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVG 1272
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 632 RTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTF 711
Cdd:PLN03130 1273 RTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAH 1352
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 712 MRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR 791
Cdd:PLN03130 1353 LKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHR 1432
|
810 820 830
....*....|....*....|....*....|....*.
gi 1907189171 792 LNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFA 827
Cdd:PLN03130 1433 LNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-836 |
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: 668.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 1 MQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQ 80
Cdd:TIGR00957 688 MDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQ 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 81 RISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECI--KKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKE 158
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 159 LMEERGRYAKLIHN----------------LRGLQFKDPEHIYNVAMVETLKESPAQRDEDAvlASGDEKDEGKE-PETE 221
Cdd:TIGR00957 848 LLQRDGAFAEFLRTyapdeqqghledswtaLVSGEGKEAKLIENGMLVTDVVGKQLQRQLSA--SSSDSGDQSRHhGSSA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 222 EFVDTNAPAH--QLIQTESPQEGIVTWKTYHTYIKASGgYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDrgSQVVCASQN 299
Cdd:TIGR00957 926 ELQKAEAKEEtwKLMEADKAQTGQVELSVYWDYMKAIG-LFITFLSIFLFVCNHVSALASNYWLSLWTD--DPMVNGTQN 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 300 NKTacnvdqtlqdtkhhmYQL-VYIAsmvsvlmFGIIKGFTFTNTTL-------MASSSLHNRVFNKIVRSPMSFFDTTP 371
Cdd:TIGR00957 1003 NTS---------------LRLsVYGA-------LGILQGFAVFGYSMavsiggiQASRVLHQDLLHNKLRSPMSFFERTP 1060
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 372 TGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISR 451
Cdd:TIGR00957 1061 SGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSR 1140
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 452 SPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSISAS 531
Cdd:TIGR00957 1141 SPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAG 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 532 SKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYILTcvpEHTHPFKV-GTCPKD-WPSRGEITFKDYRMRYRDN 609
Cdd:TIGR00957 1221 LVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSET---EKEAPWQIqETAPPSgWPPRGRVEFRNYCLRYRED 1297
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 610 TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVR 689
Cdd:TIGR00957 1298 LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLR 1377
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTD 769
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 770 TLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMllAAEVGL 836
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM--AKDAGL 1522
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-830 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 618.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 8 VAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARA 87
Cdd:PLN03232 675 VVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARA 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 88 VYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYA 167
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 168 KLIHNLRGLqfkDPEHIYNVAMVETLKESP-AQRD-EDAVLASGDEKDEGKEpeteefvdtnapahQLIQTESPQEGIVT 245
Cdd:PLN03232 835 KLMENAGKM---DATQEVNTNDENILKLGPtVTIDvSERNLGSTKQGKRGRS--------------VLVKQEERETGIIS 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 246 WKTYHTYIKASGG-YLVSFLVLCLFFLMMGSSAFSTWwLGIWLDRgsqvvcasqnnktacnvdQTLQDTKHHMYQLVYia 324
Cdd:PLN03232 898 WNVLMRYNKAVGGlWVVMILLVCYLTTEVLRVSSSTW-LSIWTDQ------------------STPKSYSPGFYIVVY-- 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 325 smvSVLMFGIIkGFTFTNT------TLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFL 398
Cdd:PLN03232 957 ---ALLGFGQV-AVTFTNSfwlissSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 399 QQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYdKKDDCI 478
Cdd:PLN03232 1033 NQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRM 1111
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 479 SKF--KTLnDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSF-----SSISASSKGLSLSYIIQLSGLLQVCV 551
Cdd:PLN03232 1112 AKIngKSM-DNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNgnaenQAGFASTMGLLLSYTLNITTLLSGVL 1190
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 552 RTGTETQAKFTSAELLREYI-----LTCVPEHTHPfkvgtcPKDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQT 626
Cdd:PLN03232 1191 RQASKAENSLNSVERVGNYIdlpseATAIIENNRP------VSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEK 1264
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 627 VGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHV 706
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEA 1344
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 707 LERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVL 786
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1907189171 787 TIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLL 830
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-832 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 573.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 2 QLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQR 81
Cdd:PTZ00243 711 EISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKAR 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 82 ISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 161
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 162 ergryAKLIHNLRGLQFKDPEhiynvamvetLKESPAQRDEDAV-LASGDEKDEGKEPETEEFVD-------TNAPAHQL 233
Cdd:PTZ00243 871 -----TSLYATLAAELKENKD----------SKEGDADAEVAEVdAAPGGAVDHEPPVAKQEGNAeggdgaaLDAAAGRL 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 234 IQTESPQEGIVTWKTYHTYIKASGGYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVCASqnnktacnvdqtlqdt 313
Cdd:PTZ00243 936 MTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAAT---------------- 999
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 314 khhmYQLVYIAsMVSVLMFGIIKGFTFTNTTL-MASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPF 392
Cdd:PTZ00243 1000 ----YLYVYLG-IVLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPM 1074
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 393 HAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYD 472
Cdd:PTZ00243 1075 SYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYG 1154
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 473 KKDDCISKFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALL----VTLSFSSISASSKGLSLSYIIQLSGLLQ 548
Cdd:PTZ00243 1155 KAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIgvigTMLRATSQEIGLVSLSLTMAMQTTATLN 1234
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 549 VCVRTGTETQAKFTSAELLREYIL-----------------------------TCVPEHTHPfkVGTCPKDWPSrGEITF 599
Cdd:PTZ00243 1235 WLVRQVATVEADMNSVERLLYYTDevphedmpeldeevdalerrtgmaadvtgTVVIEPASP--TSAAPHPVQA-GSLVF 1311
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 679
Cdd:PTZ00243 1312 EGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQ 1391
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 680 DPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL-RNSKIILLD 758
Cdd:PTZ00243 1392 DPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMD 1471
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 759 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAA 832
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
258-571 |
4.90e-152 |
|
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: 447.78 E-value: 4.90e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 258 GYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVcASQNNKTACNVDQTLQDTKHHMYQLVYIASMVSVLMFGIIKG 337
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNT-TNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 338 FTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPV 417
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 418 VLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNC 497
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 498 ALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 571
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
595-815 |
2.35e-131 |
|
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: 390.70 E-value: 2.35e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 674
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 754
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 755 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP 815
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-813 |
9.53e-128 |
|
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: 417.39 E-value: 9.53e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 5 KGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISL 84
Cdd:TIGR01271 480 EGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 85 ARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 164
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 165 RYAKLIHNL------------------------------------RGLQFKDPEHIYN-----------------VAMVE 191
Cdd:TIGR01271 640 DFSSLLLGLeafdnfsaerrnsiltetlrrvsidgdstvfsgpetIKQSFKQPPPEFAekrkqsiilnpiasarkFSFVQ 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 192 TLKESP-AQRDEDAVLASGD-------EKDEGKEPETEEFVDTNAPAHQ---------LIQTESPQEGIV---------- 244
Cdd:TIGR01271 720 MGPQKAqATTIEDAVREPSErkfslvpEDEQGEESLPRGNQYHHGLQHQaqrrqsvlqLMTHSNRGENRReqlqtsfrkk 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 245 ----------------------------------------------------TWKTYHTYIKASGGyLVSFLVLCLFFLM 272
Cdd:TIGR01271 800 ssitqqnelaseldiysrrlskdsvyeiseeineedlkecfaderenvfettTWNTYLRYITTNRN-LVFVLIFCLVIFL 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 273 MGSSAFstwWLGIWLDRGSQVVCASQNNKTACNVDQTLQ------DTKHHMYQLVYIASMVSVLMFGIIKGFTFTNTTLM 346
Cdd:TIGR01271 879 AEVAAS---LLGLWLITDNPSAPNYVDQQHANASSPDVQkpviitPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLT 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 347 ASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLA 426
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVA 1035
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 427 VIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKF-KTLNDENSSHLLYFNcALRWFALR 505
Cdd:TIGR01271 1036 VIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFhKALNLHTANWFLYLS-TLRWFQMR 1114
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 506 MDILMnIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYIlTCVPEHTHPFKVG 585
Cdd:TIGR01271 1115 IDIIF-VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFI-DLPQEEPRPSGGG 1192
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 586 T--------------CPKDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpA 651
Cdd:TIGR01271 1193 GkyqlstvlvienphAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-T 1271
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 652 SGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENG 731
Cdd:TIGR01271 1272 EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG 1351
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 732 ENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
..
gi 1907189171 812 FD 813
Cdd:TIGR01271 1432 YD 1433
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
320-835 |
1.57e-109 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 347.15 E-value: 1.57e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 320 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 399
Cdd:COG1132 65 LLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 400 QFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCIS 479
Cdd:COG1132 145 SVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 480 KFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSisassKGLS-------LSYIIQLSGLLQVCVR 552
Cdd:COG1132 225 RFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLS-----GSLTvgdlvafILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 553 TGTETQAKFTSAELLREYILTCV----PEHTHPFKvgtcpkdwPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVG 628
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPeipdPPGAVPLP--------PVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 629 IVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHV 706
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGrpDATDEEVEEA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 707 LERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVL 786
Cdd:COG1132 450 AKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTI 529
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1907189171 787 TIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAMLLAAEVG 835
Cdd:COG1132 530 VIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQFG 577
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
591-815 |
3.54e-91 |
|
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: 285.85 E-value: 3.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 591 WPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL 670
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 671 RTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLertfmrdtimklpeklqaEVTENGENFSVGERQLLCMARALLR 750
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 751 NSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP 815
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
320-834 |
5.25e-86 |
|
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: 288.66 E-value: 5.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 320 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSkDMDELDVRLPFHAENFLQ 399
Cdd:COG2274 200 IGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 400 QFFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLRIFHRGVQ-ELKQVENISRSpwFSHITSSIQGLGVIHAYDkkddC 477
Cdd:COG2274 279 DLLFVLIFLIVLFFYsPPLALVVLLLIPLYVLLGLLFQPRLRRlSREESEASAKR--QSLLVETLRGIETIKALG----A 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 478 ISKFKTLNDENSSHLLYFNCALRWFALRMDILMN--------IVTFVVALLV-----TLSFSSISASSKGLSLSYIIQLS 544
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGllqqlatvALLWLGAYLVidgqlTLGQLIAFNILSGRFLAPVAQLI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 545 GLLQvcvrtgtETQAKFTSAELLREyILTCVPEHTHPFKVGTCPKDwpsRGEITFKDYRMRYRDNTPLVLDGLNLNIQSG 624
Cdd:COG2274 433 GLLQ-------RFQDAKIALERLDD-ILDLPPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPG 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 625 QTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL---DPlgSHTDE 701
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 702 MLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK 781
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK 659
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 782 SCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAMLLAAEV 834
Cdd:COG2274 660 GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQL 711
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-149 |
4.26e-85 |
|
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: 269.72 E-value: 4.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 1 MQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQ 80
Cdd:cd03250 55 LEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQ 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 81 RISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGE 149
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
262-571 |
3.70e-83 |
|
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: 267.83 E-value: 3.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 262 SFLVLCLFFLMMGSSAFSTWWLGIWLDRgsqvvcasqnnktacNVDQTLQDTKHHMYqLVYIASMVSVLMFGIIKGFTFT 341
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD---------------WSSSPNSSSGYYLG-VYAALLVLASVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 342 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 421
Cdd:cd18580 65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 422 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 501
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 502 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 571
Cdd:cd18580 225 LGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
595-833 |
3.53e-78 |
|
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: 253.29 E-value: 3.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 674
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 754
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 755 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAE 833
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
349-821 |
8.95e-73 |
|
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: 248.90 E-value: 8.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 349 SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlPFHAeNFLQQFFMVVFI-LVIMAAVFP------VVLVV 421
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALD---GYFA-RYLPQLFLAALVpLLILVAVFPldwlsgLILLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 422 LAGLAVIFLILLRIFHRGVQElKQVENISR-SpwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDE------------- 487
Cdd:COG4988 167 TAPLIPLFMILVGKGAAKASR-RQWRALARlS---GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtmkvlrvaf 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 488 NSShllyfncalrwFALrmDILMNIVTFVVALLVtlsfssisasskGLSLSYI-IQLSGLLQVCV---------RT-GTE 556
Cdd:COG4988 243 LSS-----------AVL--EFFASLSIALVAVYI------------GFRLLGGsLTLFAALFVLLlapefflplRDlGSF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 557 TQAKF---TSAELLREYILTCVPEHTHpfkvGTCPKDWPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRT 633
Cdd:COG4988 298 YHARAngiAAAEKIFALLDAPEPAAPA----GTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 634 GSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTF 711
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR-LGRPdaSDEELEAALEAAG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 712 MRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR 791
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
490 500 510
....*....|....*....|....*....|
gi 1907189171 792 LNTVLNCDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
262-570 |
2.47e-71 |
|
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: 236.61 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 262 SFLVLCLFFLMMGSSAFSTWWLGIWLDrgsqvvcasqnnKTACNVDQTLQDTkhHMYQLVYIASMVSVLMFGIIKGFTFT 341
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSD------------DPALNGTQDTEQR--DYRLGVYGALGLGQAIFVFLGSLALA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 342 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 421
Cdd:cd18603 67 LGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 422 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 501
Cdd:cd18603 147 IIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 502 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 570
Cdd:cd18603 227 LAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
595-821 |
3.23e-70 |
|
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: 230.96 E-value: 3.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 674
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 752
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIR-LGRPnaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 753 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
321-822 |
1.42e-68 |
|
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: 237.74 E-value: 1.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 321 VYIASmVSVLMFGIIKGFT------FT-NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD-----V 388
Cdd:COG4987 54 LFVPI-VGVRAFAIGRTVFrylerlVShDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 389 RLPFHAenflqqFFMVVFILVIMAAVF--PVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLG 466
Cdd:COG4987 133 LLPLLV------ALLVILAAVAFLAFFspALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 467 VIHAYDKKDDCISKFKTLNDENSSHLLyfncALRWFALRMDILMNIVTFVVALLVtLSFSSISASSKGLSLSYII----- 541
Cdd:COG4987 207 ELAAYGALDRALARLDAAEARLAAAQR----RLARLSALAQALLQLAAGLAVVAV-LWLAAPLVAAGALSGPLLAllvla 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 542 ------QLSGLLQVCVRTGtETQAkftSAELLREyILTCVPEHTHPfkvgTCPKDWPSRGEITFKDYRMRYRDNTPLVLD 615
Cdd:COG4987 282 alalfeALAPLPAAAQHLG-RVRA---AARRLNE-LLDAPPAVTEP----AEPAPAPGGPSLELEDVSFRYPGAGRPVLD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 616 GLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL--- 692
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrla 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 772
Cdd:COG4987 433 RP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907189171 773 QSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 822
Cdd:COG4987 511 LADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
263-570 |
3.59e-68 |
|
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: 227.74 E-value: 3.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 263 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVvcaSQNNktacnvdqtlqdtkhhmYQLVYIASMVSVLMFGIIKGFTFTN 342
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDFFGL---SQGF-----------------YIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 343 TTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVL 422
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 423 AGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISK-FKTLNDENSSHLLYFNCAlRW 501
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKnEKLIDNMNRAYFLTIANQ-RW 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 502 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 570
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
263-571 |
2.95e-64 |
|
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: 217.34 E-value: 2.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 263 FLVLCLFFLMMGSSAFSTWWLGIWldrgsqvvcASQNNKTAcnvdqTLQDTKHHM--YQLVYIASMVSVLMFGIIKGFTF 340
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIW---------ASAYETSS-----ALPPSEVSVlyYLGIYALISLLSVLLGTLRYLLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 341 TNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLV 420
Cdd:cd18604 68 FFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 421 VLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALR 500
Cdd:cd18604 148 PAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 501 WFALRMDILMNIVTFVVALLVTLSFSSISASSkGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 571
Cdd:cd18604 228 WLSVRIDLLGALFSFATAALLVYGPGIDAGLA-GFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
258-570 |
5.99e-64 |
|
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: 217.19 E-value: 5.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 258 GYLVSFLVLCLFFLMMGSSAFSTWWLGIW--LDRGSQVVCASQNNKTACNVDQTLQDTKHHMYqlVYIASMVSVLMFGII 335
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLG--IYAGLTAATFVFGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 336 KGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVF 415
Cdd:cd18601 79 RSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 416 PVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYF 495
Cdd:cd18601 159 PWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 496 NCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 570
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
597-808 |
1.72e-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: 207.62 E-value: 1.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIIL 756
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 757 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGK 808
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
597-811 |
2.81e-62 |
|
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: 209.70 E-value: 2.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRY--RDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 674
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 752
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 753 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
597-821 |
5.26e-62 |
|
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: 209.01 E-value: 5.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVGTVRYNL---DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSK 753
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 754 IILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
306-811 |
5.98e-60 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 213.81 E-value: 5.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 306 VDQTLQDTKHHMyqLVYIASMVSVLMfgIIKGFT-FTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 378
Cdd:TIGR02203 41 LDDGFGGRDRSV--LWWVPLVVIGLA--VLRGICsFVSTYLLSWVSnkvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 379 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIM-------AAVFPVVLVVLAGLAVIFLILLRIFHRGVQELK-QVENIs 450
Cdd:TIGR02203 117 ITFDSEQVASAATDAFIVLVRETLTVIGLFIVLlyyswqlTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMgQVTTV- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 451 rspwfshITSSIQGLGVIHAYDKKDDCISKFKTLNDENsshllyfncalRWFALRMD----ILMNIVTFVVA------LL 520
Cdd:TIGR02203 196 -------AEETLQGYRVVKLFGGQAYETRRFDAVSNRN-----------RRLAMKMTsagsISSPITQLIASlalavvLF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 521 VTLSFSSISASSKGLSLSYIIQLsGLLQVCVRTGTETQAKFTSAELLREYILTCVPEHTHPFKvGTCPKDwPSRGEITFK 600
Cdd:TIGR02203 258 IALFQAQAGSLTAGDFTAFITAM-IALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT-GTRAIE-RARGDVEFR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 601 DYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQD 680
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 681 PVLFVGTVRYNL--DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLD 758
Cdd:TIGR02203 415 VVLFNDTIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 759 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
597-811 |
2.45e-57 |
|
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: 196.30 E-value: 2.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVGTVRYNLdPLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 754
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 755 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
593-811 |
5.22e-57 |
|
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: 206.21 E-value: 5.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 593 SRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRT 672
Cdd:COG5265 354 GGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 KLTMIPQDPVLFVGTVRYNL---DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 749
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 750 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
262-571 |
8.54e-55 |
|
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: 191.59 E-value: 8.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 262 SFLVLCLFFLMMGSSAFSTWWLGIWLdrgsqvvcasqnNKTACNVDQTLQDTKHhMYQLVYIASMVSVLMFGIIKGFTFT 341
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV------------SHSNNSFFNFINDSFN-FFLTVYGFLAGLNSLFTLLRAFLFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 342 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 421
Cdd:cd18605 68 YGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 422 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDdcisKFktlNDENSSHLLYFNCAL-- 499
Cdd:cd18605 148 LLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQE----RF---LKEYLEKLENNQRAQla 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 500 -----RWFALRMDILMNIVTFVVALLVTLSFSSISASSK---GLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 571
Cdd:cd18605 221 sqaasQWLSIRLQLLGVLIVTFVALTAVVQHFFGLSIDAgliGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
595-818 |
9.18e-52 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 182.36 E-value: 9.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpASGTIIIDEVDICTVGLEDLRTKL 674
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 754
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 755 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVL 818
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
356-832 |
1.99e-51 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 190.17 E-value: 1.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 356 FNKIVRSPMSFFDTTPTGRLMNRFSKDMDEL-DVRLPFHAENFLQqfFMVVFILVIMAAVFPVVL-VVLAGLAVIFLILL 433
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLAT--LVALVVLLPLALFMNWRLsLVLVVLGIVYTLIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 434 RIFHRGVQELK-QVENiSRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLndenSSHLLYF-NCALRWFAL-----RM 506
Cdd:PRK13657 174 TLVMRKTKDGQaAVEE-HYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDI----ADNLLAAqMPVLSWWALasvlnRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 507 D--ILMNIVTFVVALLVTlsfssisassKG-LSLSYIIQLSGLLQVCVR-----TGTETQAkFTSAELLREY--ILTCVP 576
Cdd:PRK13657 249 AstITMLAILVLGAALVQ----------KGqLRVGEVVAFVGFATLLIGrldqvVAFINQV-FMAAPKLEEFfeVEDAVP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 577 EHTHPFKVGTCPKdwpSRGEITFKDYRMRYrDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTII 656
Cdd:PRK13657 318 DVRDPPGAIDLGR---VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 657 IDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENF 734
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGrpDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 735 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE--- 811
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgs 552
|
490 500
....*....|....*....|.
gi 1907189171 812 FDkpEVLAEkpDSAFAMLLAA 832
Cdd:PRK13657 553 FD--ELVAR--GGRFAALLRA 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
597-811 |
5.64e-51 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 178.83 E-value: 5.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVGTVRYNLdplgSHTDEM--LWHVLERTFM---RDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRN 751
Cdd:cd03252 81 VLQENVLFNRSIRDNI----ALADPGmsMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 752 SKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
263-570 |
1.35e-50 |
|
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: 180.11 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 263 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVCASQNNKtacnvDQTLQDTKHHMYQLVYIA-SMVSVLMFGIIKGFTFT 341
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNIT-----SSSLEDDEVSYYISVYAGlSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 342 nTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 421
Cdd:cd18602 77 -AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 422 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 501
Cdd:cd18602 156 LIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 502 FALRMDILMNIVTFVVAL--LVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 570
Cdd:cd18602 236 LGIRLDYLGAVIVFLAALssLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
321-829 |
1.17e-49 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 186.85 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 321 VYIASMVSVL--MFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFL 398
Cdd:TIGR00958 204 IFFMCLLSIAssVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 399 QQFFMVVFILVIMAAVFP-VVLVVLAGLAVIFLI--LLRIFHRGVQELKQvENISRSPWFS-HITSSIQ--------GLG 466
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPrLTMVTLINLPLVFLAekVFGKRYQLLSEELQ-EAVAKANQVAeEALSGMRtvrsfaaeEGE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 467 VIHAYDKKDDCISKFKTlndENSSHLLYFncalrWFALRMDILMnivtFVVALLVTLSFSSISASSKGLSLSYII---QL 543
Cdd:TIGR00958 363 ASRFKEALEETLQLNKR---KALAYAGYL-----WTTSVLGMLI----QVLVLYYGGQLVLTGKVSSGNLVSFLLyqeQL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 544 SGLLQVCVRTGTETQAKFTSAELLREYIlTCVPEHTHPfkVGTCPKdwPSRGEITFKDYRMRY--RDNTPlVLDGLNLNI 621
Cdd:TIGR00958 431 GEAVRVLSYVYSGMMQAVGASEKVFEYL-DRKPNIPLT--GTLAPL--NLEGLIEFQDVSFSYpnRPDVP-VLKGLTFTL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 622 QSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLD-PLGSHTD 700
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPD 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 701 EMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKeaF 780
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--R 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1907189171 781 KSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAML 829
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-148 |
3.15e-48 |
|
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: 170.20 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 12 GPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYAN 91
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 92 RQLYLLDDPLSAVDAHVGKHVFEECIKKTLKG--KTVVLVTHQLQFLESCDEVILLEDG 148
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
595-810 |
9.07e-48 |
|
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: 168.92 E-value: 9.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 674
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 752
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNIT-LGapLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 753 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVI 810
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-180 |
2.82e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 169.19 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDP 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHn 172
Cdd:COG1132 496 PILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR- 573
|
....*...
gi 1907189171 173 lrgLQFKD 180
Cdd:COG1132 574 ---LQFGE 578
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
351-811 |
3.81e-43 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 166.05 E-value: 3.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 351 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMD---ELDVRLpfhAENFLQQFFMVVFILVIM-----------AAVFP 416
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEvirDLYVTV---VATVLRSAALIGAMLVAMfsldwrmalvaIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 417 VVLVVLAglaviflillrIFHRGVQELkqVENIsRSpWFSHITS----SIQGLGVIHAYDKKddciSKF-KTLNDENSSH 491
Cdd:PRK10790 177 AVLVVMV-----------IYQRYSTPI--VRRV-RA-YLADINDgfneVINGMSVIQQFRQQ----ARFgERMGEASRSH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 492 LLyfncaLRWFALRMD--ILMNIVTFVVALLVTlsfssisasskGLSLSYIIQLSGLLQVCVRTG--------------- 554
Cdd:PRK10790 238 YM-----ARMQTLRLDgfLLRPLLSLFSALILC-----------GLLMLFGFSASGTIEVGVLYAfisylgrlnepliel 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 555 TETQAKFTSAELLREYILTCVPEHTHPFKVGTCPKdwpSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTG 634
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPL---QSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 635 SGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLdPLGSH-TDEMLWHVLERTFMR 713
Cdd:PRK10790 378 SGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRDiSEEQVWQALETVQLA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 714 DTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLN 793
Cdd:PRK10790 457 ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLS 536
|
490
....*....|....*...
gi 1907189171 794 TVLNCDLVLVMENGKVIE 811
Cdd:PRK10790 537 TIVEADTILVLHRGQAVE 554
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-172 |
8.97e-43 |
|
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: 166.55 E-value: 8.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:COG2274 551 IGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNP 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVFeECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 172
Cdd:COG2274 631 RILILDEATSALDAETEAIIL-ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-792 |
9.42e-43 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 163.69 E-value: 9.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 320 LVYIASMVSVLMFGIIKGF-------TFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD---VR 389
Cdd:TIGR02868 50 LYLSVAAVAVRAFGIGRAVfrylerlVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 390 --LPfhaenflqqffMVVFILVIMAAV-------FPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITS 460
Cdd:TIGR02868 130 viVP-----------AGVALVVGAAAVaaiavlsVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 461 SIQGLGVIHAYDKKDDCISKFKtlnDENSSHLLYFNCALRWFALR--MDILMNIVTfVVALLVTLSFSSISASSKGLSLS 538
Cdd:TIGR02868 199 ALDGAAELVASGALPAALAQVE---EADRELTRAERRAAAATALGaaLTLLAAGLA-VLGALWAGGPAVADGRLAPVTLA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 539 YIIqlsgLLQVCVrtgTETQAKFTSA-ELLREYI-----LTCVPEHTHPFKVGTCPKDWPSRGE---ITFKDYRMRYRDN 609
Cdd:TIGR02868 275 VLV----LLPLAA---FEAFAALPAAaQQLTRVRaaaerIVEVLDAAGPVAEGSAPAAGAVGLGkptLELRDLSAGYPGA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 610 TPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVR 689
Cdd:TIGR02868 348 PP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 767
Cdd:TIGR02868 427 ENLR-LARPdaTDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
490 500
....*....|....*....|....*
gi 1907189171 768 TDTLVQSTIKEAFKSCTVLTIAHRL 792
Cdd:TIGR02868 506 TADELLEDLLAALSGRTVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
347-804 |
2.02e-42 |
|
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: 162.46 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 347 ASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVrlpfHAENFLQQFFMVVFI-LVIMAAVFP------VVL 419
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDG----YFARYLPQLVLAVIVpLAILAAVFPqdwisgLIL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 420 VVLAGLAVIFLILLrifhrgvqeLKQVENISRSPWFS------HITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLL 493
Cdd:TIGR02857 151 LLTAPLIPIFMILI---------GWAAQAAARKQWAAlsrlsgHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTM 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 494 YfncalrwfALRMDILMnivTFVVALLVTLSFSSISASSkGLSLSY--IIQLSGLL-------------QVCVRTGTETQ 558
Cdd:TIGR02857 222 R--------VLRIAFLS---SAVLELFATLSVALVAVYI-GFRLLAgdLDLATGLFvlllapefylplrQLGAQYHARAD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 559 AKFTSAELLREYILTCVPEHthpfkvGTCPKDWPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKS 638
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLA------GKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKS 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 639 SLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL---DPLGShtDEMLWHVLERTFMRDT 715
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDAS--DAEIREALERAGLDEF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 716 IMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV 795
Cdd:TIGR02857 441 VAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALA 520
|
....*....
gi 1907189171 796 LNCDLVLVM 804
Cdd:TIGR02857 521 ALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
592-829 |
7.67e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 161.73 E-value: 7.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 592 PSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 671
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKLTMIPQDPVLFVGTVRYNL--DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 749
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 750 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAML 829
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQL 575
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
245-571 |
1.24e-41 |
|
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: 155.35 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 245 TWKTYHTYIKASGGYLVsFLVLCLFFLMMGSSAFSTWwlgIW-LDRGSQVVCASQNNKTACNVDQTLQDTKHHMYQLVYI 323
Cdd:cd18600 2 TWNTYLRYITSHKSLIF-VLILCLVIFAIEVAASLVG---LWlLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 324 ASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFM 403
Cdd:cd18600 78 GVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 404 VVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKF-K 482
Cdd:cd18600 158 VIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFhK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 483 TLNDENSSHLLYFNcALRWFALRMDILMnIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFT 562
Cdd:cd18600 238 ALNLHTANWFLYLS-TLRWFQMRIEMIF-VIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMR 315
|
....*....
gi 1907189171 563 SAELLREYI 571
Cdd:cd18600 316 SVSRIFKFI 324
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-164 |
1.95e-41 |
|
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: 160.31 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:COG4988 413 IAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDA 492
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 164
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
6-170 |
1.78e-40 |
|
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: 150.39 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 6 GVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLA 85
Cdd:cd03291 92 GKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGR 165
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD 251
|
....*
gi 1907189171 166 YAKLI 170
Cdd:cd03291 252 FSSKL 256
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-169 |
2.11e-40 |
|
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: 157.24 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGekynhqRYQHT----VHVC---GLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLAR 86
Cdd:COG4987 411 IAVVPQRPHLFDTTLRENLRLA------RPDATdeelWAALervGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALAR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 87 AVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRY 166
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
...
gi 1907189171 167 AKL 169
Cdd:COG4987 564 RQL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
594-809 |
1.13e-39 |
|
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: 146.46 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 594 RGEITFKDYRMRYRdNTP--LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 671
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKLTMIPQDPVLFVGTVRYNLD-PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLR 750
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 751 NSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKV 809
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
617-835 |
2.62e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.23 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 617 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLdPLG 696
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNV-LLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 697 SH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQS 774
Cdd:PRK11174 447 NPdaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 775 TIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPdSAFAMLLAAEVG 835
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLAHRQE 586
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
605-809 |
1.69e-38 |
|
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: 141.20 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLF 684
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 685 VGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASM 764
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907189171 765 DSKTDTLVQSTIKEA-FKSCTVLTIAHRLNTVLNCDLVLVMENGKV 809
Cdd:cd03246 128 DVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-169 |
1.04e-37 |
|
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: 140.83 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:cd03251 78 IGLVSQDVFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 93 QLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 169
Cdd:cd03251 158 PILILDEATSALDT-ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
597-811 |
9.18e-37 |
|
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: 136.29 E-value: 9.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 676
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIIL 756
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 757 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
592-811 |
1.01e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 146.51 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 592 PSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 671
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKLTMIPQDPVLFVGTVRYNLdPLGSH--TDEMLWHVLERTFMrDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 749
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNL-LLAAPnaSDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 750 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
605-809 |
2.02e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.40 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLF 684
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 685 VGTVRYNLD-PLGSHTDEMLWHVLERTFMRdtiMKLPEK-LQAEVtengENFSVGERQLLCMARALLRNSKIILLDEATA 762
Cdd:COG4619 87 GGTVRDNLPfPFQLRERKFDRERALELLER---LGLPPDiLDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 763 SMDSKTDTLVQSTIKEAFKSC--TVLTIAH------RLntvlnCDLVLVMENGKV 809
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-172 |
5.00e-35 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 133.43 E-value: 5.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGEKYNHQryQHTVHVCGL---QKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYA 90
Cdd:cd03249 79 IGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 91 NRQLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 170
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLV-QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
..
gi 1907189171 171 HN 172
Cdd:cd03249 236 KA 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
597-812 |
3.42e-34 |
|
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: 130.70 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRdntplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 673
Cdd:cd03257 9 VSFPTGGGSVK-----ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQDPVLfvgtvryNLDPL---GSHTDEMLWHVleRTFMRDTIMKLPEKLQAEVTENGEN--------FSVGERQLL 742
Cdd:cd03257 84 IQMVFQDPMS-------SLNPRmtiGEQIAEPLRIH--GKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 743 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 812
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
613-820 |
8.40e-34 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 137.57 E-value: 8.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL 692
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 772
Cdd:COG4618 427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 773 QSTIKEAfKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEF-DKPEVLAE 820
Cdd:COG4618 507 AAAIRAL-KArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
600-832 |
4.37e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 134.65 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTKLTM 676
Cdd:COG1123 268 KRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPV--LF-VGTVRYNL-DPLGSHtdemlwHVLERTFMRDTIMKLPEK--LQAEVTEN--GEnFSVGERQLLCMARAL 748
Cdd:COG1123 347 VFQDPYssLNpRMTVGDIIaEPLRLH------GLLSRAERRERVAELLERvgLPPDLADRypHE-LSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 749 LRNSKIILLDEATASMdsktDTLVQSTIKEAFKS------CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:COG1123 420 ALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
250
....*....|..
gi 1907189171 822 PDSAFA-MLLAA 832
Cdd:COG1123 496 PQHPYTrALLAA 507
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
598-808 |
4.68e-33 |
|
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: 125.05 E-value: 4.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 598 TFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMI 677
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 678 PQdpvlfvgtvrynldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILL 757
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 758 DEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGK 808
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-806 |
1.85e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.31 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 56 LNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKT---LKG---KTVVLV 129
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----EYLVQKTinnLKGnenRITIII 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 130 THQLQFLESCDEVILLEDGE-----------------------------------------------ICEKGTHKELMEE 162
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKN 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 163 R-GRYAKLIHNLRglqfkdpehiynvamVETLKESPAQRDEDAVLASGDEKDE--GKEPE-----------------TEE 222
Cdd:PTZ00265 717 KnGIYYTMINNQK---------------VSSKKSSNNDNDKDSDMKSSAYKDSerGYDPDemngnskhenesasnkkSCK 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 223 FVDTNAPAHQL------------IQTESPQEGIVTWKTYHTYIKASGGYLVSFLV---LCLFFLMMGSSAFSTWWLGIWL 287
Cdd:PTZ00265 782 MSDENASENNAggklpflrnlfkRKPKAPNNLRIVYREIFSYKKDVTIIALSILVaggLYPVFALLYAKYVSTLFDFANL 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 288 DRGSQvvcasqnnktacnvdqtlqdtKHHMYQLVyiasmVSVLMF--GIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMS 365
Cdd:PTZ00265 862 EANSN---------------------KYSLYILV-----IAIAMFisETLKNYYNNVIGEKVEKTMKRRLFENILYQEIS 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 366 FFDT---TPtGRLMNRFSKDMDELDVRLPFHAENFlQQFFMVVFILVIMAAVF-PVVLVVLAGLAVIFLILLRIFHRgVQ 441
Cdd:PTZ00265 916 FFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIF-THFIVLFLVSMVMSFYFcPIVAAVLTGTYFIFMRVFAIRAR-LT 992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 442 ELKQVEN-----------------ISRSPWFShITSSIQGLGVIHAYDKKD---DCISKFKTLNDENSSHLLYFNCALRW 501
Cdd:PTZ00265 993 ANKDVEKkeinqpgtvfaynsddeIFKDPSFL-IQEAFYNMNTVIIYGLEDyfcNLIEKAIDYSNKGQKRKTLVNSMLWG 1071
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 502 FALRMDILMNIVTFVV-ALLVTLSFSSISASSKGLsLSYIIQLSGLLQVCVRTGTETQAKFTsaeLLREYILTCVPEHTH 580
Cdd:PTZ00265 1072 FSQSAQLFINSFAYWFgSFLIRRGTILVDDFMKSL-FTFLFTGSYAGKLMSLKGDSENAKLS---FEKYYPLIIRKSNID 1147
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 581 PFKVG--TCPKDWPSRGEITFKDYRMRY--RDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--------- 647
Cdd:PTZ00265 1148 VRDNGgiRIKNKNDIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhi 1226
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 648 ---------------------------------------------VEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPV 682
Cdd:PTZ00265 1227 vfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPM 1306
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 LFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEA 760
Cdd:PTZ00265 1307 LFNMSIYENIK-FGKEdaTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEA 1385
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1907189171 761 TASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLNCDLVLVMEN 806
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-169 |
2.56e-32 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 125.42 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 169
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
614-762 |
3.63e-32 |
|
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: 121.99 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVG-TVRYNL 692
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 693 -------DPLGSHTDEMLWHVLERtfmrdtiMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATA 762
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-164 |
4.48e-32 |
|
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: 124.65 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGEKYNHQ-RYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 164
Cdd:cd03254 159 KILILDEATSNIDTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-180 |
1.11e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 130.99 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGE--KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYAN 91
Cdd:TIGR02203 408 VALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 92 RQLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiH 171
Cdd:TIGR02203 488 APILILDEATSALDNESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL-H 565
|
....*....
gi 1907189171 172 NlrgLQFKD 180
Cdd:TIGR02203 566 N---MQFRE 571
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
600-832 |
2.51e-31 |
|
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: 122.99 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 679
Cdd:COG1124 9 VSYGQGGRRVP--VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 680 DPVLFV---GTVRYNLD-PLGSH----TDEMLWHVLERTFMRDTIM-KLPEKLqaevtengenfSVGERQLLCMARALLR 750
Cdd:COG1124 87 DPYASLhprHTVDRILAePLRIHglpdREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 751 NSKIILLDEATASMdsktDTLVQSTI-------KEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKP 822
Cdd:COG1124 156 EPELLLLDEPTSAL----DVSVQAEIlnllkdlREERGL-TYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|.
gi 1907189171 823 DSAFA-MLLAA 832
Cdd:COG1124 231 KHPYTrELLAA 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
597-818 |
3.03e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 122.29 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICT--VGLED 669
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQDPVLFVGTVRYNLDpLGshtdemLWHVLERTfmRDTIMKLPEK------LQAEVTE--NGENFSVGERQL 741
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YG------LRLHGIKL--KEELDERVEEalrkaaLWDEVKDrlHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 742 LCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVL 818
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
599-808 |
5.83e-31 |
|
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: 120.65 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 599 FKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIP 678
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 679 QDP--VLFVGTVR----YNLDPLGSHTDEM---LWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALL 749
Cdd:cd03225 82 QNPddQFFGPTVEeevaFGLENLGLPEEEIeerVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 750 RNSKIILLDEATASMDSKTDTLVQSTIKEaFKSC--TVLTIAHRLNTVLN-CDLVLVMENGK 808
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-169 |
1.07e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 121.05 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNIALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 93 QLYLLDDPLSAVDaHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 169
Cdd:cd03252 158 RILIFDEATSALD-YESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-172 |
1.81e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 127.65 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGEK-YNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:PRK11174 425 LSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPC 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVFeECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 172
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-150 |
4.00e-30 |
|
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: 118.85 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 16 YVSQQAWIFHGNVRENILFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQL 94
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 95 YLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
594-822 |
6.54e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.60 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 594 RGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTK 673
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQDPVLFVGTVRYNLdPLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRN 751
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNI-ALGrpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 752 SKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 822
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
597-835 |
7.62e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.33 E-value: 7.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDP-VLFVG-TVR---------YNLDPlgSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMA 745
Cdd:PRK13632 88 IFQNPdNQFIGaTVEddiafglenKKVPP--KKMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 746 RALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP-EVLAEKP 822
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNKE 234
|
250 260
....*....|....*....|
gi 1907189171 823 -------DSAFAMLLAAEVG 835
Cdd:PRK13632 235 ilekakiDSPFIYKLSKKLK 254
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
597-834 |
9.33e-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: 124.63 E-value: 9.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK 673
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQDPvlfvgtvRYNLDPL--GSHTDEMLW-HVLERTFMRDTIMKLPEK--LQAEVTENGENFSVGERQLLCMARAL 748
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVtvGDQIAEALEnLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 749 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIE-------FDKPEVL 818
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEdgppeeiLAAPQAL 237
|
250
....*....|....*.
gi 1907189171 819 AEKPDSAFAMLLAAEV 834
Cdd:COG1123 238 AAVPRLGAARGRAAPA 253
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-169 |
1.43e-29 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 125.63 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIFHGNVRENILFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLY 95
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIALCNpGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRIL 615
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 96 LLDDPLSAVDAHvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 169
Cdd:TIGR01846 616 IFDEATSALDYE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
264-547 |
2.99e-29 |
|
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: 117.74 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 264 LVLCLFFLMMGS--SAFSTWWLGIWLDrgsqvvcasqnnktACNVDQTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFT 341
Cdd:pfam00664 1 LILAILLAILSGaiSPAFPLVLGRILD--------------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 342 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 421
Cdd:pfam00664 67 HTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 422 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 501
Cdd:pfam00664 147 LLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907189171 502 FALRMDILMNIVTFVVALLVTLSFSSISASSKGL--SLSYIIQLSGLL 547
Cdd:pfam00664 227 SFGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-145 |
4.52e-29 |
|
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: 122.40 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 6 GVVAVNG-PL------------AYVSQQAWIFHGNVRENILFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERG 71
Cdd:TIGR02857 377 GSIAVNGvPLadadadswrdqiAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGG 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 72 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILL 145
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-170 |
3.40e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.37 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQ 93
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 94 LYLLDDPLSAVDAHVGKHVFEEcikKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 170
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
14-178 |
5.88e-28 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 119.80 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-------EKYNHQRYQHTvhvcglQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLAR 86
Cdd:TIGR02204 416 MALVPQDPVLFAASVMENIRYGrpdatdeEVEAAARAAHA------HEFISALPEGYDTYLGERGVTLSGGQRQRIAIAR 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 87 AVYANRQLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRY 166
Cdd:TIGR02204 490 AILKDAPILLLDEATSALDAESEQLV-QQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLY 568
|
170
....*....|..
gi 1907189171 167 AKLIHnlrgLQF 178
Cdd:TIGR02204 569 ARLAR----LQF 576
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
597-818 |
1.72e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 112.06 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVG-TV-------RYN-LDPLGSHTDE---MLWHVLERTfmrdtimKLPEKLQAEVTEngenFSVGERQLLCM 744
Cdd:COG1120 80 VPQEPPAPFGlTVrelvalgRYPhLGLFGRPSAEdreAVEEALERT-------GLEHLADRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 745 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVL 818
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-149 |
1.79e-27 |
|
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: 109.39 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILfgekynhqryqhtvhvcglqkdlnslpygdlteigergvnlSGGQRQRISLARAVYANRQ 93
Cdd:cd03228 78 IAYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPP 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 94 LYLLDDPLSAVDAHvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGE 149
Cdd:cd03228 117 ILILDEATSALDPE-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
613-808 |
3.85e-27 |
|
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: 108.81 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG--LEDLRTKLTMIPQDPVLFVG-TVR 689
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLdplgshtdemlwhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTD 769
Cdd:cd03229 95 ENI--------------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907189171 770 TLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGK 808
Cdd:cd03229 137 REVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-178 |
4.88e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 117.04 E-value: 4.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIFHGNVRENILF--GEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 93 QLYLLDDPLSAVDAHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAK 168
Cdd:PRK11176 500 PILILDEATSALDTES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
170
....*....|
gi 1907189171 169 LiHNlrgLQF 178
Cdd:PRK11176 575 L-HK---MQF 580
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-171 |
3.31e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 114.04 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 93 QLYLLDDPLSAVDAHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAK 168
Cdd:PRK10789 471 EILILDDALSAVDGRT-----EHQILHNLrqwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRD 545
|
...
gi 1907189171 169 LIH 171
Cdd:PRK10789 546 MYR 548
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
597-823 |
5.92e-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: 107.20 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 673
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQDPVLFVG-TVRYNLD-PLGSHTDEMLWHVLERTFM-------RDTIMKLPEKLqaevtengenfSVGERQLLCM 744
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTRLSEEEIREIVLEkleavglRGAEDLYPAEL-----------SGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 745 ARALLRNSKIILLDEATASMDSKTDTLVQSTI---KEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAE 820
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIrslKKELG-LTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 1907189171 821 KPD 823
Cdd:cd03261 227 SDD 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
610-808 |
7.96e-26 |
|
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: 105.63 E-value: 7.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 610 TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIdevdICTVGLedlrtkltmIPQDPVLFVGTVR 689
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV----PGSIAY---------VSQEPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLdpLGSHT--DEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 767
Cdd:cd03250 84 ENI--LFGKPfdEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907189171 768 T-DTLVQSTIKEAFKSC-TVLTIAHRLNTVLNCDLVLVMENGK 808
Cdd:cd03250 162 VgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-172 |
1.09e-25 |
|
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: 113.30 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 16 YVSQQAWIFHGNVRENILFGEKYN--HQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQ 93
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 94 LYLLDDPLSAVDAHVGKHVFEECIKktLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 172
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-171 |
1.13e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 113.50 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 2 QLQKGVVAvnGPLAYVSQQAWIFHGNVRENI-LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQ 80
Cdd:TIGR03796 545 EIPREVLA--NSVAMVDQDIFLFEGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 81 RISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKtlKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM 160
Cdd:TIGR03796 623 RLEIARALVRNPSILILDEATSALDPETEKIIDDN-LRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELW 699
|
170
....*....|.
gi 1907189171 161 EERGRYAKLIH 171
Cdd:TIGR03796 700 AVGGAYARLIR 710
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
589-822 |
1.33e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 113.97 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 589 KDWPSRGEITFKDYRMRY--RDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-DEVDICTV 665
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYdtRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 666 GLEDLRTKLTMIPQDPVLFVGTVRYNL-------------------------------------------DPLGSHTDEM 702
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgndsqenknkrnscrakcagdlnDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 703 LWH---------------VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 767
Cdd:PTZ00265 534 LIEmrknyqtikdsevvdVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 768 TDTLVQSTIK--EAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 822
Cdd:PTZ00265 614 SEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
600-810 |
5.26e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 102.51 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 679
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 680 dpvlfvgtvryNLDPLGshtdemLWHVLERTFMRdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDE 759
Cdd:cd03214 81 -----------ALELLG------LAHLADRPFNE--------------------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 760 ATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVI 810
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
597-816 |
1.11e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.71 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 747
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddVAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 748 LLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPE 816
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
597-823 |
1.32e-24 |
|
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: 103.52 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 673
Cdd:COG1127 6 IEVRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQDPVLFVG-TVRYNLD-PLGSHTD-------EMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGerqllcM 744
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHTDlseaeirELVLEKLELVGLPGAADKMPSEL-----------SGG------M 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 745 ------ARALLRNSKIILLDEATASMD----SKTDTLVQsTIKEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 813
Cdd:COG1127 147 rkrvalARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDELG-LTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
250
....*....|
gi 1907189171 814 KPEVLAEKPD 823
Cdd:COG1127 225 TPEELLASDD 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
597-811 |
2.07e-24 |
|
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: 102.66 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIIIDEVDICTV---GLEDL 670
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 671 RTKLTMIPQDPVLFVG-TVRYNLD-PL------GSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLL 742
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 743 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
597-815 |
6.04e-24 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 101.49 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 673
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQDpvlfvgtvrYNLDP------------LGSHTdemLWHVLERTFMRDTIMK---------LPEKLQAEVTEnge 732
Cdd:cd03256 80 IGMIFQQ---------FNLIErlsvlenvlsgrLGRRS---TWRSLFGLFPKEEKQRalaalervgLLDKAYQRADQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 733 nFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVL-NCDLVLVMENGKV 809
Cdd:cd03256 145 -LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAReYADRIVGLKDGRI 223
|
....*.
gi 1907189171 810 IeFDKP 815
Cdd:cd03256 224 V-FDGP 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
597-813 |
6.73e-24 |
|
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: 100.67 E-value: 6.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdlRTKLTM 676
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLF-----VGTVRYNLDPLGSHTDEMLWHVLERTFMrdtiMKLPEKLQAEVTEngenFSVGERQLLCMARALLRN 751
Cdd:cd03259 77 VFQDYALFphltvAENIAFGLKLRGVPKAEIRARVRELLEL----VGLEGLLNRYPHE----LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 752 SKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 813
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
597-810 |
1.33e-23 |
|
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: 99.89 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTvGLEDLRTKLTM 676
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVG-TVRYNLD---PLGSHTDEMLWHVLERTFmrdTIMKLPEKLQAEVTengeNFSVGERQLLCMARALLRNS 752
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyaRLKGLPKSEIKEEVELLL---RVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 753 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 810
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-173 |
1.91e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.68 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTeIGERGVNLSGGQRQRISLARAVYANRQLY 95
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAaPNASDEALIEVLQQVGLEKLLEDDKGLNAW-LGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 96 LLDDPLSAVDAHVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNL 173
Cdd:PRK11160 498 LLDEPTEGLDAETERQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
613-811 |
1.09e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 99.74 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTVGLEDLRT----KLTMIPQD----- 680
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 681 -PVLfvgTVRYNL-DPLGSHTD-----------EMlwhvLERTFMRDtimklPEKL------QaevtengenFSVGERQL 741
Cdd:COG0444 100 nPVM---TVGDQIaEPLRIHGGlskaeareraiEL----LERVGLPD-----PERRldryphE---------LSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 742 LCMARALLRNSKIILLDEATASMdsktDTLVQSTI-------KEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTAL----DVTIQAQIlnllkdlQRELG-LAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
597-820 |
1.34e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.85 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvglEDLRTKLTM 676
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQD-------PVL---FVGTVRYN----LDPLGSHTDEMLWHVLERT----FMRDTIMKLpeklqaevtengenfSVGE 738
Cdd:COG1121 80 VPQRaevdwdfPITvrdVVLMGRYGrrglFRRPSRADREAVDEALERVgledLADRPIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 739 RQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMeNGKVIEFDKP- 815
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPe 223
|
....*
gi 1907189171 816 EVLAE 820
Cdd:COG1121 224 EVLTP 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
613-820 |
1.43e-22 |
|
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: 97.12 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPVLFVG-TVRY 690
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 691 NLDpLGSHT------DEMLWHVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCMARALLRNSKIILLDEATASM 764
Cdd:cd03224 95 NLL-LGAYArrrakrKARLERVYEL-FPR-----LKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 765 DSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAE 820
Cdd:cd03224 164 APKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
597-809 |
2.31e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 96.40 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYR--DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIIIDEVDICTVGLEDL--- 670
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 671 -RTKLTMIPQD----PVLfvgTVRYNLD-PL------GSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGE 738
Cdd:cd03255 80 rRRHIGFVFQSfnllPDL---TALENVElPLllagvpKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 739 RQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKV 809
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
595-791 |
3.04e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPLVlDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIIIDEVDictvgledl 670
Cdd:COG4178 361 GALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIARPAGA--------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 671 rtKLTMIPQDPVLFVGTVR----YNLDPlGSHTDEMLWHVLERTFMRDtimkLPEKLQAEvtENGEN-FSVGERQLLCMA 745
Cdd:COG4178 427 --RVLFLPQRPYLPLGTLReallYPATA-EAFSDAELREALEAVGLGH----LAERLDEE--ADWDQvLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907189171 746 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR 791
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
597-824 |
3.98e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.13 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPV-LFVG-TVRYN----LDPLGSHTDEM---LWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 747
Cdd:PRK13648 88 VFQNPDnQFVGsIVKYDvafgLENHAVPYDEMhrrVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 748 LLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDS 824
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
262-571 |
5.77e-22 |
|
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: 96.90 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 262 SFLVLCLFFLMMGSSAFSTWWLGIWLDRgsqvvcasqnnktacNVDQTLQDTkhHMYQLVYIASMVS--VLMFGIikGFT 339
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDD---------------PVNGPQEHG--QVYLSVLGALAILqgITVFQY--SMA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 340 FTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVL 419
Cdd:cd18559 62 VSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 420 VVLAgLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFnCAL 499
Cdd:cd18559 142 VGIP-LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSI-VYL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 500 RWFALRMDILMNIVTFVVALLVTLSFSSISASSkGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 571
Cdd:cd18559 220 RALAVRLWCVGPCIVLFASFFAYVSRHSLAGLV-ALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
58-169 |
6.44e-22 |
|
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: 101.05 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 58 SLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKTL----KGKTVVLVTHQL 133
Cdd:COG5265 479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT-----ERAIQAALrevaRGRTTLVIAHRL 553
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907189171 134 QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 169
Cdd:COG5265 554 STIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-162 |
1.29e-21 |
|
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: 99.73 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 16 YVSQQAWIFHGNVRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQL 94
Cdd:TIGR01842 396 YLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKL 475
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 95 YLLDDPLSAVDAhVGKHVFEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 162
Cdd:TIGR01842 476 VVLDEPNSNLDE-EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
613-834 |
2.84e-21 |
|
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: 93.55 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdlRTKLTMIPQDPVLFVG-TVRYN 691
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 692 LDplgshtdemlWHVLERTFMRDTI----MKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 765
Cdd:cd03299 92 IA----------YGLKKRKVDKKEIerkvLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 766 SKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSAF-AMLLAAEV 834
Cdd:cd03299 162 VRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFvAEFLGFNN 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
613-810 |
2.61e-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: 88.64 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQdpvlfvgtvryn 691
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 692 ldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASMDSK-TDT 770
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907189171 771 LVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVI 810
Cdd:cd03216 121 LFK-VIRR-LRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
599-810 |
2.81e-20 |
|
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: 89.90 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 599 FKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdicTVGLEDLRTKLTMIP 678
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 679 QD-------PVL---FVGTVRYN----LDPLGSHTDEMLWHVLERTFMRDtimklpeKLQAEVTEngenFSVGERQLLCM 744
Cdd:cd03235 75 QRrsidrdfPISvrdVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSE-------LADRQIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 745 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMeNGKVI 810
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-155 |
3.24e-20 |
|
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: 90.25 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENI-LFGEKYNHQRYQhTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 155
Cdd:cd03244 159 KILVLDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
597-818 |
4.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.33 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDN-TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLT 675
Cdd:PRK13650 5 IEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 676 MIPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMAR 746
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLENKGIPHEEMKERVneaLELVGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 747 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVL 818
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-150 |
5.18e-20 |
|
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: 89.84 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 2 QLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEI 67
Cdd:cd03248 65 QPQGGQVLLDGkPIsqyehkylhskvSLVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 68 GERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLED 147
Cdd:cd03248 145 GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
...
gi 1907189171 148 GEI 150
Cdd:cd03248 224 GRI 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
614-807 |
5.52e-20 |
|
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: 89.31 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTK----LTMIPQDPVLFVGTVR 689
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLdPLGSHTDEMLWH-VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK- 767
Cdd:cd03290 97 ENI-TFGSPFNKQRYKaVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907189171 768 TDTLVQSTIKEAFK--SCTVLTIAHRLNTVLNCDLVLVMENG 807
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
58-150 |
7.01e-20 |
|
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: 94.43 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 58 SLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKtLK--GKTVVLVTHQLQF 135
Cdd:COG4618 452 RLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIRA-LKarGATVVVITHRPSL 529
|
90
....*....|....*
gi 1907189171 136 LESCDEVILLEDGEI 150
Cdd:COG4618 530 LAAVDKLLVLRDGRV 544
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
614-816 |
7.13e-20 |
|
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: 93.98 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPvlfvgtvrY 690
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--------F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 691 N-LDP-----------LGSH--------TDEMLWHVLERTFM-RDTIMKLP-EklqaevtengenFSVGERQLLCMARAL 748
Cdd:COG4172 373 GsLSPrmtvgqiiaegLRVHgpglsaaeRRARVAEALEEVGLdPAARHRYPhE------------FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 749 LRNSKIILLDEATASMD-SktdtlVQSTIKEAFKSC------TVLTIAHRLNTV--LnCDLVLVMENGKVIE-------F 812
Cdd:COG4172 441 ILEPKLLVLDEPTSALDvS-----VQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVEqgpteqvF 514
|
....
gi 1907189171 813 DKPE 816
Cdd:COG4172 515 DAPQ 518
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-150 |
9.00e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 88.51 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIF-HGNVRENILFGEKYnHQRYQHTVHVcglQKDLNSLpygDLTEIGERGV-NLSGGQRQRISLARAVYANR 92
Cdd:cd03297 78 GLVFQQYALFpHLNVRENLAFGLKR-KRNREDRISV---DELLDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQP 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVFEEC--IKKTLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELkqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
9-171 |
1.17e-19 |
|
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: 94.25 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 9 AVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAV 88
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 89 YANRQLYLLDDPLSAVDAHVGKHVFEECikKTLKGkTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAK 168
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESL--ERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ 680
|
...
gi 1907189171 169 LIH 171
Cdd:TIGR03797 681 LAR 683
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
606-820 |
1.29e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 606 YRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC--TVGLEDLRTKLTMIPQD 680
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 681 P--VLFVGTVR----YNLDPLGSHTDEMLWHVLERtfmrdtiMKLPeKLQAEVTENGENF--SVGERQLLCMARALLRNS 752
Cdd:PRK13637 92 PeyQLFEETIEkdiaFGPINLGLSEEEIENRVKRA-------MNIV-GLDYEDYKDKSPFelSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 753 KIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 820
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPrEVFKE 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
597-811 |
1.40e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRTK 673
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQD-PVLFVGTVRYNLD-PL---GSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMA 745
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENVAlPLrvtGKSRKEIRRRVrevLDLVGLSDKAKALPHEL-----------SGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 746 RALLRNSKIILLDEATASMDSKTdtlvqST-IKEAFKS-----CTVLtIA-HRLNTVLNCDL-VLVMENGKVIE 811
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPET-----SWeIMELLEEinrrgTTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
597-821 |
1.89e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKL 674
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDP--VLFVGTV----RYNLDPLGSHTDEM---LWHVLERTFMrdtimklpEKLQAEVTengENFSVGERQLLCMA 745
Cdd:PRK13636 85 GMVFQDPdnQLFSASVyqdvSFGAVNLKLPEDEVrkrVDNALKRTGI--------EHLKDKPT---HCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 746 RALLRNSKIILLDEATASMD----SKTDTLVQSTIKEAfkSCTVLTIAHRLNTV-LNCDLVLVMENGKVI-EFDKPEVLA 819
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVpLYCDNVFVMKEGRVIlQGNPKEVFA 231
|
..
gi 1907189171 820 EK 821
Cdd:PRK13636 232 EK 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
597-810 |
2.10e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNT----PLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG-LEDLR 671
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKLTMIPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLL 742
Cdd:PRK13633 85 NKAGMVFQNPdNQIVATiveedVAFGPENLGIPPEEIRERVdesLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 743 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLNCDLVLVMENGKVI 810
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-150 |
3.87e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.79 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIFHGNVRENILFGEKYNHQRYQHTvHVCGLQKDLNsLPYGDLteigERGV-NLSGGQRQRISLARAVYANRQ 93
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFPFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPD 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 94 LYLLDDPLSAVDAHvGKHVFEECIKKTL--KGKTVVLVTH-QLQFLESCDEVILLEDGEI 150
Cdd:COG4619 151 VLLLDEPTSALDPE-NTRRVEELLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
597-791 |
5.91e-19 |
|
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: 84.90 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdictvgledlRTKLTM 676
Cdd:cd03223 1 IELENLSLATPDGRVLLKD-LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVGTVRynldplgshtdEML---WhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSK 753
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907189171 754 IILLDEATASMDSKTDTLVQSTIKEAFksCTVLTIAHR 791
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
613-810 |
6.39e-19 |
|
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: 86.72 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEVDICTVGlEDLRTKLTMIP--QDPVLFVG 686
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 687 -TVRYNLD----PLGSHTDEMLWHVLERTFMRDTIMKLPE--KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDE 759
Cdd:cd03219 90 lTVLENVMvaaqARTGSGLLLARARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 760 ATASMDSK-TDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 810
Cdd:cd03219 170 PAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
606-836 |
8.10e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 606 YRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG-LEDLRTKLTMIPQDP-VL 683
Cdd:PRK13644 11 YPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 684 FVG-TVRYNLdplgSHTDEMLwhVLERTFMRDTI-MKLPE-KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEA 760
Cdd:PRK13644 90 FVGrTVEEDL----AFGPENL--CLPPIEIRKRVdRALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 761 TASMDSKTDTLVQSTIKEAF-KSCTVLTIAHRLNTVLNCDLVLVMENGKViefdkpeVLAEKPDSAFAMLLAAEVGL 836
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKI-------VLEGEPENVLSDVSLQTLGL 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
597-826 |
8.16e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 86.59 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVlDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFvgtvrynldPlgsHtdemlWHVLERTFMRDTIMKLP-EKLQAEVTE-------NGENF--------SVGERQ 740
Cdd:cd03295 80 VIQQIGLF---------P---H-----MTVEENIALVPKLLKWPkEKIRERADEllalvglDPAEFadryphelSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 741 LLCMARALLRNSKIILLDEATASMDSKTDTLVQS---TIKEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 816
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEefkRLQQELGK-TIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPD 221
|
250
....*....|
gi 1907189171 817 VLAEKPDSAF 826
Cdd:cd03295 222 EILRSPANDF 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
597-811 |
8.84e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.70 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRT-- 672
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 -KLTMIPQdpvlfvgtvRYNLdpLGSHTdemlwhVLERTFMRDTIMKLP-EKLQAEVTENGE-------------NFSVG 737
Cdd:PRK11153 82 rQIGMIFQ---------HFNL--LSSRT------VFDNVALPLELAGTPkAEIKARVTELLElvglsdkadrypaQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 738 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
597-810 |
1.33e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 85.50 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDN--TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdLRTKL 674
Cdd:cd03266 2 ITADALTKRFRDVkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVG-TVRYNLDPLGShtdemlWHVLERTFMRDTIMKLPEKLQAEVTEN--GENFSVGERQLLCMARALLRN 751
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAG------LYGLKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 752 SKIILLDEATASMdsktDTLVQSTIKEAFKS-----CTVLTIAHRLNTVLN-CDLVLVMENGKVI 810
Cdd:cd03266 155 PPVLLLDEPTTGL----DVMATRALREFIRQlralgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
74-149 |
1.80e-18 |
|
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: 83.06 E-value: 1.80e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLE-SCDEVILLEDGE 149
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
597-822 |
1.83e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTVGLEDLRTK 673
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 674 LTMIPQDP-VLFVGT-----VRYNLDPLGSHTDEML---WHVLERTFMRDTIMKLPeklqaevtengENFSVGERQLLCM 744
Cdd:PRK13640 86 VGIVFQNPdNQFVGAtvgddVAFGLENRAVPRPEMIkivRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 745 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 822
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
14-170 |
2.64e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 89.56 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANR 92
Cdd:TIGR01192 411 IATVFQDAGLFNRSIRENIRLGrEGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNA 490
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 93 QLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 170
Cdd:TIGR01192 491 PILVLDEATSALDVETEARV-KNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
318-520 |
2.73e-18 |
|
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: 86.07 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 318 YQLVYIASMVSVLMFGIIKGFTFTNTTLMASSSLH------NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLP 391
Cdd:cd07346 35 LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRvvfdlrRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 392 FHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQEL-----KQVENISrspwfSHITSSIQGLG 466
Cdd:cd07346 115 SGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKAsrevrESLAELS-----AFLQESLSGIR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 467 VIHAYDKKDDCISKFKTLNDENSSHLLYfncALRWFAL---RMDILMNIVTFVVALL 520
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLR---AARLSALfspLIGLLTALGTALVLLY 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
597-809 |
2.75e-18 |
|
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: 84.38 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICtvGLED-----LR 671
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKLTMIPQDPVLFVG-TVRYNL-------DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLC 743
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVafalevtGVPPREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 744 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNC--DLVLVMENGKV 809
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-162 |
4.15e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 84.34 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAwIFHGN--VRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLpygdlteIGergvNLSGGQRQRISL 84
Cdd:COG1131 75 IGYVPQEP-ALYPDltVRENLRFfarlyglPRKEARERIDELLELFGLTDAADRK-------VG----TLSGGMKQRLGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 85 ARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 161
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDP-EARRELWELLRE-LAaeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
.
gi 1907189171 162 E 162
Cdd:COG1131 221 R 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
65-171 |
4.15e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.86 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 65 TEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhvgkhVFEECIKKTL----KGKTVVLVTHQLQFLESCD 140
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV-----ETEAKVKAALdelmKGRTTFIIAHRLSTVRNAD 537
|
90 100 110
....*....|....*....|....*....|.
gi 1907189171 141 EVILLEDGEICEKGTHKELMEERGRYAKLIH 171
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-133 |
5.20e-18 |
|
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: 88.19 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQ 93
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLRLArPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907189171 94 LYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQL 133
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
320-521 |
5.86e-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: 85.13 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 320 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhAE---- 395
Cdd:cd18544 45 LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------NElfts 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 396 ---NFLQQFFMVVFILVIM-------AAVFPVVLVVLAGLAVIFLILLRIFHRGVQElkQVENISrspwfSHITSSIQGL 465
Cdd:cd18544 118 glvTLIGDLLLLIGILIAMfllnwrlALISLLVLPLLLLATYLFRKKSRKAYREVRE--KLSRLN-----AFLQESISGM 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 466 GVIHAYDKKDDCISKFKTLNDEnssHLLYFNCALRWFALRMDILMNIVTFVVALLV 521
Cdd:cd18544 191 SVIQLFNREKREFEEFDEINQE---YRKANLKSIKLFALFRPLVELLSSLALALVL 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
61-150 |
9.33e-18 |
|
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: 81.68 E-value: 9.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 61 YGDLTeiGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKK-TLKGKTVVLVTHQLQFLES- 138
Cdd:cd03230 85 YENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElKKEGKTILLSSHILEEAERl 161
|
90
....*....|..
gi 1907189171 139 CDEVILLEDGEI 150
Cdd:cd03230 162 CDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-145 |
1.44e-17 |
|
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: 82.20 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQA---WIFHGNVRENILFGekynhqRYQHTVHVCGLQKD-----LNSLPYGDLTEIGERGV-NLSGGQRQRISLA 85
Cdd:cd03235 71 GYVPQRRsidRDFPISVRDVVLMG------LYGHKGLFRRLSKAdkakvDEALERVGLSELADRQIgELSGGQQQRVLLA 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILL 145
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLL 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
613-816 |
1.66e-17 |
|
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: 83.16 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEVDIctVGLE-DLRTKLTM-----IPQdpv 682
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDI--TGLPpHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 LFVG-TVRYNLD-PLGSHTDEMLWHVLERTF--------MRDTIMKLPE--KLQAEVTENGENFSVGERQLLCMARALLR 750
Cdd:COG0411 90 LFPElTVLENVLvAAHARLGRGLLAALLRLPrarreereARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 751 NSKIILLDEATASMDSK-TDTLVQsTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 816
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELAE-LIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
28-165 |
2.28e-17 |
|
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: 82.21 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 28 VRENI-LFGEKY------NHQRYQHTVHVCGLQKDLNslpygdlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDP 100
Cdd:COG4555 91 VRENIrYFAELYglfdeeLKKRIEELIELLGLEEFLD-----------RRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 101 LSAVDAhVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 165
Cdd:COG4555 160 TNGLDV-MARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
613-823 |
2.31e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 82.34 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL-RTKLTMIPQDPVLFVG-TVRY 690
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 691 NLDpLGSHT-------DEMLWHVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCMARALLRNSKIILLDEATAS 763
Cdd:COG0410 98 NLL-LGAYArrdraevRADLERVYEL-FPR-----LKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 764 mdsktdtLVQSTIKEafksctVLTIAHRLN----TVL----N-------CDLVLVMENGKVIEFDKPEVLAEKPD 823
Cdd:COG0410 167 -------LAPLIVEE------IFEIIRRLNregvTILlveqNarfaleiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
614-811 |
2.82e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 87.34 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIidevdictvgleDLRTKLTMIPQDPVLFVGTVRYNLD 693
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV------------VIRGSVAYVPQVSWIFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 694 PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV- 772
Cdd:PLN03232 701 FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVf 780
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907189171 773 QSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:PLN03232 781 DSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
15-161 |
3.29e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.04 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIF-HGNVRENILFG-------EKYNHQRYQH---TVHvcglqkdlnslpygdLTEIGERGVN-LSGGQRQRI 82
Cdd:COG1118 78 GFVFQHYALFpHMTVAENIAFGlrvrppsKAEIRARVEElleLVQ---------------LEGLADRYPSqLSGGQRQRV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 83 SLARAVYANRQLYLLDDPLSAVDAHVGKHVfEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 159
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKEL-RRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
..
gi 1907189171 160 ME 161
Cdd:COG1118 222 YD 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
597-809 |
3.35e-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: 81.04 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKL 674
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDpvlfvgtvrYNLDPlgsHTDemlwhVLErtfmrdTIMKLPEKLQ----AEVTENGENF---------------- 734
Cdd:cd03262 79 GMVFQQ---------FNLFP---HLT-----VLE------NITLAPIKVKgmskAEAEERALELlekvgladkadaypaq 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 735 -SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKV 809
Cdd:cd03262 136 lSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
597-811 |
3.56e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.59 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLR 671
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKLTMIPQDpvlfvgtvrYNLdpLGSHTdemlwhV-------LErtfmrdtIMKLP-EKLQAEVTE---------NGENF 734
Cdd:COG1135 82 RKIGMIFQH---------FNL--LSSRT------VaenvalpLE-------IAGVPkAEIRKRVAEllelvglsdKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 735 ----SVGERQLLCMARALLRNSKIILLDEATASMDSKT-----DTLVQstIKEAFKScTVLTIAHRLNTVLN-CDLVLVM 804
Cdd:COG1135 138 psqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsilDLLKD--INRELGL-TIVLITHEMDVVRRiCDRVAVL 214
|
....*..
gi 1907189171 805 ENGKVIE 811
Cdd:COG1135 215 ENGRIVE 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
74-150 |
4.99e-17 |
|
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: 79.57 E-value: 4.99e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDaHVGKHVFEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
63-150 |
8.83e-17 |
|
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: 79.02 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQL-QFLESC 139
Cdd:cd03214 86 GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlARERGKTVVMVLHDLnLAARYA 165
|
90
....*....|.
gi 1907189171 140 DEVILLEDGEI 150
Cdd:cd03214 166 DRVILLKDGRI 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-147 |
9.60e-17 |
|
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: 79.82 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 7 VVAVNGPLAYVSQQAWIF-HGNVRENILFGEKYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQ 78
Cdd:cd03293 68 VTGPGPDRGYVFQQDALLpWLTVLDNVALGLELQGvpkaearERAEELLELVGLSGFENAYPH-----------QLSGGM 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 79 RQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLqflescDEVILLED 147
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE-LLDIWRetGKTVLLVTHDI------DEAVFLAD 200
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
67-162 |
1.05e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.52 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 67 IGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVI 143
Cdd:COG1121 137 IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA-TEEALYELLRE-LRreGKTILVVTHDLGAVREyFDRVL 210
|
90
....*....|....*....
gi 1907189171 144 LLEDGEICEkGTHKELMEE 162
Cdd:COG1121 211 LLNRGLVAH-GPPEEVLTP 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
613-810 |
1.15e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.13 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIIIDEVDIctvGLEDLRTKLTMIPQDPVLFVG-TVR 689
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 ynldplgshtdEMLWHVLErtfMRdtimklpeklqaevtengeNFSVGERQLLCMARALLRNSKIILLDEATASMDSKTD 769
Cdd:cd03213 101 -----------ETLMFAAK---LR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907189171 770 TLVQSTIKE-AFKSCTVLTIAHRLNTVL--NCDLVLVMENGKVI 810
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
597-816 |
1.26e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:PRK09536 4 IDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVL-FVGTVRY-----------NLDPLGShTDEMlwhVLERTFMRDTIMKLPEKlqaEVTEngenFSVGERQLLCM 744
Cdd:PRK09536 82 VPQDTSLsFEFDVRQvvemgrtphrsRFDTWTE-TDRA---AVERAMERTGVAQFADR---PVTS----LSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 745 ARALLRNSKIILLDEATASMD----SKTDTLVQSTIKEAFkscTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 816
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDinhqVRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPA 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-150 |
1.51e-16 |
|
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: 79.10 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 13 PLAYVSQQAWIF-HGNVRENILFGEKYNHQRYQHTVhvcglQKDLNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYA 90
Cdd:cd03259 73 NIGMVFQDYALFpHLTVAENIAFGLKLRGVPKAEIR-----ARVRELLELVGLEGLLNRYPHeLSGGQQQRVALARALAR 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 91 NRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 150
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
613-821 |
1.64e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVG-TVR-- 689
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 --YNLDPLGSH------TDEMLwhvLERTFMRDTIMKLPEKLqaeVTEngenFSVGERQLLCMARALLRNSKIILLDEAT 761
Cdd:PRK11231 97 vaYGRSPWLSLwgrlsaEDNAR---VNQAMEQTRINHLADRR---LTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 762 ASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAEK 821
Cdd:PRK11231 167 TYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPeEVMTPG 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
596-836 |
1.65e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.83 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 596 EITFKDYRMRYRDNTPLVLDGL---NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVG-----L 667
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERRALydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI-TAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 668 EDLRTKLTMIPQDP--VLFVGTVRYNL--DPLG---------SHTDEMLWHVlertfmrdtimKLPEKLqaeVTENGENF 734
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEKDIcfGPMNfgvseedakQKAREMIELV-----------GLPEEL---LARSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 735 SVGERQLLCMARALLRNSKIILLDEATASMDSKTdtlvQSTIKEAF------KSCTVLTIAHRLNTVLN-CDLVLVMENG 807
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907189171 808 KVIE-------FDKPEVLAEK----PDSA-FAMLLAAEVGL 836
Cdd:PRK13634 223 TVFLqgtpreiFADPDELEAIgldlPETVkFKRALEEKFGI 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
613-811 |
1.93e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRTKLTMIPQDPVLFVG--- 686
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSISAVNprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 687 TVRY----------NLDPLG--SHTDEMLWHVlertFMRDTIM-KLPEKLqaevtengenfSVGERQLLCMARALLRNSK 753
Cdd:PRK10419 107 TVREiireplrhllSLDKAErlARASEMLRAV----DLDDSVLdKRPPQL-----------SGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 754 IILLDEATASMDSKTDTLVQSTIKE-------AFksctvLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKlqqqfgtAC-----LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
27-150 |
2.42e-16 |
|
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: 78.69 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 27 NVRENILFGEKY-------NHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDD 99
Cdd:cd03255 98 TALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYP-----------SELSGGQQQRVAIARALANDPKIILADE 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 100 PLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:cd03255 167 PTGNLDSETGKEVMEL-LRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
613-811 |
2.99e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVgLEDLRTKLTMIPQDPVLFVG-TVR 689
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRSP-RDAQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLdplgshtdeML------WHVLERTFMRDTIMKLPEKLQAEV--TENGENFSVGERQLLCMARALLRNSKIILLDEAT 761
Cdd:COG1129 98 ENI---------FLgreprrGGLIDWRAMRRRARELLARLGLDIdpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 762 ASMDSK-TDTLVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:COG1129 169 ASLTEReVERLFR-IIRR-LKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
320-487 |
3.94e-16 |
|
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: 79.75 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 320 LVYIASMVsvlmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlpfhaeNFLQ 399
Cdd:cd18547 53 GLYLLSAL----FSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNIS--------QALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 400 Q--------FFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLRIFHRgVQEL--KQVENISRspWFSHITSSIQGLGVI 468
Cdd:cd18547 121 QsltqlissILTIVGTLIMMLYIsPLLTLIVLVTVPLSLLVTKFIAKR-SQKYfrKQQKALGE--LNGYIEEMISGQKVV 197
|
170
....*....|....*....
gi 1907189171 469 HAYDKKDDCISKFKTLNDE 487
Cdd:cd18547 198 KAFNREEEAIEEFDEINEE 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
605-812 |
6.37e-16 |
|
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: 77.23 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNtpLVLDGLNLNIQSGQTvGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVGLEDLRTKLTMIPQDPVLF 684
Cdd:cd03264 9 RYGKK--RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 685 VG-TVRYNLDPLG-------SHTDEMLWHVLERTFMRDtimKLPEKLQAevtengenFSVGERQLLCMARALLRNSKIIL 756
Cdd:cd03264 85 PNfTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGD---RAKKKIGS--------LSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 757 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV-LNCDLVLVMENGKVIEF 812
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
607-778 |
7.16e-16 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 77.13 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 607 RDNTPLvLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTMIPQDPVLFVG 686
Cdd:COG4133 12 RGERLL-FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 687 -TVRYNLDPL-----GSHTDEMLWHVLERtfmrdtiMKLPEKLQAEVtengENFSVGERQLLCMARALLRNSKIILLDEA 760
Cdd:COG4133 90 lTVRENLRFWaalygLRADREAIDEALEA-------VGLAGLADLPV----RQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170
....*....|....*...
gi 1907189171 761 TASMDSKTDTLVQSTIKE 778
Cdd:COG4133 159 FTALDAAGVALLAELIAA 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
597-811 |
1.11e-15 |
|
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: 76.74 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTP--LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGledlrTKL 674
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFvgtvrynldPlgshtdemlWhvleRTfMRDTIMkLPEKLQ----AEVTENGENF---------------- 734
Cdd:cd03293 76 GYVFQQDALL---------P---------W----LT-VLDNVA-LGLELQgvpkAEARERAEELlelvglsgfenayphq 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 735 -SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLN-TVLNCDLVLVMEN--GK 808
Cdd:cd03293 132 lSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGR 211
|
...
gi 1907189171 809 VIE 811
Cdd:cd03293 212 IVA 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-166 |
1.47e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 3 LQKGVvavngplAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRI 82
Cdd:PRK10790 413 LRQGV-------AMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLL 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 83 SLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKE 158
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGT-----EQAIQQALaavrEHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
....*...
gi 1907189171 159 LMEERGRY 166
Cdd:PRK10790 561 LLAAQGRY 568
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
614-820 |
1.56e-15 |
|
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: 80.23 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII----DEVDICTVGLeDLRTKLT----MIPQDPVLFv 685
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLY- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 686 gTVRYNLDPLgshTDEMLWHVLERTFMRDTIMKL-----PEKLQAEVTEN-GENFSVGERQLLCMARALLRNSKIILLDE 759
Cdd:TIGR03269 378 -PHRTVLDNL---TEAIGLELPDELARMKAVITLkmvgfDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 760 ATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 820
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPeEIVEE 518
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-162 |
1.57e-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: 78.99 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 13 PLAYVSQQAWIF-HGNVRENILFG---EKYN----HQRYQHTVHVCGLqkdlnslpygdlTEIGERGVN-LSGGQRQRIS 83
Cdd:COG3842 78 NVGMVFQDYALFpHLTVAENVAFGlrmRGVPkaeiRARVAELLELVGL------------EGLADRYPHqLSGGQQQRVA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 84 LARAVyANR-QLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 159
Cdd:COG3842 146 LARAL-APEpRVLLLDEPLSALDAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
...
gi 1907189171 160 MEE 162
Cdd:COG3842 224 YER 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-160 |
1.78e-15 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 76.96 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 16 YVSQQAWIF-HGNVRENI-----LfgEKYNHQRYQHTVhvcglqKDLNSLPYGDLTEIGER-GVNLSGGQRQRISLARAV 88
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIalvpkL--LKWPKEKIRERA------DELLALVGLDPAEFADRyPHELSGGQQQRVGVARAL 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 89 YANRQLYLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 160
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
354-759 |
1.95e-15 |
|
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: 80.23 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 354 RVFNKIVRSPMSFFDTTPTGRLMNRFSKDMD---ELDVRLPFhaenFLQQFFMVVFILVIMA----AVFPVVLVVLAGLA 426
Cdd:COG4615 86 RLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE----LLQSVALVLGCLAYLAwlspPLFLLTLVLLGLGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 427 VIFLILLRIFHRGVQELKQVENIsrspWFSHITSSIQG---LGvIHAyDKKDD--------CISKFKtlnDENSSHLLYF 495
Cdd:COG4615 162 AGYRLLVRRARRHLRRAREAEDR----LFKHFRALLEGfkeLK-LNR-RRRRAffdedlqpTAERYR---DLRIRADTIF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 496 NCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSkgLSLSYIIQ-LSGLL---------QVCVRTGTETQAKFTSAE 565
Cdd:COG4615 233 ALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFV--LVLLFLRGpLSQLVgalptlsraNVALRKIEELELALAAAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 566 llreyiltcvpEHTHPFKVGTCPKDWpsrGEITFKDYRMRYR---DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGM 642
Cdd:COG4615 311 -----------PAAADAAAPPAPADF---QTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 643 ALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFvgtvRYNLDPLGSHTDEMLWHVLERtfmrdtiMKLPEK 722
Cdd:COG4615 377 LLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLER-------LELDHK 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907189171 723 LQAevtENGE----NFSVGERQLLCMARALLRNSKIILLDE 759
Cdd:COG4615 446 VSV---EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-172 |
2.10e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.18 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 6 GVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLA 85
Cdd:PLN03232 1304 GLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLA 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVGKhVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGR 165
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDS-LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
....*...
gi 1907189171 166 -YAKLIHN 172
Cdd:PLN03232 1463 aFFRMVHS 1470
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
614-823 |
2.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDP-VLFVGT----- 687
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGAtvedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 688 VRYNLDPLGSHTDEMLWHVLERTF---MRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASM 764
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLavnMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 765 DSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP-EVLAEKPD 823
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPsELFATSED 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
27-150 |
2.24e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 76.24 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 27 NVRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDD 99
Cdd:COG1136 102 TALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADE 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 100 PLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:COG1136 171 PTGNLDSKTGEEVLEllrELNREL--GTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
597-810 |
2.56e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 75.61 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDnTPLVLDglnLNIQSGQTVGIVGRTGSGKSSLG--MALFRLvePASGTIIIDEVDICTvgLEDLRTKL 674
Cdd:cd03298 1 VRLDKIRFSYGE-QPMHFD---LTFAQGEITAIVGPSGSGKSTLLnlIAGFET--PQSGRVLINGVDVTA--APPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQDPVLFVG-TVRYNLD----P---LGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMAR 746
Cdd:cd03298 73 SMLFQENNLFAHlTVEQNVGlglsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 747 ALLRNSKIILLDEATASMD----SKTDTLVQSTIKEafKSCTVLTIAHRLNTVLNC-DLVLVMENGKVI 810
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-150 |
2.63e-15 |
|
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: 75.75 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 25 HGNVRENILFGEKYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLL 97
Cdd:cd03301 86 HMTVYDNIAFGLKLRKvpkdeidERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLM 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 98 DDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 150
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
600-807 |
2.83e-15 |
|
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: 75.93 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYRDNTPL-VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID----EVDICTVG---LEDLR 671
Cdd:COG4778 12 KTFTLHLQGGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TK--------LTMIPQdpvlfVGTVRYNLDPLgshtdemlwhvLERTFMRD----------TIMKLPEKL--QAEVTeng 731
Cdd:COG4778 92 RRtigyvsqfLRVIPR-----VSALDVVAEPL-----------LERGVDREearararellARLNLPERLwdLPPAT--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 732 enFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAfKS--CTVLTIAHRLNTVLN-CDLVLVMENG 807
Cdd:COG4778 153 --FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KArgTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
74-149 |
2.92e-15 |
|
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: 74.53 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALL--KSLQaqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
307-487 |
3.04e-15 |
|
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: 77.16 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 307 DQTLQDTKHHMYQLVYI------ASMVSVLMFGIIKGFTftNTTLMA--SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNR 378
Cdd:cd18563 28 DVLIQLGPGGNTSLLLLlvlglaGAYVLSALLGILRGRL--LARLGEriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 379 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIM---------AAVFPVVLVVLaGLAVIFLILLRIFHRgvqelkqvenI 449
Cdd:cd18563 106 VTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLfslnwklalLVLIPVPLVVW-GSYFFWKKIRRLFHR----------Q 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907189171 450 SRSpWF---SHITSSIQGLGVIHAYDKKDDCISKFKTLNDE 487
Cdd:cd18563 175 WRR-WSrlnSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
17-159 |
3.12e-15 |
|
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: 75.68 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIFHGNVRENILFGEKynhqryqhtVHVCGLQKDLNSLPYGDLTEIG--------ERGVNLSGGQRQRISLARAV 88
Cdd:cd03260 86 VFQKPNPFPGSIYDNVAYGLR---------LHGIKLKEELDERVEEALRKAAlwdevkdrLHALGLSGGQQQRLCLARAL 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 89 YANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKEL 159
Cdd:cd03260 157 ANEPEVLLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
600-823 |
3.72e-15 |
|
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: 75.66 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYrdntplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvgledlrTKLTM--- 676
Cdd:cd03218 8 KRYGKRK------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---------TKLPMhkr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 -------IPQDPVLFVG-TVRYNLDPlgshtdemlwhVLErtfmrdtIMKLPEKLQAEVTE--------------NGENF 734
Cdd:cd03218 73 arlgigyLPQEASIFRKlTVEENILA-----------VLE-------IRGLSKKEREEKLEelleefhithlrksKASSL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 735 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 812
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAE 214
|
250
....*....|.
gi 1907189171 813 DKPEVLAEKPD 823
Cdd:cd03218 215 GTPEEIAANEL 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-147 |
4.55e-15 |
|
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: 74.82 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 1 MQLQKGVVAVNG------PLAYVSQQAWIFHGN-------VRENILF-----GEKYNHQRYQHTVHVCGLQKDLNSLPYg 62
Cdd:COG4133 52 LPPSAGEVLWNGepirdaREDYRRRLAYLGHADglkpeltVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 dlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTL-KGKTVVLVTHQLQFLESCdE 141
Cdd:COG4133 131 ----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-R 198
|
....*.
gi 1907189171 142 VILLED 147
Cdd:COG4133 199 VLDLGD 204
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
613-823 |
5.21e-15 |
|
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: 76.43 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQDPVLFVGTVRYNL 692
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 dPLGSHTDEMLW-HVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDtl 771
Cdd:cd03291 119 -IFGVSYDEYRYkSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE-- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 772 vqstiKEAFKSC--------TVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEKPD 823
Cdd:cd03291 196 -----KEIFESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTfSELQSLRPD 251
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
595-826 |
5.28e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.42 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSL-----GmalfrLVEPASGTIIIDEVDIctvglED 669
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV-----TD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTK---LTMIPQDPVLFVG-TVRYNLD-PL------GSHTDEMLWHVLErtfmrdtIMKLPEKLQAEVTEngenFSVGE 738
Cdd:COG3839 70 LPPKdrnIAMVFQSYALYPHmTVYENIAfPLklrkvpKAEIDRRVREAAE-------LLGLEDLLDRKPKQ----LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 739 RQLLCMARALLRNSKIILLDEATASMDSKtdtL-VQ--STIKE---AFKSCTV---------LTIAHRlntvlncdlVLV 803
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAK---LrVEmrAEIKRlhrRLGTTTIyvthdqveaMTLADR---------IAV 206
|
250 260
....*....|....*....|...
gi 1907189171 804 MENGKVIEFDKPEVLAEKPDSAF 826
Cdd:COG3839 207 MNDGRIQQVGTPEELYDRPANLF 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
56-154 |
5.93e-15 |
|
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: 73.50 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 56 LNSLPYGDLTEIGER-GVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEeCIKKTLKGKTVVLVTHQLQ 134
Cdd:cd03247 80 LNQRPYLFDTTLRNNlGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS-LIFEVLKDKTLIWITHHLT 158
|
90 100
....*....|....*....|
gi 1907189171 135 FLESCDEVILLEDGEICEKG 154
Cdd:cd03247 159 GIEHMDKILFLENGKIIMQG 178
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
594-811 |
6.02e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.33 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 594 RGEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICTVGLE 668
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 669 DLRTKLTMIPQDPvlfvgtvrynlDPLGSHTdemLWHVLERTFMRDTIMKLPEKLQAEVTENGE---------------- 732
Cdd:PRK14247 79 ELRRRVQMVFQIP-----------NPIPNLS---IFENVALGLKLNRLVKSKKELQERVRWALEkaqlwdevkdrldapa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 733 -NFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAH------RLNtvlncDLVLVME 805
Cdd:PRK14247 145 gKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLY 219
|
....*.
gi 1907189171 806 NGKVIE 811
Cdd:PRK14247 220 KGQIVE 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
606-804 |
7.02e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 7.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 606 YRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFV 685
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 686 GTVRYNLdplgshtdEMLWHV----LERTFMRDTIMK--LPEKLqaeVTENGENFSVGERQLLCMARALLRNSKIILLDE 759
Cdd:PRK10247 95 DTVYDNL--------IFPWQIrnqqPDPAIFLDDLERfaLPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907189171 760 ATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTVLNCDLVLVM 804
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
597-830 |
7.35e-15 |
|
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: 79.22 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTM 676
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVGTVRYNLdPLGSHTDEMLWH-VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKII 755
Cdd:TIGR00957 704 VPQQAWIQNDSLRENI-LFGKALNEKYYQqVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 756 LLDEATASMDSKTDTLVQSTI---KEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEkpDSAFAMLL 830
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSyQELLQR--DGAFAEFL 859
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
600-816 |
7.89e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.69 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYR--DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTV---GLEDLR 671
Cdd:PRK09473 16 KDLRVTFStpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 T-KLTMIPQDPVLfvgtvryNLDPLgSHTDEMLWHVL-------------ERTFMRDTImKLPEKLQaEVTENGENFSVG 737
Cdd:PRK09473 96 AeQISMIFQDPMT-------SLNPY-MRVGEQLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARK-RMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 738 ERQLLCMARALLRNSKIILLDEATASMdsktDTLVQSTI-------KEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKV 809
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTAL----DVTVQAQImtllnelKREFNT-AIIMITHDLGVVAGiCDKVLVMYAGRT 240
|
....*..
gi 1907189171 810 IEFDKPE 816
Cdd:PRK09473 241 MEYGNAR 247
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
263-523 |
8.72e-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: 8.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 263 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQvvcasqnnktacnvdqtlqdtKHHMYQLVYIASMVsVLMFgIIKG-FTFT 341
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFV---------------------EKDLEALLLVPLAI-IGLF-LLRGlASYL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 342 NTTLMASSSLH------NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVF 415
Cdd:cd18552 59 QTYLMAYVGQRvvrdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 416 PV-VLVVLAGLAVIFLILLRI------FHRGVQElkQVENISrspwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEN 488
Cdd:cd18552 139 WKlTLIALVVLPLAALPIRRIgkrlrkISRRSQE--SMGDLT-----SVLQETLSGIRVVKAFGAEDYEIKRFRKANERL 211
|
250 260 270
....*....|....*....|....*....|....*
gi 1907189171 489 sshllyfncalRWFALRMDILMNIVTFVVALLVTL 523
Cdd:cd18552 212 -----------RRLSMKIARARALSSPLMELLGAI 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
610-823 |
9.42e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.80 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 610 TPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQDPVLFVGTVR 689
Cdd:TIGR01271 439 TP-VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLdPLGSHTDEMLW-HVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKT 768
Cdd:TIGR01271 505 DNI-IFGLSYDEYRYtSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 769 DtlvqstiKEAFKSC--------TVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEKPD 823
Cdd:TIGR01271 584 E-------KEIFESClcklmsnkTRILVTSKLEHLKKADKILLLHEGVCYFYGTfSELQAKRPD 640
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-159 |
1.01e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 76.65 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIF-HGNVRENILFGEKYN-------HQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLA 85
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPLKLRkvpkaeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALG 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVgKHVFEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 159
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
618-822 |
1.07e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 618 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR----TKLTMIPQDPVLF-----VGTV 688
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMphmtvLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 689 RYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD 765
Cdd:PRK10070 128 AFGMELAGinaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 766 SKTDTLVQSTIK--EAFKSCTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKP 822
Cdd:PRK10070 197 PLIRTEMQDELVklQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
613-810 |
1.33e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvgledlrTKLT------MIP---QDPVL 683
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---------TKLPeykrakYIGrvfQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 684 fvGT-----VRYNL---------DPLGshtdemlWHVL--ERTFMRDTI----MKLPEKLQAEVtengENFSVGERQLLC 743
Cdd:COG1101 92 --GTapsmtIEENLalayrrgkrRGLR-------RGLTkkRRELFRELLatlgLGLENRLDTKV----GLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 744 MARALLRNSKIILLDEATASMDSKTDTLV----QSTIKEafKSCTVLTIAHRLNTVLNC-DLVLVMENGKVI 810
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEE--NNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
618-826 |
1.61e-14 |
|
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: 74.60 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 618 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL----RTKLTMIPQDPVLF-----VGTV 688
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLphrtvLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 689 RYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD 765
Cdd:cd03294 124 AFGLEVQGvprAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 766 SKTDTLVQSTI----KEAFKscTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKPDSAF 826
Cdd:cd03294 193 PLIRREMQDELlrlqAELQK--TIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
597-823 |
1.61e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLV---LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC----TVGLED 669
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQDP--VLFVGTV----RYNLDPLGSHTDE-----MLWhvLERTFMRDTIM-KLPEKLqaevtengenfSVG 737
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVlkdvEFGPKNFGFSEDEakekaLKW--LKKVGLSEDLIsKSPFEL-----------SGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 738 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 815
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGhTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
....*...
gi 1907189171 816 EVLAEKPD 823
Cdd:PRK13641 230 KEIFSDKE 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
27-159 |
1.87e-14 |
|
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: 73.69 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 27 NVRENILFGEKYNHQRYQHTV--------HVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLD 98
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIreivleklEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYD 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 99 DPLSAVDAhVGKHVFEECI---KKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 159
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
63-163 |
1.89e-14 |
|
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: 73.52 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGV-NLSGGQRQRISLArAVYANR-QLYLLDDPLSAVDAHvGKHVFEECIKK-TLKGKTVVLVTHQLQFL-ES 138
Cdd:COG1122 123 GLEHLADRPPhELSGGQKQRVAIA-GVLAMEpEVLVLDEPTAGLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaEL 200
|
90 100
....*....|....*....|....*
gi 1907189171 139 CDEVILLEDGEICEKGTHKELMEER 163
Cdd:COG1122 201 ADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
624-834 |
2.20e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 624 GQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPVLFVG---TVRYN-LDPLG 696
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYASLDprqTVGDSiMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 697 SH--------TDEMLWhVLERTFMRdtimklPEKLQAEVTEngenFSVGERQLLCMARALLRNSKIILLDEATASMDSKT 768
Cdd:PRK10261 430 VHgllpgkaaAARVAW-LLERVGLL------PEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 769 ---------DTLVQSTIKEAFKS---CTVLTIAHRlntvlncdlVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 834
Cdd:PRK10261 499 rgqiinlllDLQRDFGIAYLFIShdmAVVERISHR---------VAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-162 |
2.40e-14 |
|
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: 73.54 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWI-FHGNVRENILFGekynhqRYQHTVHVCGLQKD--------LNSLpygDLTEIGERGVN-LSGGQRQRIS 83
Cdd:COG1120 77 IAYVPQEPPApFGLTVRELVALG------RYPHLGLFGRPSAEdreaveeaLERT---GLEHLADRPVDeLSGGERQRVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 84 LARAVYANRQLYLLDDPLSAVDAHvgkHVFE--ECIKK--TLKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKE 158
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEE 224
|
....
gi 1907189171 159 LMEE 162
Cdd:COG1120 225 VLTP 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-162 |
2.55e-14 |
|
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: 73.83 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 25 HGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLL 97
Cdd:cd03294 116 HRTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLM 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 98 DDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 162
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
597-818 |
2.55e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 669
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQDP--VLFVGTV-----------RYNLDPLGSHTDEMLwhvLERTFMRDTIMKLPEKLqaevtengenfSV 736
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQM-----------SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 737 GERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 813
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQT 228
|
....*
gi 1907189171 814 KPEVL 818
Cdd:PRK13646 229 SPKEL 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-170 |
4.10e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLY 95
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 96 LLDDPLSAVDAHVgkhvfEECIKKTL------KGKTVVLVTHQLQFLESCDEVILLEDGE-----ICEKGTHKELME-ER 163
Cdd:PTZ00265 1381 LLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQD 1455
|
....*..
gi 1907189171 164 GRYAKLI 170
Cdd:PTZ00265 1456 GVYKKYV 1462
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
74-185 |
5.08e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 75.71 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGR 482
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907189171 150 ICEKGTHKELmeergryaklihnlrglqFKDPEHIY 185
Cdd:COG1123 483 IVEDGPTEEV------------------FANPQHPY 500
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
615-811 |
5.31e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 615 DGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII---DEVDICTVGLEDLRTKLTMIPQDPVLfvgtvryN 691
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDPLA-------S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 692 LDP---LGSHTDEMLwhvleRTFM----RDTIMklpEKLQAEVTENG----------ENFSVGERQLLCMARALLRNSKI 754
Cdd:PRK15079 111 LNPrmtIGEIIAEPL-----RTYHpklsRQEVK---DRVKAMMLKVGllpnlinrypHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 755 ILLDEATASMD----SKTDTLVQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK15079 183 IICDEPVSALDvsiqAQVVNLLQQLQREMGLS--LIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
601-819 |
5.64e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 601 DYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII--DEVDICTVGLEDLRTKLTMIP 678
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 679 QDP---VLFV---GTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAevtengenFSVGERQLLCMARALLRNS 752
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 753 KIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLA 819
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPgEVFA 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
13-150 |
5.81e-14 |
|
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: 74.37 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 13 PLAYVSQQAWIF-HGNVRENILFGEKYN--HQRYQHTVHVCglqkdlnslpygDLTEIG---ERGV-NLSGGQRQRISLA 85
Cdd:COG4148 78 RIGYVFQEARLFpHLSVRGNLLYGRKRAprAERRISFDEVV------------ELLGIGhllDRRPaTLSGGERQRVAIG 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVgKHvfeECIK--KTLKGKT---VVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLAR-KA---EILPylERLRDELdipILYVSHSLDEVARlADHVVLLEQGRV 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
596-828 |
6.94e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 71.99 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 596 EITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLT 675
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 676 MipQDPVLFVG-TVRYNL------DPLGSHTDEMLwhvlertfMRDTIMKLPEKLQAEVTENG--ENFSVGERQLLCMAR 746
Cdd:cd03296 80 F--QHYALFRHmTVFDNVafglrvKPRSERPPEAE--------IRAKVHELLKLVQLDWLADRypAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 747 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTI--AHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 823
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
....*
gi 1907189171 824 SAFAM 828
Cdd:cd03296 230 SPFVY 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-149 |
6.94e-14 |
|
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: 71.34 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 23 IFHGNVRENILFGEKyNHQRYQHTVhvcgLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLArAVYANR-QLYLLDDP 100
Cdd:cd03225 88 FFGPTVEEEVAFGLE-NLGLPEEEI----EERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIA-GVLAMDpDILLLDEP 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907189171 101 LSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFL-ESCDEVILLEDGE 149
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
614-811 |
8.22e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.93 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIdevdictvgledLRTKLTMIPQDPVLFVGTVRYNLd 693
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNI- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 694 PLGSHTD-EMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 772
Cdd:PLN03130 700 LFGSPFDpERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907189171 773 -QSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 811
Cdd:PLN03130 780 fDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
74-154 |
8.52e-14 |
|
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: 71.38 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKTLK------GKTVVLVTHQLQFL-ESCDEVILLE 146
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKklqeelGLTLLFITHDLGVVaKIADRVAVMY 220
|
....*...
gi 1907189171 147 DGEICEKG 154
Cdd:cd03257 221 AGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
74-161 |
1.04e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 71.76 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEEcIKKTlKGKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGR 216
|
90
....*....|..
gi 1907189171 150 ICEKGTHKELME 161
Cdd:COG1124 217 IVEELTVADLLA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-148 |
1.04e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.04 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 10 VNGP---LAYVSQQA----WIfhgNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLS 75
Cdd:COG1116 75 VTGPgpdRGVVFQEPallpWL---TVLDNVALGlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLS 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 76 GGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgKHVFEECIKKTLK--GKTVVLVTHQLQ---FLesCDEVILLEDG 148
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALT-RERLQDELLRLWQetGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
73-159 |
1.11e-13 |
|
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: 71.46 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGE 218
|
90
....*....|
gi 1907189171 150 ICEKGTHKEL 159
Cdd:cd03258 219 VVEEGTVEEV 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
597-820 |
1.24e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 676
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQ----DPVLfvgTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTEngenFSVGERQLLCMARALLRNS 752
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 753 KIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAH------RLntvlnCDLVLVMENGKVIEFDKPEVLAE 820
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-155 |
1.36e-13 |
|
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: 70.52 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 6 GVVAVNGPLAYVSQQAWIFHGNVRENIlfgEKYNHQRyqhtvhvcglQKDLnslpYGDLtEIGERGVNLSGGQRQRISLA 85
Cdd:cd03369 76 PLEDLRSSLTIIPQDPTLFSGTIRSNL---DPFDEYS----------DEEI----YGAL-RVSEGGLNLSQGQRQLLCLA 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVgKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 155
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-161 |
1.60e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 70.83 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 16 YVSQQAWIF-HGNVRENILFG-------EKYNHQRYQHTVHvcglqkdlNSLPYGDLTEIGERGVN-LSGGQRQRISLAR 86
Cdd:cd03296 78 FVFQHYALFrHMTVFDNVAFGlrvkprsERPPEAEIRAKVH--------ELLKLVQLDWLADRYPAqLSGGQRQRVALAR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 87 AVYANRQLYLLDDPLSAVDAHVGKHvfeecIKKTLK------GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 159
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
..
gi 1907189171 160 ME 161
Cdd:cd03296 225 YD 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-162 |
1.67e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIF-HGNVRENILFG---EKYNHQRYQHTVhvcglqkdLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYAN 91
Cdd:PRK09452 91 VFQSYALFpHMTVFENVAFGlrmQKTPAAEITPRV--------MEALRMVQLEEFAQRKPhQLSGGQQQRVAIARAVVNK 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 92 RQLYLLDDPLSAVDAHVGKHVFEEC--IKKTLkGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 162
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELkaLQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
577-811 |
1.73e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 577 EHTHPFKVGTCPKDWPsrgEITFKDYRMRYRDNTpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTII 656
Cdd:PRK10522 306 PYKAEFPRPQAFPDWQ---TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 657 IDEVDICTVGLEDLRTKLTMIPQDPVLFvgtvRYNLDPLGSHTDEML---WhvLERtfmrdtiMKLPEKLQaevTENGE- 732
Cdd:PRK10522 382 LDGKPVTAEQPEDYRKLFSAVFTDFHLF----DQLLGPEGKPANPALvekW--LER-------LKMAHKLE---LEDGRi 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 733 ---NFSVGERQLLCMARALLRNSKIILLDEATASMDSK------TDTLVQstIKEAFKscTVLTIAHRLNTVLNCDLVLV 803
Cdd:PRK10522 446 snlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPL--LQEMGK--TIFAISHDDHYFIHADRLLE 521
|
....*...
gi 1907189171 804 MENGKVIE 811
Cdd:PRK10522 522 MRNGQLSE 529
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
64-162 |
2.88e-13 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 71.76 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 64 LTEIGERG-VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikKTLK---GKTVVLVTH-QLQFLES 138
Cdd:TIGR01187 90 LEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL--KTIQeqlGITFVFVTHdQEEAMTM 167
|
90 100
....*....|....*....|....
gi 1907189171 139 CDEVILLEDGEICEKGTHKELMEE 162
Cdd:TIGR01187 168 SDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
74-161 |
3.50e-13 |
|
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: 73.01 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 150
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
|
90
....*....|.
gi 1907189171 151 CEKGTHKELME 161
Cdd:COG1123 222 VEDGPPEEILA 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
605-833 |
3.77e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL-----VEPASGTIIIDEVDICTVGLEDLR----TKLT 675
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 676 MIPQDPVLfvgtvryNLDPLgsHTDE-MLWHVL------ERTFMRDTIMKLPEKL---QA--EVTENGENFSVGERQLLC 743
Cdd:PRK15134 96 MIFQEPMV-------SLNPL--HTLEkQLYEVLslhrgmRREAARGEILNCLDRVgirQAakRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 744 MARALLRNSKIILLDEATASMdsktDTLVQSTIKEAFK------SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 816
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTAL----DVSVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*...
gi 1907189171 817 VLAEKPDSAFA-MLLAAE 833
Cdd:PRK15134 243 TLFSAPTHPYTqKLLNSE 260
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
613-818 |
4.07e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.19 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVL-FVGTVR-- 689
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 --YNLDPLGS---HTDEMLWHVLERTfmrdtimklpeklqaEVTENGENF----SVGERQLLCMARALLRNS------KI 754
Cdd:PRK13548 97 vaMGRAPHGLsraEDDALVAAALAQV---------------DLAHLAGRDypqlSGGEQQRVQLARVLAQLWepdgppRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 755 ILLDEATASMDSKTdtlvQSTIKEAFKSCT------VLTIAHRLN-TVLNCDLVLVMENGKVIEFDKP-EVL 818
Cdd:PRK13548 162 LLLDEPTSALDLAH----QHHVLRLARQLAherglaVIVVLHDLNlAARYADRIVLLHQGRLVADGTPaEVL 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
613-821 |
4.11e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGL-EDLRTKLTMIPQDPVLFVGTVRYN 691
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 692 ldplgshtdeMLWHVLErtfMRDTIMKLPEKLQA-EVTEN----------GENFSVGERQLLCMARALLRNSKIILLDEA 760
Cdd:PRK10895 98 ----------NLMAVLQ---IRDDLSAEQREDRAnELMEEfhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 761 TASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAEK 821
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPtEILQDE 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
597-814 |
4.44e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYrdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--VEP---ASGTIIIDEVDIC-----TVg 666
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYsprtdTV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 667 leDLRTKLTMIPQDPVLFVGT----VRYNLDPLGSHTDEMLWHVLERTFMRDTIMklpEKLQAEVTENGENFSVGERQLL 742
Cdd:PRK14239 83 --DLRKEIGMVFQQPNPFPMSiyenVVYGLRLKGIKDKQVLDEAVEKSLKGASIW---DEVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 743 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 814
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
597-827 |
4.59e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.28 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKltM 676
Cdd:COG3842 6 LELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG--M 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLF-----VGTVRYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 748
Cdd:COG3842 82 VFQDYALFphltvAENVAFGLRMRGvpkAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 749 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC---TV---------LTIAHRlntvlncdlVLVMENGKVIEFDKPE 816
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELgitFIyvthdqeeaLALADR---------IAVMNDGRIEQVGTPE 221
|
250
....*....|.
gi 1907189171 817 VLAEKPDSAFA 827
Cdd:COG3842 222 EIYERPATRFV 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
614-820 |
5.39e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLgM-ALFRLVEPASGTIIID--EVDI--------CTVGledlrtkltMIPQDPV 682
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDgkPVRIrsprdaiaLGIG---------MVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 LF-VGTVRYNLDpLGshTDEMLWHVLERTFMRDTIMKLPEK------LQAEVtengENFSVGERQLLCMARALLRNSKII 755
Cdd:COG3845 91 LVpNLTVAENIV-LG--LEPTKGGRLDRKAARARIRELSERygldvdPDAKV----EDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 756 LLDEATASM-DSKTDTLVQsTIKEaFKS--CTVLTIAHRLNTVL-NCDLVLVMENGKVI-EFDKPEV----LAE 820
Cdd:COG3845 164 ILDEPTAVLtPQEADELFE-ILRR-LAAegKSIIFITHKLREVMaIADRVTVLRRGKVVgTVDTAETseeeLAE 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
74-162 |
5.40e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 69.19 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEC--IKKTLkGKTVVLVTH-QLQFLESCDEVILLEDGEI 150
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrLQKEL-GITFVFVTHdQEEALTMSDRIAVMNKGKI 209
|
90
....*....|..
gi 1907189171 151 CEKGTHKELMEE 162
Cdd:cd03300 210 QQIGTPEEIYEE 221
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
306-520 |
5.62e-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: 70.15 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 306 VDQTLQDTKHHMyqLVYIASMVsvLMFGIIKG-FTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 378
Cdd:cd18542 26 IDSVIGGGLREL--LWLLALLI--LGVALLRGvFRYLQGYLAEKASqkvaydLRNDLYDHLQRLSFSFHDKARTGDLMSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 379 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLrIFHRGVQelKQVENISRSpwFSH 457
Cdd:cd18542 102 CTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSInWKLTLISLAIIPFIALFSY-VFFKKVR--PAFEEIREQ--EGE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 458 ITSSIQ----GLGVIHAYDKKDDCISKFKTLNDEnsshllYFNCALR-------WFALrMDILMNIVTFVVALL 520
Cdd:cd18542 177 LNTVLQenltGVRVVKAFAREDYEIEKFDKENEE------YRDLNIKlakllakYWPL-MDFLSGLQIVLVLWV 243
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
14-160 |
6.09e-13 |
|
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: 70.91 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIF-HGNVRENILFGEK-----YNHQRYQHTVHVCGLQKDLnslpygdlteigERGVN-LSGGQRQRISLAR 86
Cdd:TIGR02142 77 IGYVFQEARLFpHLSVRGNLRYGMKrarpsERRISFERVIELLGIGHLL------------GRLPGrLSGGEKQRVAIGR 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 87 AVYANRQLYLLDDPLSAVDAHVGKHV--FEECIKKTLkGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 160
Cdd:TIGR02142 145 ALLSSPRLLLMDEPLAALDDPRKYEIlpYLERLHAEF-GIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
314-521 |
9.04e-13 |
|
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: 69.80 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 314 KHHMYQLVYIASMVSVLMFgIIKGFTFTNTTLMAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD 387
Cdd:cd18545 33 NGDLSGLLIIALLFLALNL-VNWVASRLRIYLMAKvgqrilYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 388 VRLPFHAENFLQQFFMVVFILVIMAAVFPVV-LVVLAGLAVIFLILLRIFHRgVQELKQVENISRSPWFSHITSSIQGLG 466
Cdd:cd18545 112 DLLSNGLINLIPDLLTLVGIVIIMFSLNVRLaLVTLAVLPLLVLVVFLLRRR-ARKAWQRVRKKISNLNAYLHESISGIR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 467 VIHAYDKKDDCISKFKTLNDEN-SSHLLyfncALRWFALRMDILMNIVTFVVALLV 521
Cdd:cd18545 191 VIQSFAREDENEEIFDELNRENrKANMR----AVRLNALFWPLVELISALGTALVY 242
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
306-521 |
9.76e-13 |
|
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: 69.75 E-value: 9.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 306 VDqTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFTNTTLMASS-----SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFS 380
Cdd:cd18541 26 ID-ALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASrrieyDLRNDLFAHLLTLSPSFYQKNRTGDLMARAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 381 KDMDEldVR--LPFHAENFLQQFFMVVFILVIMAAVFP----VVLVVLAGLAVIFLILLRIFHRG---VQELkqvenisr 451
Cdd:cd18541 105 NDLNA--VRmaLGPGILYLVDALFLGVLVLVMMFTISPkltlIALLPLPLLALLVYRLGKKIHKRfrkVQEA-------- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 452 spwFSHITSSIQ----GLGVIHAYDKKDDCISKFKTLNDENSSHllyfNCAL-RWFALrMDILMNIVTFVVALLV 521
Cdd:cd18541 175 ---FSDLSDRVQesfsGIRVIKAFVQEEAEIERFDKLNEEYVEK----NLRLaRVDAL-FFPLIGLLIGLSFLIV 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
613-811 |
1.02e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.27 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPvlfvgtvR 689
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLDP-----------LGSHTDEMlwHVLERTFMRDTIMKL----PEKLQAEVTEngenFSVGERQLLCMARALLRNSKI 754
Cdd:PRK15134 373 SSLNPrlnvlqiieegLRVHQPTL--SAAQREQQVIAVMEEvgldPETRHRYPAE----FSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 755 ILLDEATASMDsKTdtlVQSTIKEAFKS------CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK15134 447 IILDEPTSSLD-KT---VQAQILALLKSlqqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-161 |
1.12e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIF-HGNVRENILFGekynhqryqhTVHVCGLQK-DLNSLPYGDLTEIG--ERG----VNLSGGQRQRISLARAV 88
Cdd:PRK09493 82 VFQQFYLFpHLTALENVMFG----------PLRVRGASKeEAEKQARELLAKVGlaERAhhypSELSGGQQQRVAIARAL 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 89 YANRQLYLLDDPLSAVDAHVGKHVFEecIKKTL--KGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELME 161
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLK--VMQDLaeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
74-150 |
1.17e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 67.94 E-value: 1.17e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEI 150
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
614-807 |
1.36e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDLRTKLT------MIPQD-PVLFVG 686
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-----YNKLDHKLAaqlgigIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 687 TVRYNLdPLGSHTDEMLW--HVLERTFMRD--TIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATA 762
Cdd:PRK09700 96 TVLENL-YIGRHLTKKVCgvNIIDWREMRVraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907189171 763 SM-DSKTDTL--VQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENG 807
Cdd:PRK09700 175 SLtNKEVDYLflIMNQLRKEGTA--IVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
597-811 |
1.72e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDI-CTVGLEDLRTKLT 675
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 676 MIPQDpvlfVGTV--RYNLDPLGShtdeMLWHVLE-----RTFMRDTIMKLPEKLQAEVTENGEN------FSVGERQLL 742
Cdd:PRK11264 82 QLRQH----VGFVfqNFNLFPHRT----VLENIIEgpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 743 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
318-521 |
1.74e-12 |
|
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: 68.74 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 318 YQLVYIASMVSVLMFgiIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENF 397
Cdd:cd18557 40 LILLAIYLLQSVFTF--VRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 398 LQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQEL-KQV-ENISRSPwfSHITSSIQGLGVIHAYDKKD 475
Cdd:cd18557 118 LRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLsKEVqDALAKAG--QVAEESLSNIRTVRSFSAEE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907189171 476 DCISKFKTLNDEnsSHLLYFNCAlRWFALRMDIlMNIVTFVVALLV 521
Cdd:cd18557 196 KEIRRYSEALDR--SYRLARKKA-LANALFQGI-TSLLIYLSLLLV 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
613-811 |
2.13e-12 |
|
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: 66.78 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPVLFVGtvr 689
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 ynldplgshtdemlwhVLERTFMRDTimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIILLDEatasMDSKTD 769
Cdd:cd03217 92 ----------------VKNADFLRYV---------------NEGFSGGEKKRNEILQLLLLEPDLAILDE----PDSGLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907189171 770 TLVQSTIKEAFKS-----CTVLTIAH--RLNTVLNCDLVLVMENGKVIE 811
Cdd:cd03217 137 IDALRLVAEVINKlreegKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
47-160 |
2.16e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 47 VHVCGLQKDL---NSLPYGDLTEIGERG-----VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIK 118
Cdd:PRK10619 118 IQVLGLSKQEareRAVKYLAKVGIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQ 197
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907189171 119 KTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 160
Cdd:PRK10619 198 LAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
613-813 |
2.65e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEvdictvgledlRTKLTMIPQDPVLFVG-- 686
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 687 ---TVRYNLDPLGSHTDEMLwHVLERTFMRDTIMKLPEKLQAEVTENGE--------------------------NFSVG 737
Cdd:COG0488 78 vldTVLDGDAELRALEAELE-ELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 738 ERQLLCMARALLRNSKIILLDEATASMDSKT-----DTLVQSTikeafksCTVLTIAH-R--LNTVlnCDLVLVMENGKV 809
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNYP-------GTVLVVSHdRyfLDRV--ATRILELDRGKL 227
|
....
gi 1907189171 810 IEFD 813
Cdd:COG0488 228 TLYP 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
595-811 |
2.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV------DICTVGLE 668
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 669 DLRTKLTMIPQDPVLFVGTVRYN--LDPLGSHTDEMLWHVleRTFMRDTIMK--LPEKLQAEVTENGENFSVGERQLLCM 744
Cdd:PRK14246 87 KLRKEVGMVFQQPNPFPHLSIYDniAYPLKSHGIKEKREI--KKIVEECLRKvgLWKEVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 745 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
15-161 |
2.75e-12 |
|
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: 67.36 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIF-HGNVRENILFGEKYN-------HQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLAR 86
Cdd:cd03299 74 SYVPQNYALFpHMTVYKNIAYGLKKRkvdkkeiERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIAR 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 87 AVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 161
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTKEKLREE-LKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
597-826 |
3.13e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 67.42 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGtiiiDEVDIC-----TVGLEDLR 671
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFgerrgGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKL---------TMIPQDPVL------FVGTV-RYNldplgSHTDEM------------LWHVLERTFmrdtimklpekl 723
Cdd:COG1119 78 KRIglvspalqlRFPRDETVLdvvlsgFFDSIgLYR-----EPTDEQrerarellellgLAHLADRPF------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 724 qaevtengENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNC-DL 800
Cdd:COG1119 141 --------GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTH 212
|
250 260
....*....|....*....|....*..
gi 1907189171 801 VLVMENGKVIEF-DKPEVLAEKPDSAF 826
Cdd:COG1119 213 VLLLKDGRVVAAgPKEEVLTSENLSEA 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
597-821 |
3.67e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDP--VLFVGTV-------RYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 747
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 748 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIA-HRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
600-816 |
3.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMRYRDNTpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKLTMI 677
Cdd:PRK13639 5 RDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgePIKYDKKSLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 678 PQDP--VLFVGTVRYNL--DP--LGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 748
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVafGPlnLGLSKEEVEKRVkeaLKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 749 LRNSKIILLDEATASMD----SKTDTLVQSTIKEAFkscTVLTIAHRLNTV-LNCDLVLVMENGKVIEFDKPE 816
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKEGI---TIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
74-150 |
4.62e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 64.76 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGEI 150
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaqGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
73-163 |
5.02e-12 |
|
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: 66.44 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVD---AHVGKHVFEEcIKKTlKGKTVVLVTHQLQF-LESCDEVILLEDG 148
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDG 221
|
90
....*....|....*
gi 1907189171 149 EICEKGTHKELMEER 163
Cdd:cd03256 222 RIVFDGPPAELTDEV 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
614-811 |
5.85e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC---TVGLEDLRTKLTMIPQDPvlfVG---- 686
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP---YGslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 687 --TVRYNL-DPLGSHTDemlwhvLERTFMRDTIMKLPEK--LQAEVTENGEN-FSVGERQLLCMARALLRNSKIILLDEA 760
Cdd:PRK11308 108 rkKVGQILeEPLLINTS------LSAAERREKALAMMAKvgLRPEHYDRYPHmFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 761 TasmdSKTDTLVQSTI-------KEAFKSCTVLtIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK11308 182 V----SALDVSVQAQVlnlmmdlQQELGLSYVF-ISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-178 |
8.32e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 16 YVSQQAWIF-HGNVRENILFGEKYNHQRYQHTVHVCGlQKDLNSLPYGDLTEIGER-GVNLSGGQRQRISLARAVYANRQ 93
Cdd:PRK10851 78 FVFQHYALFrHMTVFDNIAFGLTVLPRRERPNAAAIK-AKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 94 LYLLDDPLSAVDAHVGK-------HVFEEcikktLKgKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL------ 159
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKelrrwlrQLHEE-----LK-FTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepat 230
|
170 180
....*....|....*....|..
gi 1907189171 160 ---MEERGRYAKLIHNLRGLQF 178
Cdd:PRK10851 231 rfvLEFMGEVNRLQGTIRGGQF 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
605-759 |
9.45e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.82 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIIIDEVDIctvgledlrTKLTM---- 676
Cdd:COG1137 12 SYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDI---------THLPMhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 ------IPQDPVLFVG-TVRYNLdplgshtdeMLwhVLERTFM-RDTIMKLPEKLQAE-----VTEN-GENFSVGERQLL 742
Cdd:COG1137 77 rlgigyLPQEASIFRKlTVEDNI---------LA--VLELRKLsKKEREERLEELLEEfgithLRKSkAYSLSGGERRRV 145
|
170
....*....|....*..
gi 1907189171 743 CMARALLRNSKIILLDE 759
Cdd:COG1137 146 EIARALATNPKFILLDE 162
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
597-809 |
9.65e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdicTVGLEDLRTKLTM 676
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLF--------VGtvrynLDPLGSHTDEMLwHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 748
Cdd:PRK11247 86 MFQDARLLpwkkvidnVG-----LGLKGQWRDAAL-QALAAVGLADRANEWPAAL-----------SGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 749 LRNSKIILLDEATASMDSKTDTLVQSTI-----KEAFkscTVLTIAHRLN-TVLNCDLVLVMENGKV 809
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
605-826 |
9.94e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIID--EV--------DICtvgledl 670
Cdd:PRK11432 15 RFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDgeDVthrsiqqrDIC------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 671 rtkltMIPQDPVLF----VG-TVRYNLDPLGSHTDEMLWHVLERTFMRDtimklpekLQAEVTENGENFSVGERQLLCMA 745
Cdd:PRK11432 82 -----MVFQSYALFphmsLGeNVGYGLKMLGVPKEERKQRVKEALELVD--------LAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 746 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKP 822
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQP 228
|
....
gi 1907189171 823 DSAF 826
Cdd:PRK11432 229 ASRF 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
597-809 |
9.97e-12 |
|
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: 64.97 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDlrTKLTM 676
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDpvlfvgtvrYNLDPLGSHTDEMLWHVLERTFMRDTI----------MKLPEKLQAEVTEngenFSVGERQLLCMAR 746
Cdd:cd03301 77 VFQN---------YALYPHMTVYDNIAFGLKLRKVPKDEIdervrevaelLQIEHLLDRKPKQ----LSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 747 ALLRNSKIILLDEATASMDSKTDTLVQSTIK---EAFKSCTV---------LTIAHRlntvlncdlVLVMENGKV 809
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKrlqQRLGTTTIyvthdqveaMTMADR---------IAVMNDGQI 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
597-821 |
1.04e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 676
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQ-DPVLFVGTVRYNLDPLGSH-------TDEMLWHVLErtFMRdtimkLPEKLQAEVTEngenFSVGERQLLCMARAL 748
Cdd:PRK13536 119 VPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLE--FAR-----LESKADARVSD----LSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 749 LRNSKIILLDEATASMDSKTDTLVQSTIKEAF-KSCTVLTIAH------RLntvlnCDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
614-833 |
1.05e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK--------LTMIPQDPV 682
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHgtyEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 L---FVGTV-----RYNLDPLGSHTDEMLWHVlertfmrdtimklpeKLQAEVTENGENFSVGERQLLCMARALLRNSKI 754
Cdd:PRK13549 100 LeniFLGNEitpggIMDYDAMYLRAQKLLAQL---------------KLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 755 ILLDEATASM-DSKTDTLVqsTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEkpDSAFAMLL 830
Cdd:PRK13549 165 LILDEPTASLtESETAVLL--DIIRDLKAhgIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTE--DDIITMMV 240
|
...
gi 1907189171 831 AAE 833
Cdd:PRK13549 241 GRE 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
74-150 |
1.10e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.85 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 150
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
74-150 |
1.16e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.21 E-value: 1.16e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFeeCIKKTL--KGKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM--AILHQLrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
614-810 |
1.19e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 65.01 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQ---SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDLRTKLTMIPQD---------- 680
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-----LFDSRKKINLPPQQrkiglvfqqy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 681 ---PVLfvgTVRYNLdplgshtdEMLWHVLERTFMRDTIMKLPEKLQAEVTENG--ENFSVGERQLLCMARALLRNSKII 755
Cdd:cd03297 85 alfPHL---NVRENL--------AFGLKRKRNREDRISVDELLDLLGLDHLLNRypAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 756 LLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTV-LNCDLVLVMENGKVI 810
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
582-810 |
1.22e-11 |
|
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: 65.37 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 582 FKVGTCPKDWpsrgeitfkdyrmryrDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIIID 658
Cdd:cd03234 7 WDVGLKAKNW----------------NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 659 EVDictvgledlRTKLTM------IPQDPVLFVG-TVR-----YNLDPLGSHTDEmlwhvlERTFMRDTIMKLpekLQAE 726
Cdd:cd03234 71 GQP---------RKPDQFqkcvayVRQDDILLPGlTVRetltyTAILRLPRKSSD------AIRKKRVEDVLL---RDLA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 727 VTENG----ENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAH--RLNTVLNCD 799
Cdd:cd03234 133 LTRIGgnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFD 212
|
250
....*....|.
gi 1907189171 800 LVLVMENGKVI 810
Cdd:cd03234 213 RILLLSSGEIV 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
613-833 |
1.27e-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: 67.79 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP----ASGTIIIDEVDICTVGLEDLRT----KLTMIPQDPVlf 684
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 685 vgTvryNLDPLgsHTDE------MLWH--------------VLERTFMRDtimklPEK-LQAEVTEngenFSVGERQLLC 743
Cdd:COG4172 103 --T---SLNPL--HTIGkqiaevLRLHrglsgaaararaleLLERVGIPD-----PERrLDAYPHQ----LSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 744 MARALLRNSKIILLDEATasmdskT--DTLVQSTIKEAFKSCT------VLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 814
Cdd:COG4172 167 IAMALANEPDLLIADEPT------TalDVTVQAQILDLLKDLQrelgmaLLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
250 260
....*....|....*....|
gi 1907189171 815 PEVLAEKPDSAFA-MLLAAE 833
Cdd:COG4172 241 TAELFAAPQHPYTrKLLAAE 260
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
613-811 |
1.44e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.15 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlED----LRTKLtmipqdpvlfVGTV 688
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDararLRARH----------VGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 689 RYNLDPLGSHTdeMLWHV---LERTFMRDtimklPEKLQAEVTEN---GENF-------SVGERQLLCMARALLRNSKII 755
Cdd:COG4181 96 FQSFQLLPTLT--ALENVmlpLELAGRRD-----ARARARALLERvglGHRLdhypaqlSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 756 LLDEATASMDSKTDTLVQS---TIKEAFKSCTVLT-----IAHRlntvlnCDLVLVMENGKVIE 811
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDllfELNRERGTTLVLVthdpaLAAR------CDRVLRLRAGRLVE 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
597-826 |
1.51e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 64.95 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctVGLEDLRTKLTM 676
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFvgtvrynldplgSHTDemlwhVLERTFMRDTIMKLPEK-LQAEVTE-----NGENF--------SVGERQLL 742
Cdd:cd03300 77 VFQNYALF------------PHLT-----VFENIAFGLRLKKLPKAeIKERVAEaldlvQLEGYanrkpsqlSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 743 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLA 819
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIY 219
|
....*..
gi 1907189171 820 EKPDSAF 826
Cdd:cd03300 220 EEPANRF 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
14-102 |
1.58e-11 |
|
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: 63.05 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIF-HGNVRENILFGEkyNHQRYQHTVHVCGLQKDLNSLPYGDL--TEIGERGVNLSGGQRQRISLARAVYA 90
Cdd:pfam00005 61 IGYVFQDPQLFpRLTVRENLRLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLT 138
|
90
....*....|..
gi 1907189171 91 NRQLYLLDDPLS 102
Cdd:pfam00005 139 KPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
74-161 |
1.74e-11 |
|
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: 65.00 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
90
....*....|.
gi 1907189171 151 CEKGTHKELME 161
Cdd:COG1127 221 IAEGTPEELLA 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
597-824 |
1.78e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC--TVGLEDLRTKL 674
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 675 TMIPQdpvlfvgtvRYNLDP-LGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEV--TENGENF----SVGERQLLCMARA 747
Cdd:PRK09493 80 GMVFQ---------QFYLFPhLTALENVMFGPLRVRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 748 LLRNSKIILLDEATASMDSKTD----TLVQSTIKEAFKSCTV---LTIAHRLNTVLncdlvLVMENGKVIEFDKPEVLAE 820
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGMTMVIVtheIGFAEKVASRL-----IFIDKGRIAEDGDPQVLIK 225
|
....
gi 1907189171 821 KPDS 824
Cdd:PRK09493 226 NPPS 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-163 |
2.01e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.78 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 13 PLAYVSQQAWIF-HGNVRENILFG----EKYN---HQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISL 84
Cdd:COG3840 72 PVSMLFQENNLFpHLTVAQNIGLGlrpgLKLTaeqRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 85 ARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTH 156
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrqemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPT 214
|
....*..
gi 1907189171 157 KELMEER 163
Cdd:COG3840 215 AALLDGE 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
613-811 |
2.23e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.65 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-----------DEVDICtvgleDLRTKLTMIPQD- 680
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIR-----ELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 681 ---PVLfvgTVRYNL--DP---LGshtdemlwhvLERTFMRDTIMKLPEKLQaeVTENGENF----SVGERQLLCMARAL 748
Cdd:PRK11124 92 nlwPHL---TVQQNLieAPcrvLG----------LSKDQALARAEKLLERLR--LKPYADRFplhlSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 749 LRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
613-819 |
3.40e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVdictvgledLRTKLT----------MIPQDPV 682
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTpakahqlgiyLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 LFVG-TVRYN-LDPLGSHTDEMlwhvlertfmrdtimklpEKLQAEVTENGENFS---------VGERQLLCMARALLRN 751
Cdd:PRK15439 97 LFPNlSVKENiLFGLPKRQASM------------------QKMKQLLAALGCQLDldssagsleVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 752 SKIILLDEATASMD-SKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI------EFDKPEVLA 819
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIAlsgktaDLSTDDIIQ 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
597-795 |
3.57e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYrdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICT-------VGLED 669
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNqniyerrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQDPVLF----VGTVRYNLDPLGSHTDEMLWHVLERTfMRDTimKLPEKLQAEVTENGENFSVGERQLLCMA 745
Cdd:PRK14258 86 LRRQVSMVHPKPNLFpmsvYDNVAYGVKIVGWRPKLEIDDIVESA-LKDA--DLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 746 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTV 795
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
582-813 |
4.79e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 63.32 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 582 FKVGTCPKDWPSRGEITFKDYRMRYRdntpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDE-- 659
Cdd:cd03220 10 YPTYKGGSSSLKKLGILGRKGEVGEF----WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 660 ---VDIcTVGLEDlrtKLTMIpqDPVLFVGTVrYNLDPlgshtDEMlwhvleRTFMRDTIM--KLPEKLQAEVtengENF 734
Cdd:cd03220 86 sslLGL-GGGFNP---ELTGR--ENIYLNGRL-LGLSR-----KEI------DEKIDEIIEfsELGDFIDLPV----KTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 735 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEF 812
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
.
gi 1907189171 813 D 813
Cdd:cd03220 224 G 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
74-165 |
5.16e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFL-ESCDEVILLEDGEICE 152
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
|
90
....*....|....*..
gi 1907189171 153 KGTHKELM----EERGR 165
Cdd:PRK11264 225 QGPAKALFadpqQPRTR 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-147 |
5.83e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.88 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 19 QQAWIF-HGNVRENILFG--EKYNHQRYQHTVhvcglQKDLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQL 94
Cdd:COG4136 83 QDDLLFpHLSVGENLAFAlpPTIGRAQRRARV-----EQALEEA---GLAGFADRDPAtLSGGQRARVALLRALLAEPRA 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 95 YLLDDPLSAVDAH----VGKHVFEECIKKTLkgkTVVLVTHQLQFLESCDEVILLED 147
Cdd:COG4136 155 LLLDEPFSKLDAAlraqFREFVFEQIRQRGI---PALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
612-778 |
6.14e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 612 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvGLEDLRTKLTMI-PQD---PVLfvgT 687
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 688 VRYNL----DPLGSHtDEMLWHVLERTFMRDtIMKLPEKlqaevtengeNFSVGERQLLCMARALLRNSKIILLDEATAS 763
Cdd:PRK13539 90 VAENLefwaAFLGGE-ELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*
gi 1907189171 764 MDSKTDTLVQSTIKE 778
Cdd:PRK13539 158 LDAAAVALFAELIRA 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
613-827 |
7.45e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVglEDLRTKLTMIPQDPVLFVG-TVRYN 691
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 692 L-----------DPLGSHTDEMLWHVlertFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEA 760
Cdd:PRK11607 112 IafglkqdklpkAEIASRVNEMLGLV----HMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 761 TASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSAFA 827
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
600-819 |
9.47e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 600 KDYRMR---YRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 676
Cdd:PRK15112 12 KTFRYRtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPV-----------LFVGTVRYNLDPLGSHTDEMLWHVLERTFMR-DTIMKLPEKLqaevtengenfSVGERQLLCM 744
Cdd:PRK15112 92 IFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHML-----------APGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 745 ARALLRNSKIILLDEATASMD-SKTDTLVQSTIK-EAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF-DKPEVLA 819
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERgSTADVLA 239
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
74-165 |
9.61e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 62.70 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhvgkhvfeECIKKTLK--------GKTVVLVTHQLQF-LESCDEVIL 144
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDP--------ELVGEVLDvmrdlakeGMTMVVVTHEMGFaREVADRVVF 208
|
90 100
....*....|....*....|....*
gi 1907189171 145 LEDGEICEKGTHKELME----ERGR 165
Cdd:COG1126 209 MDGGRIVEEGPPEEFFEnpqhERTR 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
597-821 |
9.92e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.21 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLV---EPASGTIIIdEVDIC-TVGLEDLRT 672
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRIIY-HVALCeKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 KL---------TMIPQDpVLFVG---TVRYNLDplgshtdEMLWHVLERTF-------MRDTIMK-LPE----------- 721
Cdd:TIGR03269 77 KVgepcpvcggTLEPEE-VDFWNlsdKLRRRIR-------KRIAIMLQRTFalygddtVLDNVLEaLEEigyegkeavgr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 722 --------KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTV-LTIAHRL 792
Cdd:TIGR03269 149 avdliemvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|.
gi 1907189171 793 NTVLN--CDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:TIGR03269 229 PEVIEdlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
63-159 |
1.02e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLES 138
Cdd:PRK11432 125 DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREK-IRELQQqfNITSLYVTHdQSEAFAV 203
|
90 100
....*....|....*....|.
gi 1907189171 139 CDEVILLEDGEICEKGTHKEL 159
Cdd:PRK11432 204 SDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
70-162 |
1.27e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.70 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 70 RGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLED 147
Cdd:PRK13536 169 RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEA 247
|
90
....*....|....*
gi 1907189171 148 GEICEKGTHKELMEE 162
Cdd:PRK13536 248 GRKIAEGRPHALIDE 262
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-162 |
1.32e-10 |
|
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: 62.07 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHG-NVRENILFGEKYNHQRyqhtvhvcGLQKDLNSLpYGDLTEIGER----GVNLSGGQRQRISLARAV 88
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLLLGAYARRRA--------KRKARLERV-YELFPRLKERrkqlAGTLSGGEQQMLAIARAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 89 YANRQLYLLDDP---LSAVdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 162
Cdd:cd03224 148 MSRPKLLLLDEPsegLAPK---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
73-159 |
1.35e-10 |
|
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: 62.14 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDaHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEIC 151
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
....*...
gi 1907189171 152 EKGTHKEL 159
Cdd:cd03263 212 CIGSPQEL 219
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
323-431 |
1.57e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 62.95 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 323 IASMVSVLmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFF 402
Cdd:cd18572 44 LLSVLSGL-FSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122
|
90 100 110
....*....|....*....|....*....|
gi 1907189171 403 MVVFILVIMAAV-FPVVLVVLAGLAVIFLI 431
Cdd:cd18572 123 QLVGGLAFMFSLsWRLTLLAFITVPVIALI 152
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
597-813 |
1.66e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRL----VEPASGTIIIDEvdictvgledlRT 672
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKLGE-----------TV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 KLTMIPQDpvlfvgtvRYNLDPlgshtDEMLWHVLERTFMRDTIMKL----------PEKLQAEVtengENFSVGERQLL 742
Cdd:COG0488 379 KIGYFDQH--------QEELDP-----DKTVLDELRDGAPGGTEQEVrgylgrflfsGDDAFKPV----GVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 743 CMARALLRNSKIILLDEAT-----ASMDSKTDTLvqstikEAFKScTVLTIAH-R--LNTVlnCDLVLVMENGKVIEFD 813
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTnhldiETLEALEEAL------DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
593-825 |
1.80e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 593 SRGEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV------- 665
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 666 ------GLEDLRTKLTMIPQdpvlfvgtvRYNldpLGSHTdEMLWHVLE---------RTFMRDTIMKLPEKLQAEVTEN 730
Cdd:PRK10619 80 kvadknQLRLLRTRLTMVFQ---------HFN---LWSHM-TVLENVMEapiqvlglsKQEARERAVKYLAKVGIDERAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 731 GE---NFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNC-DLVLVME 805
Cdd:PRK10619 147 GKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLH 226
|
250 260
....*....|....*....|
gi 1907189171 806 NGKVIEFDKPEVLAEKPDSA 825
Cdd:PRK10619 227 QGKIEEEGAPEQLFGNPQSP 246
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
64-163 |
1.83e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 64 LTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvgkHVFEecIKKTL-----KGKTVVLVTHQL-QFL 136
Cdd:PRK11231 128 INHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN---HQVE--LMRLMrelntQGKTVVTVLHDLnQAS 202
|
90 100
....*....|....*....|....*..
gi 1907189171 137 ESCDEVILLEDGEICEKGTHKELMEER 163
Cdd:PRK11231 203 RYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
613-820 |
1.85e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdiCTVGledlrtkltmipqdPVLFVGTvryNL 692
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN----GRVS--------------ALLELGA---GF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 DPlgSHTdemlwhVLERTFMRDTIMKLP-----EKLQ--AEVTENGE-------NFSVGERQLLCMARALLRNSKIILLD 758
Cdd:COG1134 100 HP--ELT------GRENIYLNGRLLGLSrkeidEKFDeiVEFAELGDfidqpvkTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 759 EATASMDS----KTDTLVQSTIKEAfksCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 820
Cdd:COG1134 172 EVLAVGDAafqkKCLARIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPeEVIAA 236
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
74-152 |
1.93e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 62.52 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLES-CDEVILLEDGEIC 151
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
.
gi 1907189171 152 E 152
Cdd:TIGR02769 231 E 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
58-162 |
2.31e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.02 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 58 SLPYGDLTEIGERGVN-LSGGQRQRISLArAVYANRQLY-LLDDPLSAVDAhvgKHVFEecIKKTLK------GKTVVLV 129
Cdd:COG4604 119 AIAYLDLEDLADRYLDeLSGGQRQRAFIA-MVLAQDTDYvLLDEPLNNLDM---KHSVQ--MMKLLRrladelGKTVVIV 192
|
90 100 110
....*....|....*....|....*....|....*
gi 1907189171 130 THQLQFlESC--DEVILLEDGEICEKGTHKELMEE 162
Cdd:COG4604 193 LHDINF-ASCyaDHIVAMKDGRVVAQGTPEEIITP 226
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
350-488 |
2.38e-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: 62.51 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 350 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAV-FPVVLVVLAGLAVI 428
Cdd:cd18546 73 DLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLdPRLALVALAALPPL 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 429 FlILLRIFHRGVQEL--KQVENISRSpwFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEN 488
Cdd:cd18546 153 A-LATRWFRRRSSRAyrRARERIAAV--NADLQETLAGIRVVQAFRRERRNAERFAELSDDY 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
597-815 |
2.45e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.07 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 669
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQDP--VLFVGTV----RYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKlqaevteNGENFSVGERQLLC 743
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVlkdvAFGPQNFGVSQEEAEALAREKLALVGISESLFEK-------NPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 744 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 815
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
617-834 |
2.67e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 617 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI-------------IIDEVDICTVGLEDLR-TKLTMIPQDPV 682
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgADMAMIFQEPM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 LFVGTVRynldPLGSHTDEMLwhVLERTFMRDTIM----------KLPEKlQAEVTENGENFSVGERQLLCMARALLRNS 752
Cdd:PRK10261 115 TSLNPVF----TVGEQIAESI--RLHQGASREEAMveakrmldqvRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 753 KIILLDEATASMdsktDTLVQSTIKEAFK------SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSA 825
Cdd:PRK10261 188 AVLIADEPTTAL----DVTIQAQILQLIKvlqkemSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
....*....
gi 1907189171 826 FAMLLAAEV 834
Cdd:PRK10261 264 YTRALLAAV 272
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
611-836 |
2.86e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 611 PLVlDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA----SGTIIIDEVdicTVGLEDLRTKLT-MIPQDPvlfv 685
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRGRKIaTIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 686 gtvRYNLDPLgsHTdeMLWHVLERTFMR---DTIMKLPEKLQAEVTENGE--------NFSVGERQLLCMARALLRNSKI 754
Cdd:PRK10418 89 ---RSAFNPL--HT--MHTHARETCLALgkpADDATLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 755 ILLDEATASMDSktdtLVQSTIKEAFKSCT------VLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKPDSAFA 827
Cdd:PRK10418 162 IIADEPTTDLDV----VAQARILDLLESIVqkralgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
250
....*....|
gi 1907189171 828 -MLLAAEVGL 836
Cdd:PRK10418 238 rSLVSAHLAL 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
614-810 |
2.96e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTvGLEDLRTKLTMIPQDPVLFVG-TVRY 690
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkEIDFKS-SKEALENGISMVHQELNLVLQrSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 691 NLdPLGSHTDEMLWhVLERTFMRDTImKLPEKLQAEV--TENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK- 767
Cdd:PRK10982 93 NM-WLGRYPTKGMF-VDQDKMYRDTK-AIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKe 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907189171 768 TDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 810
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
597-823 |
2.97e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICTVGLE--D 669
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMK---LPEKLQAEVTENGENFSVGERQLLCMAR 746
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKkaaLWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 747 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR-LNTVLNCDLVLVMENGKVIEFDKPEVLAEKPD 823
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
597-836 |
3.55e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPLV---LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 669
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQDP--VLFVGT----VRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVtengenfSVGERQLLC 743
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETvlkdVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFEL-------SGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 744 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 821
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
250
....*....|....*
gi 1907189171 822 PDsafaMLLAAEVGL 836
Cdd:PRK13643 235 VD----FLKAHELGV 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
74-145 |
3.72e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.94 E-value: 3.72e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILL 145
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
27-145 |
4.07e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.42 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 27 NVRENILFGEKYN-------HQRYQHTVHVCGLQkdlnslpygdltEIGERGV-NLSGGQRQRISLARAVYANRQLYLLD 98
Cdd:COG4525 92 NVLDNVAFGLRLRgvpkaerRARAEELLALVGLA------------DFARRRIwQLSGGMRQRVGIARALAADPRFLLMD 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 99 DPLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQ---FLEScdEVILL 145
Cdd:COG4525 160 EPFGALDALTREQMQElllDVWQRT--GKGVFLITHSVEealFLAT--RLVVM 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
613-810 |
4.09e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL----RTKLTMIPQdpvlfvgtv 688
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQ--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 689 RYNLDP--LGSHTDEM--LWHVLERTFMRDTIMKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATA 762
Cdd:PRK10535 94 RYHLLShlTAAQNVEVpaVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907189171 763 SMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVI 810
Cdd:PRK10535 174 ALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-159 |
4.11e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.18 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 23 IFHGNVRENILFG------EKYN-HQRYQHTVHVCGLQKD-LNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQL 94
Cdd:PRK13631 129 LFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEI 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 95 YLLDDPLSAVDAHvGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 159
Cdd:PRK13631 198 LIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
73-155 |
4.26e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.02 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE---EcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDG 148
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENG 217
|
....*..
gi 1907189171 149 EICEKGT 155
Cdd:COG1135 218 RIVEQGP 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-201 |
4.49e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 8 VAVNGPLAYVSQQAWIFHGNVRENILFGEKYNhqryqhtvhvcGLQKDLNSLPYGDLTE----------IGERGVNLSGG 77
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGARIN-----------GYKGDMDELVERSLRQaalwdevkdkLKQSGLSLSGG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 78 QRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGthk 157
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG--- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907189171 158 elmeerGRYAKLIhnlrglQFKDPEHIYNvamvetlkeSPAQRD 201
Cdd:PRK14243 232 ------GRYGYLV------EFDRTEKIFN---------SPQQQA 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
75-154 |
5.22e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 75 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEV 504
|
....
gi 1907189171 151 CEKG 154
Cdd:PRK15134 505 VEQG 508
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
63-148 |
5.33e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIK---KTlkGKTVVLVTHQLQ---F 135
Cdd:PRK11248 117 GLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwqET--GKQVLLITHDIEeavF 194
|
90
....*....|...
gi 1907189171 136 LEScdEVILLEDG 148
Cdd:PRK11248 195 MAT--ELVLLSPG 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
618-792 |
9.98e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.60 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 618 NLNIQSGQTVGIVGRTGSGKSSLG--MALFrlVEPASGTIIIDEVDiCTVGLEDLRtKLTMIPQDPVLFVG-TVRYN--- 691
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLnlIAGF--LTPASGSLTLNGQD-HTTTPPSRR-PVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 692 -LDP---LGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD-- 765
Cdd:PRK10771 95 gLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*....
gi 1907189171 766 --SKTDTLVQSTIKEafKSCTVLTIAHRL 792
Cdd:PRK10771 164 lrQEMLTLVSQVCQE--RQLTLLMVSHSL 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-170 |
1.10e-09 |
|
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: 59.92 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQ 93
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 94 LYLLDDPLSAVDAHVgKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM-EERGRYAKLI 170
Cdd:cd03288 177 ILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
74-150 |
1.14e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 59.37 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV----FEecIKKTlKGKTVVLVTHQLQFLESCDEVILLEDGE 149
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
.
gi 1907189171 150 I 150
Cdd:COG4181 224 L 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
589-818 |
1.20e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 589 KDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLE 668
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 669 DLRTKLTMIPQD-PVLFVGTVRyNLDPLGSHTdemlWH-VLERTFMRDTimklpEKLQAEVTENG---------ENFSVG 737
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVR-ELVAIGRYP----WHgALGRFGAADR-----EKVEEAISLVGlkplahrlvDSLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 738 ERQLLCMARALLRNSKIILLDEATASMD--SKTDT--LVQSTIKEafKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 812
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDiaHQVDVlaLVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
....*.
gi 1907189171 813 DKPEVL 818
Cdd:PRK10575 230 GTPAEL 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
28-154 |
1.31e-09 |
|
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: 58.92 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 28 VRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 106
Cdd:cd03266 95 ARENLEyFAGLYGLKGDELTARLEELADRLGMEELLD-----RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 107 HVGKHVFEecIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 154
Cdd:cd03266 170 MATRALRE--FIRQLRalGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
74-152 |
1.31e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.91 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVyANR-QLYLLDDPLSAVDAHVGK---HVFEEcIKKTlkGKTVVLVTHQLQFLESCDE-VILLEDG 148
Cdd:COG2884 138 LSGGEQQRVAIARAL-VNRpELLLADEPTGNLDPETSWeimELLEE-INRR--GTTVLIATHDLELVDRMPKrVLELEDG 213
|
....
gi 1907189171 149 EICE 152
Cdd:COG2884 214 RLVR 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
74-150 |
1.43e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 58.83 E-value: 1.43e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-161 |
1.60e-09 |
|
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: 59.09 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHG-NVRENIL-------FGEKYNHQRYQHTVHVCGLQKDLNSLpygdlteigerGVNLSGGQRQRISLA 85
Cdd:cd03218 77 IGYLPQEASIFRKlTVEENILavleirgLSKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAhvgKHVFE-ECIKKTLKGKTV-VLVT-HQL-QFLESCDEVILLEDGEICEKGTHKELME 161
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDP---IAVQDiQKIIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
613-825 |
1.68e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVgtvRYNL 692
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQ---RPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 DPLgSHTDEMLWHVLERTFM-----------RDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEAT 761
Cdd:PRK14271 113 FPM-SIMDNVLAGVRAHKLVprkefrgvaqaRLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 762 ASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSA 825
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
610-809 |
1.84e-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: 57.83 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 610 TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPV---LFV 685
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 686 G-TVRYNLDpLGSHtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASM 764
Cdd:cd03215 92 DlSVAENIA-LSSL-----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907189171 765 DSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 809
Cdd:cd03215 136 DVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
614-834 |
1.87e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK--------LTMIPQDPV 682
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHgtwDGEIYWSGSPLKASNIRDTERAgiviihqeLTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 L---FVGTvryNLDPLGSHTDEMLWHVLERTFMRDtiMKLPEklqAEVTENGENFSVGERQLLCMARALLRNSKIILLDE 759
Cdd:TIGR02633 96 AeniFLGN---EITLPGGRMAYNAMYLRAKNLLRE--LQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 760 ATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEkpDSAFAMLLAAEV 834
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSE--DDIITMMVGREI 242
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-150 |
2.27e-09 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 58.33 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 13 PLAYVSQQAWIF-HGNVRENILFG----EKYNHQRYQHTVHVC---GLQKDLNSLPYgdlteigergvNLSGGQRQRISL 84
Cdd:TIGR01277 71 PVSMLFQENNLFaHLTVRQNIGLGlhpgLKLNAEQQEKVVDAAqqvGIADYLDRLPE-----------QLSGGQRQRVAL 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 85 ARAVYANRQLYLLDDPLSAVDAHVGKHVFeeCIKKTL---KGKTVVLVTHQLQFL-ESCDEVILLEDGEI 150
Cdd:TIGR01277 140 ARCLVRPNPILLLDEPFSALDPLLREEML--ALVKQLcseRQRTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
64-156 |
2.62e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 64 LTEIGER-GVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFL-ESC 139
Cdd:PRK11124 131 LKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAetGITQVIVTHEVEVArKTA 208
|
90
....*....|....*..
gi 1907189171 140 DEVILLEDGEICEKGTH 156
Cdd:PRK11124 209 SRVVYMENGHIVEQGDA 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
613-818 |
2.68e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC---TVGLedLRTKLTMIPQDPVLFVG-TV 688
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqTAKI--MREAVAIVPEGRRVFSRmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 689 RYNLDPLGSHTDEMLWHV-LERTFmrdtimKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 767
Cdd:PRK11614 98 EENLAMGGFFAERDQFQErIKWVY------ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 768 TDTLVQSTIKEAF-KSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVL 818
Cdd:PRK11614 172 IIQQIFDTIEQLReQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
620-777 |
2.77e-09 |
|
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: 58.57 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 620 NIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdictvgLEDLRTKLTMIPQDpvlFVGTVRynlDPLGSHT 699
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE--------LDTVSYKPQYIKAD---YEGTVR---DLLSSIT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 700 DEMLWHvlerTFMRDTIMKlPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIK 777
Cdd:cd03237 87 KDFYTH----PYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
612-834 |
3.23e-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: 59.73 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 612 LVLDGLNLNIQ-----SGQTVgIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDlRTKLTMIP-------- 678
Cdd:COG4148 9 LRRGGFTLDVDftlpgRGVTA-LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV-----LQD-SARGIFLPphrrrigy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 679 --QDPVLFVG-TVRYNLD------PLGSHTDEM--------LWHVLERTfmrdtimklPEKLqaevtengenfSVGERQL 741
Cdd:COG4148 82 vfQEARLFPHlSVRGNLLygrkraPRAERRISFdevvellgIGHLLDRR---------PATL-----------SGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 742 LCMARALLRNSKIILLDEATASMD--SKTDTL--VQSTIKEAfkSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP- 815
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDlaRKAEILpyLERLRDEL--DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLa 219
|
250
....*....|....*....
gi 1907189171 816 EVLAEKPDSAFAMLLAAEV 834
Cdd:COG4148 220 EVLSRPDLLPLAGGEEAGS 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
64-163 |
3.38e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 64 LTEIG------ERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEC--IKKTlKGKTVVLVTHQLQF 135
Cdd:PRK09984 137 LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQN-DGITVVVTLHQVDY 215
|
90 100
....*....|....*....|....*....
gi 1907189171 136 -LESCDEVILLEDGEICEKGTHKELMEER 163
Cdd:PRK09984 216 aLRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
73-155 |
3.41e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.43 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGR 218
|
....*.
gi 1907189171 150 ICEKGT 155
Cdd:PRK11153 219 LVEQGT 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
74-154 |
3.44e-09 |
|
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: 57.50 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVD----AHVGKHVFEECIKktlKGKTVVLVTHQLQFLESCDE-VILLEDG 148
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNG 205
|
....*.
gi 1907189171 149 EICEKG 154
Cdd:cd03298 206 RIAAQG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
614-809 |
3.57e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALfrlvepaSGTIIIDEVDICTVGL------------EDLRTKLT----MI 677
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELlgrtvqregrlaRDIRKSRAntgyIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 678 PQDPVLFVGTVRYNLdPLGSHTDEMLWHVLERTFMRdtiMKLPEKLQAeVTENG---------ENFSVGERQLLCMARAL 748
Cdd:PRK09984 93 QQFNLVNRLSVLENV-LIGALGSTPFWRTCFSWFTR---EQKQRALQA-LTRVGmvhfahqrvSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 749 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKV 809
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
74-150 |
3.85e-09 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 57.18 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFeecikKTLK-----GKTVVLVTHQL--QFLESCDEVILLE 146
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM-----SLLRrladtGRTIICSIHQPssEIFELFDKLLLLS 186
|
....
gi 1907189171 147 DGEI 150
Cdd:cd03213 187 QGRV 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
595-815 |
3.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 595 GEITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVGL---- 667
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI-PANLkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 668 --EDLRTKLTMIPQDP--VLFVGTVRYNL--DP--LGSHTDEMLWHVLERTfmrdTIMKLPEKLqaeVTENGENFSVGER 739
Cdd:PRK13645 84 evKRLRKEIGLVFQFPeyQLFQETIEKDIafGPvnLGENKQEAYKKVPELL----KLVQLPEDY---VKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 740 QLLCMARALLRNSKIILLDEATASMDSKTD----TLVQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 814
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERLNKEYKKR--IIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
.
gi 1907189171 815 P 815
Cdd:PRK13645 235 P 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
614-810 |
3.93e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII--DEV------DICTVGLEDLRTKLTMIPQDPV--- 682
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVtfngpkSSQEAGIGIIHQELNLIPQLTIaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 LFVGtvRYNLDPLGShtdeMLWHVlertfMRDTIMKLPEKLQAEVTEN---GEnFSVGERQLLCMARALLRNSKIILLDE 759
Cdd:PRK10762 100 IFLG--REFVNRFGR----IDWKK-----MYAEADKLLARLNLRFSSDklvGE-LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 760 ATasmDSKTDTLVQS---TIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 810
Cdd:PRK10762 168 PT---DALTDTETESlfrVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-159 |
4.01e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 25 HGNVRENILFGEKYN-------HQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLL 97
Cdd:PRK11000 89 HLSVAENMSFGLKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 98 DDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 159
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIE-ISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-170 |
4.27e-09 |
|
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: 58.33 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPyGDLT-EIGERGVNLSGGQRQRISLARAVYANRQLY 95
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFP-GQLDfVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 96 LLDDPLSAVDAhvgkhVFEECIKKTLK----GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 170
Cdd:cd03289 161 LLDEPSAHLDP-----ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-145 |
4.60e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 15 AYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKdlnslpYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQ 93
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLER------FALPDTILTKNIAeLSGGEKQRISLIRNLQFMPK 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 94 LYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESCDEVILL 145
Cdd:PRK10247 158 VLLLDEITSALDES-NKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
53-166 |
4.66e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 53 QKDLNSLPYGDLTEIG----------ERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVfEECIKKTLK 122
Cdd:PRK14271 133 RKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLAD 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907189171 123 GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELME-----ERGRY 166
Cdd:PRK14271 212 RLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSspkhaETARY 261
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
74-162 |
6.43e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.07 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEK 153
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
....*....
gi 1907189171 154 GTHKELMEE 162
Cdd:PRK13644 217 GEPENVLSD 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
73-161 |
6.81e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEIC 151
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
90
....*....|
gi 1907189171 152 EKGTHKELME 161
Cdd:PRK14267 228 EVGPTRKVFE 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
74-161 |
7.18e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 59.31 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGK 503
|
90
....*....|..
gi 1907189171 150 ICEKGTHKELME 161
Cdd:COG4172 504 VVEQGPTEQVFD 515
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-132 |
8.11e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 28 VRENILFGEKYNHQRyQHTVHVC----GLQkDLNSLPYGdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSA 103
Cdd:PRK13539 90 VAENLEFWAAFLGGE-ELDIAAAleavGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
90 100 110
....*....|....*....|....*....|
gi 1907189171 104 VDAHvGKHVFEECIKKTLK-GKTVVLVTHQ 132
Cdd:PRK13539 158 LDAA-AVALFAELIRAHLAqGGIVIAATHI 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
74-160 |
9.38e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.51 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEIC 151
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
|
....*....
gi 1907189171 152 EKGTHKELM 160
Cdd:PRK10070 245 QVGTPDEIL 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
614-811 |
1.21e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV--------DICTVGLEDLRTKLTMIPQdpvlfv 685
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttAALAAGVAIIYQELHLVPE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 686 GTVRYNLdplgshtdeMLWH-------VLERTFMRDTIMKLpEKLQAEVTENG--ENFSVGERQLLCMARALLRNSKIIL 756
Cdd:PRK11288 94 MTVAENL---------YLGQlphkggiVNRRLLNYEAREQL-EHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 757 LDEATASMDSKTDTLVQSTIKEAFKSCTV-LTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRViLYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
73-162 |
1.29e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.12 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTLKGK--TVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKL 221
|
90
....*....|..
gi 1907189171 151 CEKGTHKELMEE 162
Cdd:PRK13640 222 LAQGSPVEIFSK 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
62-154 |
1.31e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.93 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 62 GDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-C 139
Cdd:PRK09536 127 TGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyC 206
|
90
....*....|....*
gi 1907189171 140 DEVILLEDGEICEKG 154
Cdd:PRK09536 207 DELVLLADGRVRAAG 221
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
350-452 |
1.47e-08 |
|
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: 57.06 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 350 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPV-VLVVLAGLAVI 428
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVlTLVTLAVVPLA 149
|
90 100
....*....|....*....|....
gi 1907189171 429 FLILLRIfhrgvqeLKQVENISRS 452
Cdd:cd18551 150 FLIILPL-------GRRIRKASKR 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
606-815 |
1.58e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 606 YRDNTP---LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV----DICTVG------------ 666
Cdd:PRK13631 31 FDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdKKNNHElitnpyskkikn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 667 LEDLRTKLTMIPQDP--VLFVGTVRYNL--DP--LGSHTDE---MLWHVLERTFMRDTIMKlpeklqaevtENGENFSVG 737
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDImfGPvaLGVKKSEakkLAKFYLNKMGLDDSYLE----------RSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 738 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 815
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
612-823 |
1.59e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 612 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFR---LVEP--ASGTIIIDEVDICTVGLE--DLRTKLTMIPQDPVLF 684
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 685 VGTVRYNL------DPLGSHTDEMLWHVLERTFMRDTImklPEKLQaevtENGENFSVGERQLLCMARALLRNSKIILLD 758
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEV---KDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 759 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV---------LNCDLVLV-MENGKVIEFDKPEVLAEKPD 823
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAarvsdmtafFNVELTEGgGRYGYLVEFDRTEKIFNSPQ 251
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
73-161 |
1.85e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.89 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDG 148
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
90
....*....|...
gi 1907189171 149 EICEKGTHKELME 161
Cdd:TIGR03269 246 EIKEEGTPDEVVA 258
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
63-154 |
1.92e-08 |
|
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: 55.28 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CD 140
Cdd:cd03264 119 NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESlCN 197
|
90
....*....|....
gi 1907189171 141 EVILLEDGEICEKG 154
Cdd:cd03264 198 QVAVLNKGKLVFEG 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
592-791 |
2.02e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.84 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 592 PSRGEITFKDYRMRYrDNTPLV-------LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdict 664
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 665 vgledlRTKLTMIPQDPVLFVGTVR----YnldPLGShtDEMLwhvlERTFMRDTIMKLPEKLQAE--VTENG------- 731
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLRdqiiY---PDSS--EDMK----RRGLSDKDLEQILDNVQLThiLEREGgwsavqd 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 732 --ENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAfkSCTVLTIAHR 791
Cdd:TIGR00954 579 wmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
597-808 |
2.58e-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: 53.61 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdictvgledlRTKLTM 676
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQdpvlfvgtvrynldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIIL 756
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 757 LDEATASMDSKTDTLVQSTIKEaFKsCTVLTIAH-R--LNTVlnCDLVLVMENGK 808
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-YP-GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
74-152 |
2.76e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.85 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVERfCQRVMVMDNGQ 229
|
...
gi 1907189171 150 ICE 152
Cdd:PRK10419 230 IVE 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
59-159 |
2.96e-08 |
|
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: 55.07 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 59 LPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQF 135
Cdd:cd03265 116 LDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEefGMTILLTTHYMEE 194
|
90 100
....*....|....*....|....*
gi 1907189171 136 LES-CDEVILLEDGEICEKGTHKEL 159
Cdd:cd03265 195 AEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-161 |
3.72e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 28 VRENIL-FGEKYNHQRYQHTVHVCGLqkdlnsLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 105
Cdd:PRK13537 97 VRENLLvFGRYFGLSAAAARALVPPL------LEFAKLENKADAKVgELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 106 AHvGKHVFEECIKKTL-KGKTVVLVTHqlqFLES----CDEVILLEDGEICEKGTHKELME 161
Cdd:PRK13537 171 PQ-ARHLMWERLRSLLaRGKTILLTTH---FMEEaerlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
613-823 |
3.85e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIidevdictvgledlrtkltmipQDPVLFVGTVrynl 692
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------------------RNGKLRIGYV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 dPLGSHTDEMLWHVLERtFMR-------DTIMKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATAS 763
Cdd:PRK09544 73 -PQKLYLDTTLPLTVNR-FLRlrpgtkkEDILPALKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 764 MDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVL-NCDLVLVMeNGKVIEFDKPEVLAEKPD 823
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
332-523 |
4.29e-08 |
|
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: 55.57 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 332 FGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIM 411
Cdd:cd18576 52 FSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 412 AAVFP-VVLVVLAGLAVIFLIlLRIFHRGVQEL-KQV-ENISRSpwFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEn 488
Cdd:cd18576 132 FFISWkLTLLMLATVPVVVLV-AVLFGRRIRKLsKKVqDELAEA--NTIVEETLQGIRVVKAFTREDYEIERYRKALER- 207
|
170 180 190
....*....|....*....|....*....|....*
gi 1907189171 489 sshllYFNCALRwFALRMDILMNIVTFVVALLVTL 523
Cdd:cd18576 208 -----VVKLALK-RARIRALFSSFIIFLLFGAIVA 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
74-159 |
4.36e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEICE 152
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVE 232
|
....*..
gi 1907189171 153 KGTHKEL 159
Cdd:PRK14246 233 WGSSNEI 239
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
316-471 |
4.64e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 55.65 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 316 HMYQLVYIASMVsVLMFGIIKGFTFTNTTLM---ASSSLHN-RV--FNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVR 389
Cdd:cd18565 49 PRGQLWLLGGLT-VAAFLLESLFQYLSGVLWrrfAQRVQHDlRTdtYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 390 LPFHAENFLQQFFMVVFILVIMA------AVFPVVLV-VLAGLAVIFLILLRIFHRGVQElkQVENISrspwfSHITSSI 462
Cdd:cd18565 128 LDDGANSIIRVVVTVLGIGAILFylnwqlALVALLPVpLIIAGTYWFQRRIEPRYRAVRE--AVGDLN-----ARLENNL 200
|
....*....
gi 1907189171 463 QGLGVIHAY 471
Cdd:cd18565 201 SGIAVIKAF 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
613-817 |
5.26e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGlEDLRTKLTMIPQD-------PVL 683
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRIRSPR-DAIRAGIAYVPEDrkgeglvLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 684 fvgTVRYN-----LDPLGSHTdeMLWHVLERTFMRDTIMKL---PEKLQAEVTengeNFSVGERQLLCMARALLRNSKII 755
Cdd:COG1129 346 ---SIRENitlasLDRLSRGG--LLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 756 LLDEATASMD--SKTDtlVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMENGKVI-EFDKPEV 817
Cdd:COG1129 417 ILDEPTRGIDvgAKAE--IYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-160 |
5.34e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.59 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 25 HGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLL 97
Cdd:PRK10771 85 HLTVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLL 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 98 DDPLSAVD----AHVGKHVFEECIKKTLkgkTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 160
Cdd:PRK10771 154 DEPFSALDpalrQEMLTLVSQVCQERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
74-160 |
6.04e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 54.84 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKhvfeECIKKTLK-----GKTVVLVTHQLQFLESC-DEVILLED 147
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRS----QIINLMLElqeklGISYIYVSQHLGIVKHIsDKVLVMHQ 225
|
90
....*....|...
gi 1907189171 148 GEICEKGTHKELM 160
Cdd:COG4167 226 GEVVEYGKTAEVF 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-132 |
6.56e-08 |
|
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: 53.52 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 1 MQLQKGVVAVNG-PLA-----YVSQQAWIFHGN-------VRENILFgekYN--HQRYQHTVHvcglqkdlNSLPYGDLT 65
Cdd:TIGR01189 50 LRPDSGEVRWNGtPLAeqrdePHENILYLGHLPglkpelsALENLHF---WAaiHGGAQRTIE--------DALAAVGLT 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 66 EIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTL-KGKTVVLVTHQ 132
Cdd:TIGR01189 119 GFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
74-139 |
6.67e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 6.67e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTL-KGKTVVLVTHQLQFLESC 139
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GVARLEALLAQHAeQGGMVILTTHQDLPVASD 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-152 |
7.74e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 27 NVRENI-----LFGEKYNHQRYQ--HTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDD 99
Cdd:PRK10584 104 NALENVelpalLRGESSRQSRNGakALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 100 PLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGEICE 152
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-150 |
8.48e-08 |
|
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: 53.69 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 24 FHGN--VRENILFG-------EKYNHQRYQHTVHVCGLQKDLNsLPYGdlteigergvNLSGGQRQRISLARAVYANRQL 94
Cdd:cd03220 95 FNPEltGRENIYLNgrllglsRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 95 YLLDDPLSAVDAHvgkhvF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:cd03220 164 LLIDEVLAVGDAA-----FqEKCQRRlrelLKQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-170 |
9.05e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYL 96
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 97 LDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 170
Cdd:TIGR01271 1377 LDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
614-765 |
9.40e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTvGLEDLRTKLTMIPQDPVLF-----VGTV 688
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFhhltvAEHI 1024
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 689 RYNLDPLGSHTDEMLWHVleRTFMRDTimklpeKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 765
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEM--EAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-185 |
9.91e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 55.23 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 13 PLAYVSQQAWIF-HGNVRENILFGEKYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISL 84
Cdd:PRK11607 92 PINMMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVAL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 85 ARAVYANRQLYLLDDPLSAVDahvgkhvfeecikKTLKGKTvvlvthQLQFLEscdevILLEDGEICEKGTH--KELMEE 162
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALD-------------KKLRDRM------QLEVVD-----ILERVGVTCVMVTHdqEEAMTM 216
|
170 180
....*....|....*....|....*
gi 1907189171 163 RGRYAklIHNlRG--LQFKDPEHIY 185
Cdd:PRK11607 217 AGRIA--IMN-RGkfVQIGEPEEIY 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
74-149 |
1.15e-07 |
|
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: 51.68 E-value: 1.15e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKtLKGkTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-YPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
74-161 |
1.16e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.25 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE--TVRQLKeqkGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
90
....*....|.
gi 1907189171 151 CEKGTHKELME 161
Cdd:PRK13635 219 LEEGTPEEIFK 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
69-134 |
1.19e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.89 E-value: 1.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 69 ERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD----AHVgkhvfEECIKKtLKGK-TVVLVTHQLQ 134
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKI-----EELILE-LKKDyTIVIVTHNMQ 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-159 |
1.31e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.24 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 23 IFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPygdlTEIGERG-VNLSGGQRQRISLARAVYANRQLYLLDDPL 101
Cdd:PRK13645 103 LFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 102 SAVDAHvGKHVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 159
Cdd:PRK13645 179 GGLDPK-GEEDFINLFERLNKeyKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
297-428 |
1.37e-07 |
|
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: 54.02 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 297 SQNNKTACNVDQTLQDTKHHMYQLVYIAsmVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLM 376
Cdd:cd18577 30 TDFGSGESSPDEFLDDVNKYALYFVYLG--IGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELT 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 377 NRFSKDMDELDV----RLPFhaenFLQQFFMVV------FI------LVIMaAVFPVVLVVLAGLAVI 428
Cdd:cd18577 108 SRLTSDTNLIQDgigeKLGL----LIQSLSTFIagfiiaFIyswkltLVLL-ATLPLIAIVGGIMGKL 170
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
597-810 |
1.37e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.73 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLrtkLTM 676
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQD-------PVLFVGTV---RYN----LDPLGSHTDEMLWHVLERTFMrdtimklpekLQAEVTENGEnFSVGERQLL 742
Cdd:PRK15056 83 VPQSeevdwsfPVLVEDVVmmgRYGhmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 743 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF-KSCTVLTIAHRLNTVLN-CDLVlVMENGKVI 810
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
63-161 |
1.50e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.64 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-AHvgkHVFEECIKKTL---KGKTVVLVTHQLQFLE 137
Cdd:PRK10575 136 GLKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAH---QVDVLALVHRLsqeRGLTVIAVLHDINMAA 212
|
90 100
....*....|....*....|....*
gi 1907189171 138 S-CDEVILLEDGEICEKGTHKELME 161
Cdd:PRK10575 213 RyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
74-160 |
1.91e-07 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 53.20 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARA-------VYANRQLYLLDDPLSAVD-AHVgKHVFEecIKKTL--KGKTVVLVTHQL----QFlesC 139
Cdd:COG4559 134 LSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTSALDlAHQ-HAVLR--LARQLarRGGGVVAVLHDLnlaaQY---A 207
|
90 100
....*....|....*....|.
gi 1907189171 140 DEVILLEDGEICEKGTHKELM 160
Cdd:COG4559 208 DRILLLHQGRLVAQGTPEEVL 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
613-812 |
2.06e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdictvgledlrtKLTMIPQDPVLFVGTVRYNL 692
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-------------SIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKT-DTL 771
Cdd:PTZ00243 742 LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907189171 772 VQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKViEF 812
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV-EF 861
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
16-150 |
2.30e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.72 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 16 YVSQQAWIF-HGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQ 93
Cdd:PRK11144 80 YVFQDARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPE 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 94 LYLLDDPLSAVDAHVGKHV--FEECIKKTLKgKTVVLVTHQLQ-FLESCDEVILLEDGEI 150
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELlpYLERLAREIN-IPILYVSHSLDeILRLADRVVVLEQGKV 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
613-816 |
2.70e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVL--------F 684
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditvqeL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 685 VGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLpeklqaeVTENGENFSVGERQLLCMARALLRNSKIILLDEATASM 764
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 765 D--SKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLV-MENGKVIEFDKPE 816
Cdd:PRK10253 175 DisHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPK 229
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
351-519 |
2.73e-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: 52.92 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 351 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvRLPFHAenfLQQFFMVVFILVIMAAVFPVVLVVLAGLAVI-- 428
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVE-RLIADG---IPQGITNVLTLVGVAIILFSINPKLALLTLIpi 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 429 -FLILL-RIFHRGVQEL-KQVENISrspwfSHITS----SIQGLGVIHAYDKKDDCISKFKTLNDEnsshllYFNCALRw 501
Cdd:cd18778 151 pFLALGaWLYSKKVRPRyRKVREAL-----GELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180
....*....|....*....|..
gi 1907189171 502 fALRmdiLMNI----VTFVVAL 519
Cdd:cd18778 219 -AMK---LWAIfhplMEFLTSL 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
321-470 |
2.95e-07 |
|
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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 52.90 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 321 VYIASMVSVLMFGIIKGFTFTNTTLMASSS----LHNRVFNKIVRSPMSFFDTTPTGRLMnrfsKDMDELD-VRlpfhae 395
Cdd:cd18783 43 VLTIGVVIALLFEGILGYLRRYLLLVATTRidarLALRTFDRLLSLPIDFFERTPAGVLT----KHMQQIErIR------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 396 NFL-QQFFMVVF----ILVIMAAVF----PVVLVVLAGLAVIFLIL---LRIFHRGVQELKQVEnISRSpwfSHITSSIQ 463
Cdd:cd18783 113 QFLtGQLFGTLLdatsLLVFLPVLFfyspTLALVVLAFSALIALIIlafLPPFRRRLQALYRAE-GERQ---AFLVETVH 188
|
....*..
gi 1907189171 464 GLGVIHA 470
Cdd:cd18783 189 GIRTVKS 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-159 |
3.07e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.47 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 17 VSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVcGLQKDLNSLPYGDltEIGER----GVNLSGGQRQRISLARAVYANR 92
Cdd:PRK14239 91 VFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSP 167
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 93 QLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 159
Cdd:PRK14239 168 KIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
73-163 |
3.48e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEIC 151
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKII 244
|
90
....*....|...
gi 1907189171 152 EKG-THKELMEER 163
Cdd:PRK13651 245 KDGdTYDILSDNK 257
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
74-162 |
3.88e-07 |
|
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: 52.75 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGE 149
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQIlnlLKD-LQREL-GLAILFITHDLGVVaEIADRVAVMYAGR 228
|
90
....*....|...
gi 1907189171 150 ICEKGTHKELMEE 162
Cdd:COG0444 229 IVEEGPVEELFEN 241
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
329-442 |
4.40e-07 |
|
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: 52.64 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 329 VLMFGIIKGFTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD----VRLPFHAENFL 398
Cdd:cd18780 49 LGVVLIGSIATFLRSWLFTLAGervvarLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQnavtVNLSMLLRYLV 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 399 QQFFMVVFILV-------IMAAVFPVVLVVlaglAVIFLILLRIFHRGVQE 442
Cdd:cd18780 129 QIIGGLVFMFTtswkltlVMLSVVPPLSIG----AVIYGKYVRKLSKKFQD 175
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-150 |
4.48e-07 |
|
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: 51.64 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 23 IFHGNVRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLY 95
Cdd:cd03292 90 LPDRNVYENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTIL 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 96 LLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDE-VILLEDGEI 150
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
74-181 |
4.57e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKH----VFEECIKKtlKGKTVVLVTHQLQ-FLESCDEVILLEDG 148
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK-GRKemmeMFYKLHKE--KGLTTVLVTHSMEdAARYADQIVVMHKG 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907189171 149 EICEKGTHKEL------MEERG-------RYAKLIHNLRGLQFKDP 181
Cdd:PRK13634 223 TVFLQGTPREIfadpdeLEAIGldlpetvKFKRALEEKFGISFPKP 268
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
74-160 |
5.41e-07 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 51.62 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESC-DEVILLEDGEI 150
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
90
....*....|
gi 1907189171 151 CEKGTHKELM 160
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-187 |
6.54e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 20 QAWIFHGNVRENILFGEKynhqRYQHTVhvcglqKDLNSLPYGDLTEIG-ERGV------NLSGGQRQRISLARAVYANR 92
Cdd:PRK13646 95 ESQLFEDTVEREIIFGPK----NFKMNL------DEVKNYAHRLLMDLGfSRDVmsqspfQMSGGQMRKIAIVSILAMNP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 93 QLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 169
Cdd:PRK13646 165 DIIVLDEPTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
170 180
....*....|....*....|.
gi 1907189171 170 ---IHNLRGLQfKDPEHIYNV 187
Cdd:PRK13646 244 higLPEIVQLQ-YDFEQKYQT 263
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
74-193 |
6.68e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.63 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEIC 151
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 152 EKGTHKE------LMEERG----RYAKLIHNLRGLQFKDPEHIYNV-AMVETL 193
Cdd:PRK13633 224 MEGTPKEifkeveMMKKIGldvpQVTELAYELKKEGVDIPSDILTIdEMVNEL 276
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
614-809 |
7.35e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA-SGTIIID--EVDICTVgLEDLRTKLTMIPQD-------PVL 683
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINgkPVDIRNP-AQAIRAGIAMVPEDrkrhgivPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 684 FVGTvRYNLDPLGSHTDEM-LWHVLERTFMRDTIMKLPEKLQAEVTENGeNFSVGERQLLCMARALLRNSKIILLDEATA 762
Cdd:TIGR02633 355 GVGK-NITLSVLKSFCFKMrIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907189171 763 SMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 809
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
613-834 |
7.55e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMipQDPVLF-----VGT 687
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF--QHYALFrhmtvFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 688 VRYNLDPLGSHtdemlwhvlER---TFMRDTIMKLPEKLQAEVTEN--GENFSVGERQLLCMARALLRNSKIILLDEATA 762
Cdd:PRK10851 95 IAFGLTVLPRR---------ERpnaAAIKAKVTQLLEMVQLAHLADryPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 763 SMDSKTDTLVQSTIK---EAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 834
Cdd:PRK10851 166 ALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
609-811 |
7.89e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 609 NTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALfrLVEPA----SGTIIIDEVDICTVGLEDlRTKLTMIP--QDPV 682
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEE-RAHLGIFLafQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 683 LFVGT-------VRYN----------LDPLgshtdEMLWHVLERtfmrdtiMKLPEKLQAEVTEN-GENFSVGER---QL 741
Cdd:CHL00131 95 EIPGVsnadflrLAYNskrkfqglpeLDPL-----EFLEIINEK-------LKLVGMDPSFLSRNvNEGFSGGEKkrnEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 742 LCMAralLRNSKIILLDEATASMDskTDTL--VQSTIKEAFKSCT-VLTIAH--RLNTVLNCDLVLVMENGKVIE 811
Cdd:CHL00131 163 LQMA---LLDSELAILDETDSGLD--IDALkiIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
604-823 |
8.22e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 604 MRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTV---GLEDLRTKLTM 676
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMsrsRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 677 IPQDPVLFVG-TVRYNLD-PLGSHTDemlwhvLERTFMRDTIMKlpeKLQAEVTENGEN-----FSVGERQLLCMARALL 749
Cdd:PRK11831 89 LFQSGALFTDmNVFDNVAyPLREHTQ------LPAPLLHSTVMM---KLEAVGLRGAAKlmpseLSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 750 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 823
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
70-162 |
8.84e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.22 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 70 RGVN--LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTL-KGKTVVLVTHQLQFLESC--DEVIL 144
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-INKLReEGKSVLIITHYQRLLDYIkpDRVHV 177
|
90
....*....|....*...
gi 1907189171 145 LEDGEICEKGThKELMEE 162
Cdd:cd03217 178 LYDGRIVKSGD-KELALE 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-146 |
9.04e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQA---WIFHGNVRENILFGeKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVY 89
Cdd:PRK15056 80 VAYVPQSEevdWSFPVLVEDVVMMG-RYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIA 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 90 ANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLE 146
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
320-470 |
9.15e-07 |
|
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: 51.44 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 320 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSkdmdELD-VRlpfhaeNFL 398
Cdd:cd18782 46 VVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS----ELDtIR------GFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 399 QQ---------FFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLrIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIH 469
Cdd:cd18782 116 TGtalttlldvLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF-LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVK 194
|
.
gi 1907189171 470 A 470
Cdd:cd18782 195 A 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
74-159 |
9.68e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.07 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTH-QLQFLESCDEVILLEDGEICE 152
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDP-ENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 1907189171 153 KGTHKEL 159
Cdd:PRK14247 226 WGPTREV 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
74-150 |
1.13e-06 |
|
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: 49.74 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDahVG--KHVFEECIKKTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEI 150
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
306-464 |
1.14e-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: 51.36 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 306 VDQTLQDTKHHMYQLVYIASMVSVLMFGI---IKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRF-SK 381
Cdd:cd18555 29 IDNVIVPGNLNLLNVLGIGILILFLLYGLfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAnSN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 382 DMdeldVRlpfhaeNFLQQ--------FFMVVFILVIMaAVFPVVL--VVLAGLAVIFLILLrIFHRGVQELKQVENISR 451
Cdd:cd18555 109 VY----IR------QILSNqvisliidLLLLVIYLIYM-LYYSPLLtlIVLLLGLLIVLLLL-LTRKKIKKLNQEEIVAQ 176
|
170
....*....|...
gi 1907189171 452 SPWFSHITSSIQG 464
Cdd:cd18555 177 TKVQSYLTETLYG 189
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
315-483 |
1.17e-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: 51.29 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 315 HHMYQLVYIASmVSVLMFGIIK-GFTFTNTTLMA--SSSLHNRV----FNKIVRSPMSFFDTTPTGRLMNRFSkdmDELD 387
Cdd:cd18570 35 SGDINLLNIIS-IGLILLYLFQsLLSYIRSYLLLklSQKLDIRLilgyFKHLLKLPLSFFETRKTGEIISRFN---DANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 388 VRlpfhaeNFLQQ--------FFMVVFILVIMAA----VFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRspwf 455
Cdd:cd18570 111 IR------EAISSttislfldLLMVIISGIILFFynwkLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELN---- 180
|
170 180
....*....|....*....|....*...
gi 1907189171 456 SHITSSIQGLGVIHAYDKKDDCISKFKT 483
Cdd:cd18570 181 SYLIESLKGIETIKSLNAEEQFLKKIEK 208
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
74-143 |
1.35e-06 |
|
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: 48.90 E-value: 1.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 74 LSGGQRQRISLARAV----YANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVI 143
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
70-161 |
1.79e-06 |
|
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: 49.98 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 70 RGVNLSGGQRQRISLARAVYANRQLYLLDDP---LSAVdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVI 143
Cdd:COG0410 133 RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAY 207
|
90
....*....|....*...
gi 1907189171 144 LLEDGEICEKGTHKELME 161
Cdd:COG0410 208 VLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
74-162 |
1.84e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVD--AHVGKHVFEECIKKTlkGKTVVLVTHQL-QFLESCDEVILLEDGEI 150
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkARIEMMQLFESIHQS--GQTVVLVTHLMdDVADYADYVYLLEKGHI 222
|
90
....*....|..
gi 1907189171 151 CEKGTHKELMEE 162
Cdd:PRK13643 223 ISCGTPSDVFQE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
74-162 |
2.19e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 51.34 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQF-LESCDEVILLEDGEI 150
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKI 506
|
90
....*....|..
gi 1907189171 151 CEKGTHKELMEE 162
Cdd:TIGR03269 507 VKIGDPEEIVEE 518
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
353-517 |
2.51e-06 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 50.14 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 353 NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdVRLPFHA-ENFLQQFFMVVFILVIMAAVFP----VVLVVLAGLAV 427
Cdd:cd18549 79 RDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI-SELAHHGpEDLFISIITIIGSFIILLTINVpltlIVFALLPLMII 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 428 IFLILLRIFHRGVQELK-QVENISrspwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDE--NSSHLLYFNCAlrWFAL 504
Cdd:cd18549 158 FTIYFNKKMKKAFRRVReKIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRflESKKKAYKAMA--YFFS 230
|
170
....*....|...
gi 1907189171 505 RMDILMNIVTFVV 517
Cdd:cd18549 231 GMNFFTNLLNLVV 243
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-159 |
2.58e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.80 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 23 IFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLY 95
Cdd:PRK13652 91 IFSPTVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 96 LLDDPLSAVDAHVGKHV--FEECIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKEL 159
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-132 |
2.77e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.96 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILF---GEKYNHQRYQHTVHVCGLQkDLNslpyGDLTEIGERGVNLSGGQRQRISLARAVYA 90
Cdd:COG4178 428 VLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLG-HLA----ERLDEEADWDQVLSLGEQQRLAFARLLLH 502
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907189171 91 NRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQ 132
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQL-LREELPGTTVISVGHR 543
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-161 |
3.08e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.26 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHG-NVRENIL----FGEKYNHQRyqhtvhvcglQKDLNSLpygdLTEIG------ERGVNLSGGQRQRI 82
Cdd:COG1137 80 IGYLPQEASIFRKlTVEDNILavleLRKLSKKER----------EERLEEL----LEEFGithlrkSKAYSLSGGERRRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 83 SLARAVYANRQLYLLDDPLSAVD--AhvgkhVFEecIKK---TLKGKTV-VLVT-HQLQ-FLESCDEVILLEDGEICEKG 154
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDpiA-----VAD--IQKiirHLKERGIgVLITdHNVReTLGICDRAYIISEGKVLAEG 218
|
....*..
gi 1907189171 155 THKELME 161
Cdd:COG1137 219 TPEEILN 225
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
351-438 |
3.65e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 49.40 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 351 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDEldVR-----LPFhaenFLQQFFMVVFILVIMAAVFPVV-LVVLAG 424
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSL--VQrflafGPF----LLGNLLTLVVGLVVMLVLSPPLaLVALAS 147
|
90
....*....|....
gi 1907189171 425 LAVIFLILLRIFHR 438
Cdd:cd18543 148 LPPLVLVARRFRRR 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-173 |
3.87e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.44 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 14 LAYVSQQAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDL-NSLPYgdlteigergvNLSGGQRQRISLA 85
Cdd:PRK13641 89 LVFQFPEAQLFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLiSKSPF-----------ELSGGQMRRVAIA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 86 RAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERG 164
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
....*....
gi 1907189171 165 RYAKliHNL 173
Cdd:PRK13641 238 WLKK--HYL 244
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
74-195 |
4.13e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.74 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQFL-ESCDEVILLEDGE 149
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIElllELQQK--ENMALVLITHDLALVaEAAHKIIVMYAGQ 231
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907189171 150 ICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVETLKE 195
Cdd:PRK11022 232 VVETGKAHDI------------------FRAPRHPYTQALLRALPE 259
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-132 |
4.51e-06 |
|
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: 48.26 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 11 NGPLA-----YVSQQAWIFHGN-------VRENIlfgekynhqRYQHTVHvcGLQKDLNSLPYGDLTEIGERGVN-LSGG 77
Cdd:cd03231 61 GGPLDfqrdsIARGLLYLGHAPgikttlsVLENL---------RFWHADH--SDEQVEEALARVGLNGFEDRPVAqLSAG 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 78 QRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ 132
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
71-162 |
4.68e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 71 GVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhvgKHVFEecIKKTLK-----GKTVVLVTHQL-QFLESCDEVIL 144
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP---ISVID--IKRIIEhlrdsGLGVLITDHNVrETLAVCERAYI 209
|
90
....*....|....*...
gi 1907189171 145 LEDGEICEKGTHKELMEE 162
Cdd:PRK10895 210 VSQGHLIAHGTPTEILQD 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
74-180 |
5.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.08 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLE-SCDEVILLEDGEI 150
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907189171 151 CEKGTHKELMEERG-------RYAKLIHNLRGLQFKD 180
Cdd:PRK13636 221 ILQGNPKEVFAEKEmlrkvnlRLPRIGHLMEILKEKD 257
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
75-206 |
5.44e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 75 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF-------EECikktlkGKTVVLVTHQLQFLES-CDEVILLE 146
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLnlmmdlqQEL------GLSYVFISHDLSVVEHiADEVMVMY 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 147 DGEICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVE-TLKESPAQRDEDAVL 206
Cdd:PRK11308 230 LGRCVEKGTKEQI------------------FNNPRHPYTQALLSaTPRLNPDDRRERIKL 272
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
74-161 |
5.49e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.98 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDGEICE 152
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
....*....
gi 1907189171 153 KGTHKELME 161
Cdd:PRK13648 223 EGTPTEIFD 231
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
351-519 |
5.50e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.01 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 351 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFP-------VVLVVLA 423
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalivlAVVPVLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 424 GLAVIFLILLRIFHRGVQELkqveNisrspwfSHITSS----IQGLGVIHAYDKKDDCISKFKTLNDE--NSS-HLLYFN 496
Cdd:cd18540 157 VVSIYFQKKILKAYRKVRKI----N-------SRITGAfnegITGAKTTKTLVREEKNLREFKELTEEmrRASvRAARLS 225
|
170 180
....*....|....*....|...
gi 1907189171 497 calrwfALRMDILMNIVTFVVAL 519
Cdd:cd18540 226 ------ALFLPIVLFLGSIATAL 242
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
74-143 |
6.15e-06 |
|
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: 47.32 E-value: 6.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 74 LSGGQRQRISLARAVYAN--RQLYLLDDPLSAVDaHVGKHVFEECIKKTL-KGKTVVLVTHQLQFLESCDEVI 143
Cdd:cd03238 88 LSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
73-169 |
7.12e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.45 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKL 220
|
90 100
....*....|....*....|.
gi 1907189171 151 CEKGTHKELM--EERGRYAKL 169
Cdd:PRK13632 221 IAQGKPKEILnnKEILEKAKI 241
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
306-545 |
7.22e-06 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 48.79 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 306 VDQTLQDTKHHMYQLVYIASMVSVLMfGIIKGFTFTNTTLMAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRF 379
Cdd:cd18556 29 TDLLTSSSSDSYNYIVVLAALYVITI-SATKLLGFLSLYLQSSlrveliISISSSYFRYLYEQPKTFFVKENSGDITQRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 380 SKDMDELDVRLPFHAENF----LQQFFMVVFIL----VIMAAVFPVvlvvlagLAVIFLILLRIFHRGVQELKQ-VENIS 450
Cdd:cd18556 108 NQASNDLYTLVRNLSTNIlpplLQLIIAIVVILssgdYFVAALFLL-------YAVLFVINNTIFTKKIVSLRNdLMDAG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 451 RSPwFSHITSSIQGLGVIHAYDKKDDCISKFK-TLNDENSSHLLYFNCALRWFALrmDILMNIVTFVVALLVTLSFSSIS 529
Cdd:cd18556 181 RKS-YSLLTDSVKNIVAAKQNNAFDFLFKRYEaTLTNDRNSQKRYWKLTFKMLIL--NSLLNVILFGLSFFYSLYGVVNG 257
|
250
....*....|....*....
gi 1907189171 530 ASSKG---LSLSYIIQLSG 545
Cdd:cd18556 258 QVSIGhfvLITSYILLLST 276
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
613-811 |
7.50e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDlrtklTMIPQDPVLF-----VGT 687
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLpwrnvQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 688 VRYNLDPLGshtdemlwhvLERTFMRDTIMKLPEKLQAEvtENGENF----SVGERQLLCMARALLRNSKIILLDEATAS 763
Cdd:PRK11248 91 VAFGLQLAG----------VEKMQRLEIAHQMLKKVGLE--GAEKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 764 MDSKT----DTLVQSTIKEAFKSctVLTIAHRLN--TVLNCDLVLVMEN-GKVIE 811
Cdd:PRK11248 159 LDAFTreqmQTLLLKLWQETGKQ--VLLITHDIEeaVFMATELVLLSPGpGRVVE 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
73-155 |
8.44e-06 |
|
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: 47.82 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDP---LSAVDAHVGKHVFEEcIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDG 148
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPaagLNPEETEELAELIRE-LRE--RGITVLLVEHDMDVVMSlADRVTVLDQG 219
|
....*..
gi 1907189171 149 EICEKGT 155
Cdd:cd03219 220 RVIAEGT 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
623-816 |
8.47e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 623 SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIdevdictVGLEDLRTKLTMipqdpvlfvgtvrynldplgshtdem 702
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 703 lwhvlertfmrdtimklpEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQS-------T 775
Cdd:smart00382 48 ------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrllL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907189171 776 IKEAFKSCTVLTIAHRLNTVLncDLVLVMENGKVIEFDKPE 816
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
605-811 |
8.98e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE--PASGTIIIDEVDIC--TVGLEDLRTKLTmiPQD 680
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGreASLIDAIGRKGD--FKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 681 PVLFVGTVRYNldplgshtDEMLWhvlERTFmrdtimklpeklqaevtengENFSVGERQLLCMARALLRNSKIILLDEA 760
Cdd:COG2401 115 AVELLNAVGLS--------DAVLW---LRRF--------------------KELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 761 TASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTV--LNCDLVLVMENGKVIE 811
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAgiTLVVATHHYDVIddLQPDLLIFVGYGGVPE 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
613-814 |
9.74e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.11 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAS--GTIIIDEVDIctvgledlrTKLTM-----IPQDPVLFV 685
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP---------TKQILkrtgfVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 686 G-TVRynldplgshtdEMLWHV----LERTFMRDTIMKLPEKLQAEV----TEN---GENF----SVGERQLLCMARALL 749
Cdd:PLN03211 154 HlTVR-----------ETLVFCsllrLPKSLTKQEKILVAESVISELgltkCENtiiGNSFirgiSGGERKRVSIAHEML 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 750 RNSKIILLDEATASMDSKTD-TLVQSTIKEAFKSCTVLTIAHRLNTVL--NCDLVLVMENGKVIEFDK 814
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEGRCLFFGK 290
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
70-150 |
1.04e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.50 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 70 RGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDG 148
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
..
gi 1907189171 149 EI 150
Cdd:PRK11629 222 RL 223
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
323-521 |
1.29e-05 |
|
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: 47.78 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 323 IASMVSVLmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhaENFLQQFF 402
Cdd:cd18548 47 LLALLGLI-AGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQV--------QNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 403 MVVF---ILVI------------MAAVFPVVLVVLAG-LAVIFLILLRIFHRgVQelKQVENISRSpwfshITSSIQGLG 466
Cdd:cd18548 118 RMLVrapIMLIgaiimafrinpkLALILLVAIPILALvVFLIMKKAIPLFKK-VQ--KKLDRLNRV-----VRENLTGIR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 467 VIHAYDKKDDCISKFKTLNDENSSHLLYfncALRWFALRMDILMNIVTFVVALLV 521
Cdd:cd18548 190 VIRAFNREDYEEERFDKANDDLTDTSLK---AGRLMALLNPLMMLIMNLAIVAIL 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
70-160 |
1.47e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 70 RGVnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVILLED 147
Cdd:PLN03211 205 RGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSE 282
|
90
....*....|...
gi 1907189171 148 GEICEKGTHKELM 160
Cdd:PLN03211 283 GRCLFFGKGSDAM 295
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
65-159 |
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 1907189171 65 TEIGERGV--NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCD 140
Cdd:TIGR00955 156 TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFD 235
|
90
....*....|....*....
gi 1907189171 141 EVILLEDGEICEKGTHKEL 159
Cdd:TIGR00955 236 KIILMAEGRVAYLGSPDQA 254
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
596-810 |
1.51e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 596 EITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-----------DEVD 661
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 662 ICTVGLEDLRTKLTMIPQDPVLF--VGTV----RYNLdplgshtdemlwhvLERTFMRDTI-----MKLP----EKLQAE 726
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKKIKEIRrrVGVVfqfaEYQL--------------FEQTIEKDIIfgpvsMGVSkeeaKKRAAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 727 VTE-----------NGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNT 794
Cdd:PRK13651 148 YIElvgldesylqrSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDN 227
|
250
....*....|....*..
gi 1907189171 795 VLN-CDLVLVMENGKVI 810
Cdd:PRK13651 228 VLEwTKRTIFFKDGKII 244
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
269-488 |
1.54e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 47.89 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 269 FFLMMGSSAFST---WWLGIWLDRgsqvVCASQNNKTACNVDQTLQDTKhhmYQLVYIASMVSVLMFGIIKGFTFTNTTL 345
Cdd:cd18564 5 LLALLLETALRLlepWPLKVVIDD----VLGDKPLPGLLGLAPLLGPDP---LALLLLAAAALVGIALLRGLASYAGTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 346 MAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhaENFLQ----QFFMVVFILVIMAAVF 415
Cdd:cd18564 78 TALvgqrvvLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAI--------QDLLVsgvlPLLTNLLTLVGMLGVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 416 PVV-----LVVLAGLAVIFLILLRI---FHRGVQELKQVEnisrspwfSHITSSIQ-GLG---VIHAYDKKDDCISKFKT 483
Cdd:cd18564 150 FWLdwqlaLIALAVAPLLLLAARRFsrrIKEASREQRRRE--------GALASVAQeSLSairVVQAFGREEHEERRFAR 221
|
....*
gi 1907189171 484 LNDEN 488
Cdd:cd18564 222 ENRKS 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
597-790 |
1.55e-05 |
|
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: 48.39 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEvdicTVGLEdlrt 672
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMItgqeQPDSGTIEIGE----TVKLA---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 kltmipqdpvlFVGTVRYNLDPlgshtDEMLWHVLERTFmrDTIMKLPEKLQAEVTENGENF------------SVGERQ 740
Cdd:TIGR03719 389 -----------YVDQSRDALDP-----NKTVWEEISGGL--DIIKLGKREIPSRAYVGRFNFkgsdqqkkvgqlSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907189171 741 LLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIkEAFKSCTVLtIAH 790
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVV-ISH 498
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
74-132 |
1.59e-05 |
|
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: 45.99 E-value: 1.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikkTLKGKTVVLVTHQ 132
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KELGITVISVGHR 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
605-821 |
1.69e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTPL-VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRtKLTM--IPQDP 681
Cdd:COG3845 264 SVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR-RLGVayIPEDR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 682 vLFVG-----TVRYNLDpLGSHTDEMLWHvleRTFM-RDTIMKLPEKLQAE---VTENGE----NFSVGERQLLCMARAL 748
Cdd:COG3845 343 -LGRGlvpdmSVAENLI-LGRYRRPPFSR---GGFLdRKAIRAFAEELIEEfdvRTPGPDtparSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 749 LRNSKIIL-------LDEATASMdsktdtlVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVI-EFDKPEVL 818
Cdd:COG3845 418 SRDPKLLIaaqptrgLDVGAIEF-------IHQRLLELRDAgAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEAT 490
|
...
gi 1907189171 819 AEK 821
Cdd:COG3845 491 REE 493
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
613-773 |
1.84e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRT-KLTMIPQDPVLFVG-T 687
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 688 VRYNLD-PL---GSHTDEMLWHVLErtfmrdtiMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATAS 763
Cdd:PRK11629 104 ALENVAmPLligKKKPAEINSRALE--------MLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170
....*....|.
gi 1907189171 764 MDSKT-DTLVQ 773
Cdd:PRK11629 176 LDARNaDSIFQ 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
614-790 |
2.26e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.41 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED---LRTKLTMIPQDPVLFVG-TVR 689
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 690 YNLD-PL---GSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATA 762
Cdd:PRK10908 98 DNVAiPLiiaGASGDDIRRRVsaaLDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|..
gi 1907189171 763 SMDsktDTLVQSTIK--EAFK--SCTVLTIAH 790
Cdd:PRK10908 167 NLD---DALSEGILRlfEEFNrvGVTVLMATH 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
74-161 |
2.39e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 150
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
90
....*....|.
gi 1907189171 151 CEKGTHKELME 161
Cdd:PRK11650 214 EQIGTPVEVYE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
6-150 |
3.05e-05 |
|
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: 46.11 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 6 GVVAVNG-PL---------AYVSQQ-AWIFHGNVRENILF------GEKYNHQRYQHTVHVCGLqKDLNSLPYGdlteiG 68
Cdd:cd03234 65 GQILFNGqPRkpdqfqkcvAYVRQDdILLPGLTVRETLTYtailrlPRKSSDAIRKKRVEDVLL-RDLALTRIG-----G 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 69 ERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ-----LQFLescDEVI 143
Cdd:cd03234 139 NLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLF---DRIL 215
|
....*..
gi 1907189171 144 LLEDGEI 150
Cdd:cd03234 216 LLSSGEI 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
612-765 |
3.21e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 612 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvGLEDlRTKLTMIPQDPVLFvgtVRYN 691
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI----------GLAK-GIKLGYFAQHQLEF---LRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 692 LDPLgSHtdemlwhvLERTFMRDTIMKLPEKLQA------EVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 765
Cdd:PRK10636 392 ESPL-QH--------LARLAPQELEQKLRDYLGGfgfqgdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
64-177 |
3.36e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.52 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 64 LTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE--ECIKKTlKGKTVVLVTHQL-QFLESC 139
Cdd:PRK10253 133 ITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEllSELNRE-KGYTLAAVLHDLnQACRYA 211
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907189171 140 DEVILLEDGEICEKGTHKELMEergryAKLIHNLRGLQ 177
Cdd:PRK10253 212 SHLIALREGKIVAQGAPKEIVT-----AELIERIYGLR 244
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
74-162 |
3.42e-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: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVlnlLED-LQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGK 235
|
90
....*....|...
gi 1907189171 150 ICEKGTHKELMEE 162
Cdd:COG4608 236 IVEIAPRDELYAR 248
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
306-382 |
3.61e-05 |
|
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: 46.35 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 306 VDQTLQDTKHHMYQLVYIA-SMVSVLMFGIIkgFTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 378
Cdd:cd18573 26 ASKESGDIEIFGLSLKTFAlALLGVFVVGAA--ANFGRVYLLRIAGerivarLRKRLFKSILRQDAAFFDKNKTGELVSR 103
|
....
gi 1907189171 379 FSKD 382
Cdd:cd18573 104 LSSD 107
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
72-150 |
3.71e-05 |
|
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: 47.10 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 72 VNLSGGQRQRISLARAVYANRQLYLLD------DPlsavdahVGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVI 143
Cdd:COG4615 456 TDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVFYTELLPELKarGKTVIAISHDDRYFDLADRVL 528
|
....*..
gi 1907189171 144 LLEDGEI 150
Cdd:COG4615 529 KMDYGKL 535
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
74-185 |
3.93e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 46.99 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVyANR-QLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQL----QFlesCDEVILL 145
Cdd:COG4172 157 LSGGQRQRVMIAMAL-ANEpDLLIADEPTTALDVTVQAQILD--LLKDLQrelGMALLLITHDLgvvrRF---ADRVAVM 230
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907189171 146 EDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIY 185
Cdd:COG4172 231 RQGEIVEQGPTAEL------------------FAAPQHPY 252
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
617-828 |
4.27e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 617 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVGLEDL-RTKLTMIPQDPVLFVGTVRYNLD-- 693
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 694 -PLGSHTDEmLWHVLERTFMRdtiMKLPEKLQAEVTengeNFSVGERQLLCMARALLR-------NSKIILLDEATASMD 765
Cdd:PRK03695 94 qPDKTRTEA-VASALNEVAEA---LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 766 SKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMENGKVI------EFDKPEVLAEkpdsAFAM 828
Cdd:PRK03695 166 VAQQAALDRLLSElCQQGIAVVMSSHDLNHTLrHADRVWLLKQGKLLasgrrdEVLTPENLAQ----VFGV 232
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
320-431 |
4.82e-05 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 45.93 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 320 LVYIASMVSVLMFGIIkgftFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 399
Cdd:cd18589 44 LLTIASAVSEFVCDLI----YNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMW 119
|
90 100 110
....*....|....*....|....*....|...
gi 1907189171 400 QFFMVVFILVIMAAVFP-VVLVVLAGLAVIFLI 431
Cdd:cd18589 120 YLARGLFLFIFMLWLSPkLALLTALGLPLLLLV 152
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
613-765 |
4.92e-05 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 45.18 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL 692
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 693 DPLGS-HTDEMLWHVLertfmrdtimklpeklqAEVTENG------ENFSVGERQLLCMARALLRNSKIILLDEATASMD 765
Cdd:cd03231 95 RFWHAdHSDEQVEEAL-----------------ARVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
331-431 |
5.01e-05 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 46.15 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 331 MFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVI 410
Cdd:cd18784 51 VAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVF 130
|
90 100
....*....|....*....|..
gi 1907189171 411 MAAV-FPVVLVVLAGLAVIFLI 431
Cdd:cd18784 131 MFKLsWQLSLVTLIGLPLIAIV 152
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
613-823 |
5.92e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.56 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDP--VLFVGTVRY 690
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 691 NL--DPLGSHTD-EMLWHVLERTFMRDTIMKLPEKLQaevtengENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 767
Cdd:PRK13652 99 DIafGPINLGLDeETVAHRVSSALHMLGLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 768 -TDTLVQ--STIKEAFkSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 823
Cdd:PRK13652 172 gVKELIDflNDLPETY-GMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
74-155 |
6.14e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 45.53 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARA------VYANRQLYLLDDPLSAVD-AHvGKHVFEecIKKTL---KGKTVVLVTHQL----QFlesC 139
Cdd:PRK13548 135 LSGGEQQRVQLARVlaqlwePDGPPRWLLLDEPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---A 208
|
90
....*....|....*.
gi 1907189171 140 DEVILLEDGEICEKGT 155
Cdd:PRK13548 209 DRIVLLHQGRLVADGT 224
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
67-149 |
6.24e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.68 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 67 IGERGVNLSGGQRQRISLARAVyANRQ----LYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEV 142
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWI 241
|
....*....
gi 1907189171 143 ILL--EDGE 149
Cdd:cd03271 242 IDLgpEGGD 250
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
323-436 |
6.62e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. 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). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 45.57 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 323 IASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRfskdMDELD-VRlpfhaeNFLQ-Q 400
Cdd:cd18588 49 LVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELEsIR------QFLTgS 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907189171 401 FFMVV----FILVIMAAVF----PVVLVVLAGLAVIFLILLRIF 436
Cdd:cd18588 119 ALTLVldlvFSVVFLAVMFyyspTLTLIVLASLPLYALLSLLVT 162
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
67-159 |
7.74e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 67 IGERGVNLSGGQRQRISLARAVYA---NRQLYLLDDPLSavdahvGKHvFEEcIKKTL--------KGKTVVLVTHQLQF 135
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTT------GLH-FDD-IKKLLevlqrlvdKGNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 1907189171 136 LESCDEVILL------EDGEICEKGTHKEL 159
Cdd:TIGR00630 895 IKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
329-385 |
7.97e-05 |
|
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: 45.61 E-value: 7.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 329 VLMFGIIKGFTFTNTTLMA------SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDE 385
Cdd:cd18574 49 LGLYLLQSLLTFAYISLLSvvgervAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQE 111
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
73-150 |
9.43e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGE 149
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGR 217
|
.
gi 1907189171 150 I 150
Cdd:COG1129 218 L 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
597-767 |
1.01e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTvgLEDLRT 672
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVagleRITSGEIWIGGRVVNE--LEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 KLTMIPQDpvlfvgtvrYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKlQAEVTENGE-------NFSVGERQLLCMA 745
Cdd:PRK11650 77 DIAMVFQN---------YALYPHMSVRENMAYGLKIRGMPKAEIEERVAE-AARILELEPlldrkprELSGGQRQRVAMG 146
|
170 180
....*....|....*....|..
gi 1907189171 746 RALLRNSKIILLDEATASMDSK 767
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAK 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
74-150 |
1.03e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.83 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDP-----LSAVDAhvgkhvFEECIKkTLKGkTVVLVTHQLQFLES-CDEVILLED 147
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA------LEEALD-DFPG-TVLLVSHDRYFLDRvATRILEFED 504
|
...
gi 1907189171 148 GEI 150
Cdd:COG0488 505 GGV 507
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
74-159 |
1.03e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.07 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICE 152
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIK 217
|
....*..
gi 1907189171 153 KGTHKEL 159
Cdd:PRK13639 218 EGTPKEV 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
74-159 |
1.05e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.11 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEIC 151
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE-GRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
....*...
gi 1907189171 152 EKGTHKEL 159
Cdd:PRK13650 220 STSTPREL 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
64-215 |
1.12e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 64 LTEI-GERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDE 141
Cdd:NF000106 134 LTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHE 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 142 VILLEDGEICEKGTHKELMEERGRyaklihnlRGLQFKdPEHiynVAMVETLKESPAQRDEDAVLASGDEKDEG 215
Cdd:NF000106 214 LTVIDRGRVIADGKVDELKTKVGG--------RTLQIR-PAH---AAELDRMVGAIAQAGLDGIAGATADHEDG 275
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
597-826 |
1.16e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.32 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTVGLEDlRT 672
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 KLTMIpQDPVLFVG-TVRYN----LDPLGSHTDEMLWHVLERTFMrdtimklpEKLQAEVTENGENFSVGERQLLCMARA 747
Cdd:PRK09452 88 VNTVF-QSYALFPHmTVFENvafgLRMQKTPAAEITPRVMEALRM--------VQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 748 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDS 824
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
..
gi 1907189171 825 AF 826
Cdd:PRK09452 239 LF 240
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
329-523 |
1.21e-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: 44.78 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 329 VLMFGIIKGFTFTNTTLMA---SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVV 405
Cdd:cd18575 46 ALVLALASALRFYLVSWLGervVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 406 FILVIMAAVFP-VVLVVLAGLAVIFLILLrIFHRGVQEL-----KQVENISrspwfSHITSSIQGLGVIHAYDKKDDCIS 479
Cdd:cd18575 126 GGLVMLFITSPkLTLLVLLVIPLVVLPII-LFGRRVRRLsrasqDRLADLS-----AFAEETLSAIKTVQAFTREDAERQ 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907189171 480 KFKTLNDEnsshllYFNCALRWFALRmDILMNIVTFVVALLVTL 523
Cdd:cd18575 200 RFATAVEA------AFAAALRRIRAR-ALLTALVIFLVFGAIVF 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
69-149 |
1.55e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 69 ERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLED 147
Cdd:PRK10982 130 AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRD 209
|
..
gi 1907189171 148 GE 149
Cdd:PRK10982 210 GQ 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
74-155 |
1.71e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.95 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVD--AHVGKHVFEECIKKTLkGKTVVLVTHQLQF-LESCDEVILLeDGEI 150
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQVALYDLIDQLRREL-DCAVLMVSHDLHLvMAKTDEVLCL-NHHI 198
|
....*
gi 1907189171 151 CEKGT 155
Cdd:PRK09544 199 CCSGT 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
67-148 |
1.78e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 67 IGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVI 143
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELL 1091
|
....*
gi 1907189171 144 LLEDG 148
Cdd:PLN03140 1092 LMKRG 1096
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
72-149 |
1.87e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 72 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlKGKTVVLVTHQLQFLESCDEVIL 144
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKTALVVEHDLAVLDYLSDRIH 143
|
....*
gi 1907189171 145 LEDGE 149
Cdd:cd03222 144 VFEGE 148
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
621-820 |
2.03e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.04 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 621 IQSGQTVGIVGRTGSGKSSLGMAL-FRL---VEpASGTIIIDEVDIctvGLEDLRTKLTMIPQDPvLFVG--TVRYNLD- 693
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALaFRSpkgVK-GSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPtlTVREHLMf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 694 ----PLGSHTD-----EMLWHVLERTFMR---DTIMKLPEKLQAevtengenFSVGERQLLCMARALLRNSKIILLDEAT 761
Cdd:TIGR00955 123 qahlRMPRRVTkkekrERVDEVLQALGLRkcaNTRIGVPGRVKG--------LSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189171 762 ASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNC--DLVLVMENGKVIEFDKPEVLAE 820
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
74-164 |
2.08e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.84 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTL-KGKTVVLVTHQLQFL-ESCDEVILLEDGEIC 151
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP-AGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQIL 215
|
90
....*....|....*....
gi 1907189171 152 EKG------THKELMEERG 164
Cdd:PRK13638 216 THGapgevfACTEAMEQAG 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
74-196 |
2.13e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.96 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEICE 152
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLA 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907189171 153 KG-----THKELMEERGRYAKLIHNLrglqFKDPEHIYNVAMVETLKES 196
Cdd:PRK13647 219 EGdksllTDEDIVEQAGLRLPLVAQI----FEDLPELGQSKLPLTVKEA 263
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
75-189 |
2.31e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.31 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 75 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN--LLQQLQremGLSLIFIAHDLAVVKHiSDRVLVMYLGHA 240
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907189171 151 CEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAM 189
Cdd:PRK15079 241 VELGTYDEV------------------YHNPLHPYTKAL 261
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
601-809 |
2.37e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 601 DYRMRYRDNTPLVLDGL---------NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGlED 669
Cdd:PRK11288 247 GYRPRPLGEVRLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgkPIDIRSPR-DA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 670 LRTKLTMIPQD----PVLFVGTVRYNLD--------PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVtengeNFSVG 737
Cdd:PRK11288 326 IRAGIMLCPEDrkaeGIIPVHSVADNINisarrhhlRAGCLINNRWEAENADRFIRSLNIKTPSREQLIM-----NLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 738 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 809
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
73-150 |
2.38e-04 |
|
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: 43.87 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVdAHVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES-CDEVILLEDGE 149
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGL-NPEETEELAELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGR 230
|
.
gi 1907189171 150 I 150
Cdd:COG0411 231 V 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-133 |
2.57e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.49 E-value: 2.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 66 EIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGK-TVVLVTHQL 133
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
74-145 |
2.72e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 74 LSGGQRQRISLARAVYA---NRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILL 145
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
74-195 |
2.81e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.54 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKtLKGK---TVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDP-TGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEI 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 151 CEKGTHKEL------MEERGR----YAKLIHNLRGLQFKDPE-HIYNVAMVETLKE 195
Cdd:PRK13642 219 IKEAAPSELfatsedMVEIGLdvpfSSNLMKDLRKNGFDLPEkYLSEDELVELLAD 274
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
74-194 |
2.85e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.50 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGK--TVVLVTHQLQFLES-CDEVILLEDGEI 150
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK-IKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 151 CEKGTHKELMEERGRYAK----------LIHNLRGLQFKDPEHIYNV--AMVETLK 194
Cdd:PRK13637 224 ELQGTPREVFKEVETLESiglavpqvtyLVRKLRKKGFNIPDDIFTIeeAKEEILK 279
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
73-150 |
2.93e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.54 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQF-LESCDEVILLEDG 148
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEG 225
|
..
gi 1907189171 149 EI 150
Cdd:COG1101 226 RI 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
75-148 |
2.96e-04 |
|
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: 43.19 E-value: 2.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 75 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDG 148
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
75-149 |
3.38e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 3.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189171 75 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTlkgKTVVLVTHQLQFLESCDEVILLEDGE 149
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-147 |
3.40e-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: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 9 AVNGPLAYVSQQAWIFHG-NVRENILFGEKYNHQRYQHTvhvcglQKDLNSLpygdLTEIG------ERGVNLSGGQRQR 81
Cdd:TIGR01257 1000 AVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA------QLEMEAM----LEDTGlhhkrnEEAQDLSGGMQRK 1069
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189171 82 ISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTlKGKTVVLVTHQLqflescDEVILLED 147
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHM------DEADLLGD 1128
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
74-235 |
3.53e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKT---VVLVTHQLQFL-ESCDEVILLEDGE 149
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 150 ICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVETLKESPAQRDEDA----VLASGDEKDEgKEPETEEfvD 225
Cdd:PRK10261 247 AVETGSVEQI------------------FHAPQHPYTRALLAAVPQLGAMKGLDYprrfPLISLEHPAK-QEPPIEQ--D 305
|
170
....*....|
gi 1907189171 226 TNAPAHQLIQ 235
Cdd:PRK10261 306 TVVDGEPILQ 315
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
74-161 |
4.07e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQ--LYLLDDPlsavdaHVGKHVFE-ECIKKTLK-----GKTVVLVTHQLQFLESCDEVILL 145
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEP------SIGLHQRDnRRLINTLKrlrdlGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100
....*....|....*....|..
gi 1907189171 146 ------EDGEICEKGTHKELME 161
Cdd:TIGR00630 563 gpgageHGGEVVASGTPEEILA 584
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
63-150 |
5.66e-04 |
|
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: 42.32 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES- 138
Cdd:cd03267 142 DLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEAl 220
|
90
....*....|..
gi 1907189171 139 CDEVILLEDGEI 150
Cdd:cd03267 221 ARRVLVIDKGRL 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-149 |
6.93e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.89 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 4 QKGVVAVNGPLAYVSQQAwifhgnVRENILFGEKYNHQ----RYQHTVHVC-------GLQKDLNSLPYGDLteigergv 72
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELS------VAENIFLGNEITLPggrmAYNAMYLRAknllrelQLDADNVTRPVGDY-------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 nlSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKTV--VLVTHQLQFLES-CDEVILLEDGE 149
Cdd:TIGR02633 143 --GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
74-132 |
8.16e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 8.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ 132
Cdd:PRK13540 128 LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
613-666 |
8.66e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 8.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 613 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALF-----RLVepaSGTIIID--EVDICTVG 666
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDgkEVDVSTVS 332
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
74-179 |
1.07e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.04 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICE 152
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVL 225
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907189171 153 KGTHK------ELMEERG----RYAKLIHNL--RGLQFK 179
Cdd:PRK13649 226 SGKPKdifqdvDFLEEKQlgvpKITKFAQRLadRGISFS 264
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
614-811 |
1.13e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEvDICTVGleDLRT-----------KLTMIPQ 679
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVYPHgsyEGEILFDG-EVCRFK--DIRDsealgiviihqELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 680 DPV---LFVG--TVRY---NLDPLGSHTDEMLWHVlertfmrdtimKLPEKLQAEVTENGenfsVGERQLLCMARALLRN 751
Cdd:NF040905 93 LSIaenIFLGneRAKRgviDWNETNRRARELLAKV-----------GLDESPDTLVTDIG----VGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189171 752 SKIILLDEATASM-DSKTDTLVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 811
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLD-LLLE-LKAqgITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
73-149 |
1.37e-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: 42.23 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH----VGKHVFEecikktLKGkTVVLVTHQLQFLESCDEVIL-LED 147
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE------YPG-TVVAVTHDRYFLDNVAGWILeLDR 233
|
..
gi 1907189171 148 GE 149
Cdd:TIGR03719 234 GR 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
73-159 |
1.44e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 150
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
90
....*....|
gi 1907189171 151 CE-KGTHKEL 159
Cdd:PRK10522 528 SElTGEERDA 537
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
63-132 |
1.63e-03 |
|
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: 42.04 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 63 DLTEIGERGVN----------LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKktlKGKTVVLVTHQ 132
Cdd:TIGR00954 562 QLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE---FGITLFSVSHR 638
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
347-433 |
1.73e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 41.24 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 347 ASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlPFHAEnFLQQFFMVVFI-LVIMAAVFP------VVL 419
Cdd:cd18584 68 VKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALD---GYFAR-YLPQLVLAAIVpLLILVAVFPldwvsaLIL 143
|
90
....*....|....
gi 1907189171 420 VVLAGLAVIFLILL 433
Cdd:cd18584 144 LVTAPLIPLFMILI 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
63-133 |
1.79e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189171 63 DLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDahvgkhVFE-----ECIKKTLKGKTVVLVTHQL 133
Cdd:PRK13409 201 GLENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDL 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
64-149 |
1.88e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 64 LTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlKGKTVVLVTHQLQF 135
Cdd:PRK13409 443 LERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE------REATALVVDHDIYM 516
|
90
....*....|....
gi 1907189171 136 LESCDEVILLEDGE 149
Cdd:PRK13409 517 IDYISDRLMVFEGE 530
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
626-664 |
2.22e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.90 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1907189171 626 TVGIVGRTGSGKSSLGMALFRlvepaSGTIIIDEVDICT 664
Cdd:COG3596 41 VIALVGKTGAGKSSLINALFG-----AEVAEVGVGRPCT 74
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
75-159 |
2.30e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.86 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 75 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLE-SCDEVILLEDGEI 150
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKrefNTAIIMITHDLGVVAgICDKVLVMYAGRT 240
|
....*....
gi 1907189171 151 CEKGTHKEL 159
Cdd:PRK09473 241 MEYGNARDV 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
74-160 |
2.35e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.54 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEIC 151
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQGEVV 229
|
....*....
gi 1907189171 152 EKGTHKELM 160
Cdd:PRK15112 230 ERGSTADVL 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
614-790 |
2.40e-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: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 614 LDGLNLNIQSGQ-----TVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQ----DpvlF 684
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyispD---Y 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 685 VGTVRYNL-----DPLGSHtdeMLWH-VLERtfmrdtiMKLPEKLQAEVTEngenFSVGERQLLCMARALLRNSKIILLD 758
Cdd:COG1245 415 DGTVEEFLrsantDDFGSS---YYKTeIIKP-------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*
gi 1907189171 759 EATASMDSKTDTLVQSTIK---EAFKScTVLTIAH 790
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRrfaENRGK-TAMVVDH 514
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
74-154 |
2.51e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.45 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE--ECIKKTlKGKTVVLVTHQLQFLESC-DEVILLEDGEI 150
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLaDDVAVMSHGRI 219
|
....
gi 1907189171 151 CEKG 154
Cdd:PRK10418 220 VEQG 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
72-150 |
2.64e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 40.24 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 72 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKktlKGKTVVLVTHQLQFLESCD-EVILLED 147
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNR---VGVTVLMATHDIGLISRRSyRMLTLSD 212
|
...
gi 1907189171 148 GEI 150
Cdd:PRK10908 213 GHL 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
69-160 |
3.13e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 40.25 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 69 ERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLED 147
Cdd:PRK11614 133 QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLEN 212
|
90
....*....|...
gi 1907189171 148 GEICEKGTHKELM 160
Cdd:PRK11614 213 GHVVLEDTGDALL 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
69-164 |
3.24e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 69 ERGVN-LSGGQRQRISLA-------RAVYANRQLYLLDDPLSAVDahVGKHVFEECIKKTL--KGKTVVLVTHQL-QFLE 137
Cdd:PRK03695 121 GRSVNqLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD--VAQQAALDRLLSELcqQGIAVVMSSHDLnHTLR 198
|
90 100
....*....|....*....|....*..
gi 1907189171 138 SCDEVILLEDGEICEKGTHKELMEERG 164
Cdd:PRK03695 199 HADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
605-644 |
3.24e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 3.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMAL 644
Cdd:NF033858 10 RYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSL-LSL 46
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
329-442 |
3.37e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 40.51 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 329 VLMFGIIKGF-TFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTP--TGRLMNRFSKDMDEL----DVRLPFhae 395
Cdd:cd18578 58 FLVLAIVAGIaYFLQGYLFGIAGerltrrLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVrglvGDRLGL--- 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189171 396 nFLQQFFMVVFILVI-----------MAAVFPvvLVVLAGlaVIFLILLRIFHRGVQE 442
Cdd:cd18578 135 -ILQAIVTLVAGLIIafvygwklalvGLATVP--LLLLAG--YLRMRLLSGFEEKNKK 187
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
312-432 |
3.69e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 40.16 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 312 DTKHHMYQLVYIASM-VSVLMFGIIKGFTF---TNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELd 387
Cdd:cd18579 31 PDEPLSEGYLLALALfLVSLLQSLLLHQYFflsFRLGMRVRSALSSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRI- 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907189171 388 vrlpfhaENFLQQFFMVVFILVIMAAVFpVVLV------VLAGLAVIFLIL 432
Cdd:cd18579 110 -------EDFFLFLHYLWSAPLQIIVAL-YLLYrllgwaALAGLGVLLLLI 152
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
605-792 |
3.71e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 40.04 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 605 RYRDNTpLVLDGLNLnIQSGQTVGIVGRTGSGKSS--------LGMALFRLVEPASGTIIID-----EVDICTVGLEDLR 671
Cdd:cd03236 9 RYGPNS-FKLHRLPV-PREGQVLGLVGPNGIGKSTalkilagkLKPNLGKFDDPPDWDEILDefrgsELQNYFTKLLEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 672 TKLTMIPQD----PVLFVGTVRYNLDplgsHTDEmlwhvlerTFMRDTIMKLPEkLQAEVTENGENFSVGERQLLCMARA 747
Cdd:cd03236 87 VKVIVKPQYvdliPKAVKGKVGELLK----KKDE--------RGKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907189171 748 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRL 792
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDnYVLVVEHDL 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
74-163 |
3.77e-03 |
|
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: 40.58 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICE 152
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKG 483
|
90
....*....|.
gi 1907189171 153 KGTHKELMEER 163
Cdd:TIGR02633 484 DFVNHALTQEQ 494
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
597-790 |
5.20e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 597 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEvdicTVgledlrt 672
Cdd:PRK11819 325 IEAENLSKSFGDR--LLIDDLSFSLPPGGIVGIIGPNGAGKST----LFKMItgqeQPDSGTIKIGE----TV------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 673 KLTmipqdpvlFVGTVRYNLDPlgshtDEMLWHV----LErtfmrdtIMKLpeklqAEVTENGE------NF-------- 734
Cdd:PRK11819 388 KLA--------YVDQSRDALDP-----NKTVWEEisggLD-------IIKV-----GNREIPSRayvgrfNFkggdqqkk 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189171 735 ----SVGERQLLCMARALLRNSKIILLDEATASMDskTDTLvqSTIKEA---FKSCTVLtIAH 790
Cdd:PRK11819 443 vgvlSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD--VETL--RALEEAlleFPGCAVV-ISH 500
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
73-149 |
5.28e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.40 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 73 NLSGGQRQRISLARAVYANRQLYLLDDPlSAV--DAHVgKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLED 147
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEP-TAVltPQEA-DELFE--ILRRLAaeGKSIIFITHKLReVMAIADRVTVLRR 216
|
..
gi 1907189171 148 GE 149
Cdd:COG3845 217 GK 218
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
350-517 |
7.04e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 39.39 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 350 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIF 429
Cdd:cd18550 73 DLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 430 LILLRIFHRGVQEL--KQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRWFALRMD 507
Cdd:cd18550 153 VLPTRRVGRRRRKLtrEQQEKLAELNSIMQETLSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALG 232
|
170
....*....|
gi 1907189171 508 ILMNIVTFVV 517
Cdd:cd18550 233 LFTAIGPALV 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
74-162 |
7.13e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICE 152
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
90
....*....|
gi 1907189171 153 KGTHKELMEE 162
Cdd:PRK09700 490 ILTNRDDMSE 499
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
74-170 |
8.05e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 74 LSGGQRQRISLA-----RAvyANRQLYLLDDPLsavdahVGKHvFEEcIKKTL--------KGKTVVLVTHQLQFLESCD 140
Cdd:PRK00349 831 LSGGEAQRVKLAkelskRS--TGKTLYILDEPT------TGLH-FED-IRKLLevlhrlvdKGNTVVVIEHNLDVIKTAD 900
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907189171 141 EVILL------EDGEICEKGTHKELMEER----GRYAKLI 170
Cdd:PRK00349 901 WIIDLgpeggdGGGEIVATGTPEEVAKVEasytGRYLKPV 940
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
51-148 |
9.55e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.38 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189171 51 GLQKDLNslpygdlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFeeCIKKTLK--GKTVVL 128
Cdd:PRK09700 134 GLKVDLD-----------EKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLF--LIMNQLRkeGTAIVY 200
|
90 100
....*....|....*....|.
gi 1907189171 129 VTHQL-QFLESCDEVILLEDG 148
Cdd:PRK09700 201 ISHKLaEIRRICDRYTVMKDG 221
|
|
| |
