|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-493 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 835.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 2 NAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 82 ISMIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNAD 161
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 162 IVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVGRE 241
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 242 LTQLFPKFNNTIGEEVLTVRNLSRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDS 321
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 322 PSVAIEKGMALLTEDRKKSGLFLVLSVMENMSIVNMPEYiGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGN 401
Cdd:COG1129 321 PRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRL-SRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 402 QQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKD 481
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDRE 479
|
490
....*....|..
gi 490997255 482 EADQETILSLAS 493
Cdd:COG1129 480 EATEEAIMAAAT 491
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-492 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 638.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFaLEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRA 80
Cdd:PRK11288 1 SSPY-LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGS-RQTGEFTRQSLITQMVG 239
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQAMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 240 RELTQLFPKFNNTIGEEVLTVRNLSRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVII 319
Cdd:PRK11288 240 REIGDIYGYRPRPLGEVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 320 DSPSVAIEKGMALLTEDRKKSGLFLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSG 399
Cdd:PRK11288 320 RSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 400 GNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILD 479
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
490
....*....|...
gi 490997255 480 KDEADQETILSLA 492
Cdd:PRK11288 480 REQATERQALSLA 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-492 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 623.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYrPD---KGAIRVKGEPVQFQDTMDA 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 78 LRAGISMIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 158 WNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQM 237
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 238 VGRELTQLFPKFNNTIGEEVLTVRNLS-------RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGM--ERFdSG 308
Cdd:PRK13549 240 VGRELTALYPREPHTIGEVILEVRNLTawdpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAypGRW-EG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 309 EVLIDGQPVIIDSPSVAIEKGMALLTEDRKKSGLFLVLSVMENMSIVNMPEYiGKSGFVKHMKMAQDCMEQIRRLNIKTP 388
Cdd:PRK13549 319 EIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRF-TGGSRIDDAAELKTILESIQRLKVKTA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 389 TMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMV 468
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLV 477
|
490 500
....*....|....*....|....
gi 490997255 469 MHEGRITGILDKDEADQETILSLA 492
Cdd:PRK13549 478 MHEGKLKGDLINHNLTQEQVMEAA 501
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-492 |
0e+00 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 620.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPM-KYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVGRELTQ 244
Cdd:PRK10762 165 MDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKLED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 245 LFPKFNNTIGEEVLTVRNLSRKGyFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSV 324
Cdd:PRK10762 245 QYPRLDKAPGEVRLKVDNLSGPG-VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 325 AIEKGMALLTEDRKKSGLFLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQK 404
Cdd:PRK10762 324 GLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 405 VLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDEAD 484
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQAT 483
|
....*...
gi 490997255 485 QETILSLA 492
Cdd:PRK10762 484 QEKLMAAA 491
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-493 |
0e+00 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 580.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 9 EGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMIHQE 88
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 89 LNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEP 168
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 169 TSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVGRELTQLFPK 248
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 249 FNNTIGEEVLTVRNLS--RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAI 326
Cdd:PRK10982 242 KENKPGEVILEVRNLTslRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 327 EKGMALLTEDRKKSGLFLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVL 406
Cdd:PRK10982 322 NHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 407 IARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDEADQE 486
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQN 481
|
....*..
gi 490997255 487 TILSLAS 493
Cdd:PRK10982 482 EILRLAS 488
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-488 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 579.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRA 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVGR 240
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 241 ELTQLFPKFNNTIGEEVLTVRNLSRKGYF-----EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQ 315
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVRDDRgvpalKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 316 PVIIDSPSVAIEKGMALLTEDRKKSGLFLVLSVMENMSI--VNMPEYiGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQI 393
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILgrYRRPPF-SRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 394 INNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490
....*....|....*
gi 490997255 474 ITGILDKDEADQETI 488
Cdd:COG3845 480 IVGEVPAAEATREEI 494
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-491 |
0e+00 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 562.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYrPD---KGAIRVKGEPVQFQDTMDALRAGI 82
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADI 162
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 163 VIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGS--RQTGEFTRQSLITQMVGR 240
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETldCRADEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 241 ELTQLFPKFNNTIGEEVLTVRNLS--------RKgYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGME--RFDSGEV 310
Cdd:NF040905 241 DLEDRYPERTPKIGEVVFEVKNWTvyhplhpeRK-VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 311 LIDGQPVIIDSPSVAIEKGMALLTEDRKKSGLFLVLSVMENMSIVNMPEyIGKSGFV---KHMKMAQDCMeqiRRLNIKT 387
Cdd:NF040905 320 FKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGK-VSRRGVIdenEEIKVAEEYR---KKMNIKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 388 PTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVM 467
Cdd:NF040905 396 PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIY 475
|
490 500
....*....|....*....|....
gi 490997255 468 VMHEGRITGILDKDEADQETILSL 491
Cdd:NF040905 476 VMNEGRITGELPREEASQERIMRL 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-492 |
4.04e-174 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 499.70 E-value: 4.04e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKYGF----VDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNAD 161
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 162 IVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVGRE 241
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 242 LTQLFPKFN----NTIGEEVLTVRNLSRK--GYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQ 315
Cdd:PRK09700 246 LQNRFNAMKenvsNLAHETVFEVRNVTSRdrKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 316 PVIIDSPSVAIEKGMALLTEDRKKSGLFLVLSVMENMSIVN---MPEYIGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQ 392
Cdd:PRK09700 326 DISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRslkDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 393 IINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
490 500
....*....|....*....|.
gi 490997255 473 RITGILD-KDEADQETILSLA 492
Cdd:PRK09700 486 RLTQILTnRDDMSEEEIMAWA 506
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-492 |
2.20e-166 |
|
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: 479.32 E-value: 2.20e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYrPD---KGAIRVKGEPVQFQDTMDALRAGI 82
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVPHMTVAENIWLGRE-PMKYGFVDHRQLARQTQTLLNKLNIRLSAD-RLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVGR 240
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 241 ELTQLFPKFNNTIGEEVLTVRNLS-------RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGM-ERFDSGEVLI 312
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTcwdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 313 DGQPVIIDSPSVAIEKGMALLTEDRKKSGLFLVLSVMENMSIVNMPEYIGKsGFVKHMKMAQDCMEQIRRLNIKTPTMDQ 392
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFK-MRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 393 IINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
490 500
....*....|....*....|
gi 490997255 473 RITGILDKDEADQETILSLA 492
Cdd:TIGR02633 480 KLKGDFVNHALTQEQVLAAA 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-492 |
2.44e-143 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 421.00 E-value: 2.44e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWlgrepmkYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PRK15439 92 PQEPLLFPNLSVKENIL-------FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMV------- 238
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITpaareks 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 239 ---GRELTQLFPKFNNT--IGEEVLTVRNLSRKGyFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLID 313
Cdd:PRK15439 245 lsaSQKLWLELPGNRRQqaAGAPVLTVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 314 GQPVIIDSPSVAIEKGMALLTEDRKKSGLFLVLSVMENMSIVNMpeyiGKSGFVKHMKMAQDCMEQIRR-LNIKTPTMDQ 392
Cdd:PRK15439 324 GKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALTH----NRRGFWIKPARENAVLERYRRaLNIKFNHAEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 393 IINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:PRK15439 400 AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
490 500
....*....|....*....|
gi 490997255 473 RITGILDKDEADQETILSLA 492
Cdd:PRK15439 480 EISGALTGAAINVDTIMRLA 499
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
254-474 |
2.15e-95 |
|
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: 286.25 E-value: 2.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNLSRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALL 333
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDRKKSGLFLVLSVMENMSIVNMpeyigksgfvkhmkmaqdcmeqirrlniktptmdqiinnLSGGNQQKVLIARWLLA 413
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-222 |
1.32e-84 |
|
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: 257.74 E-value: 1.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQelnlvphmtvaeniwlgrepmkygfvdhrqlarqtqtllnklnirlsadrlvgeLSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGS 222
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-474 |
1.78e-71 |
|
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: 235.57 E-value: 1.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPD---KGAIRVKGEPVqFQDTMDALR 79
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 AGISMIHQE--LNLVPhMTVAENIwlgREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:COG1123 83 RRIGMVFQDpmTQLNP-VTVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 158 WNADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGE-FTRQSLIT 235
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEiLAAPQALA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 236 QMVGRELTQLFPKFNNTIGEEVLTVRNLS------RKGYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFD 306
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvrGKGGVravDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 307 SGEVLIDGQPVIIDSPsvaiekgmALLTEDRKK---------SGLFLVLSVMEnmsIVNMPeyIGKSGFVKHMKMAQDCM 377
Cdd:COG1123 319 SGSILFDGKDLTKLSR--------RSLRELRRRvqmvfqdpySSLNPRMTVGD---IIAEP--LRLHGLLSRAERRERVA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 378 EQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSEL 456
Cdd:COG1123 386 ELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDL 465
|
490
....*....|....*...
gi 490997255 457 PEILGMSDRVMVMHEGRI 474
Cdd:COG1123 466 AVVRYIADRVAVMYDGRI 483
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-213 |
6.69e-54 |
|
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: 181.78 E-value: 6.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISM 84
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGRE-PMKYGFV-----------DHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEI 152
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHaRLGRGLLaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 153 AKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLR-EQGKAIIYISHKMDEIFAITDEISV 213
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-214 |
1.80e-53 |
|
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: 179.94 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREP-MKYGFVDHR------QLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSW 158
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQArTGSGLLLARarreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 159 NADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVF 214
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-217 |
1.37e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.86 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmDALRAGISMI 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP--AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENI-WLGRepmKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFAR---LYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-218 |
3.37e-48 |
|
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: 166.19 E-value: 3.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmDALRAGISMI 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP--REARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 166 DEPTSALtesEVAH---LFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:COG4555 157 DEPTNGL---DVMArrlLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-217 |
9.92e-45 |
|
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: 156.14 E-value: 9.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDALRAGISMI 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03259 78 FQDYALFPHLTVAENIAFG---LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 166 DEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-217 |
2.66e-44 |
|
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: 153.71 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfQDTMDALRAGISMI 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIwlgrepmkygfvdhrqlarqtqtllnklnirlsadrlvgELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03230 79 PEEPSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-217 |
3.19e-44 |
|
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: 154.96 E-value: 3.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPV-QFQDT-MDALR 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsKLSEKeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 A-GISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSW 158
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVEL---PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 159 NADIVIMDEPTSAL---TESEVahlFTIIRDL-REQGKAIIYISHKMdEIFAITDEISVFRDG 217
Cdd:cd03255 158 DPKIILADEPTGNLdseTGKEV---MELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
9.04e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 148.65 E-value: 9.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAfALEAEGISKFFP----GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQF--QDT 74
Cdd:COG1136 1 MSP-LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlsERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 75 MDALRAG-ISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIA 153
Cdd:COG1136 80 LARLRRRhIGFVFQFFNLLPELTALENVAL---PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 154 KAVSWNADIVIMDEPTSAL---TESEVAHLFtiiRDL-REQGKAIIYISHKMdEIFAITDEISVFRDG 217
Cdd:COG1136 157 RALVNRPKLILADEPTGNLdskTGEEVLELL---RELnRELGTTIVMVTHDP-ELAARADRVIRLRDG 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-241 |
1.84e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.79 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISkffpGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISM 84
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 I---HQELNLVPHMTVAENIWLGREPM--KYGFVDHRQLARQTQTLLNKLNIRL-SADRLVGELSIAAQQMVEIAKAVSW 158
Cdd:COG1129 332 VpedRKGEGLVLDLSIRENITLASLDRlsRGGLLDRRRERALAEEYIKRLRIKTpSPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 159 NADIVIMDEPT-----SALTEsevahLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSL 233
Cdd:COG1129 412 DPKVLILDEPTrgidvGAKAE-----IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAI 486
|
....*...
gi 490997255 234 ITQMVGRE 241
Cdd:COG1129 487 MAAATGGA 494
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-170 |
2.04e-41 |
|
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: 145.10 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtMDALRAGISMIHQELNLVPHMTVAEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE-RKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 101 IWLGREPMkygFVDHRQLARQTQTLLNKLNIRLSADRLVG----ELSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:pfam00005 80 LRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-217 |
3.45e-40 |
|
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: 143.96 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmdalRAGISMI 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAEN-IWLGRepmKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:cd03269 76 PEERGLYPKMKVIDQlVYLAQ---LKG-LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-218 |
4.55e-40 |
|
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: 144.01 E-value: 4.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGIS-KFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISM 84
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-KKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQ--ELNLVpHMTVAENIWLGrePMKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADI 162
Cdd:COG1122 80 VFQnpDDQLF-APTVEEDVAFG--PENLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 163 VIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
258-474 |
4.66e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.44 E-value: 4.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRK-GYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPsvAIEKGMALL 333
Cdd:COG1131 1 IEVRGLTKRyGDKtalDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDrkkSGLFLVLSVMENMsivnmpEYIGKSGFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLA 413
Cdd:COG1131 79 PQE---PALYPDLTVRENL------RFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-218 |
3.61e-39 |
|
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: 141.07 E-value: 3.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISM 84
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-KLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQ--ELNLVpHMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADI 162
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVAFGLENLG---LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 163 VIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-218 |
2.46e-38 |
|
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: 137.70 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMD-ALRAGISM 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGrepmkygfvdhrqlarqtqtllnklnirlsadrlvgeLSIAAQQMVEIAKAVSWNADIVI 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-217 |
5.22e-38 |
|
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: 138.79 E-value: 5.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPV-QFQDTMDALRA 80
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 G-ISMIHQE----LNlvPHMTVAENIwlgREPMKYGFVDHRQLARQTQTLLNKLNIRLS---ADRLVGELSIAAQQMVEI 152
Cdd:cd03257 82 KeIQMVFQDpmssLN--PRMTIGEQI---AEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 153 AKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-217 |
9.46e-38 |
|
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: 137.57 E-value: 9.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKYGFVDhRQLARQTQtLLNKLNIRLsaDRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRK-ARLERVYE-LFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-217 |
2.86e-37 |
|
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: 136.93 E-value: 2.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMD--ALRAGI 82
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVPHMTVAENIWLGREPMK------YGFVD--HRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAK 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslFGLFPkeEKQRALA---ALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 155 AVSWNADIVIMDEPTSAL---TESEVAHLFTIIRdlREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03256 158 ALMQQPKLILADEPVASLdpaSSRQVMDLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-474 |
1.14e-36 |
|
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: 142.13 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKS----TLMKCLIGIYRPDKGAIRVKGEPVQFQD--TM 75
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSerEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 76 DALRAG-ISMIHQE----LNlvPHMTVAENIwlgREPMKYgfvdHRQL----ARQ-TQTLLNKLNIRLSADRLVG---EL 142
Cdd:COG4172 87 RRIRGNrIAMIFQEpmtsLN--PLHTIGKQI---AEVLRL----HRGLsgaaARArALELLERVGIPDPERRLDAyphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 143 SIAAQQMVEIAKAVSWNADIVIMDEPTSAL---TESEVAHLftiIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQILDL---LKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 219 WVGSRQTGEF--------TRQSLITQMVGRELTQlfpkfnNTIGEEVLTVRNLS-----RKGYF----------EEVNFS 275
Cdd:COG4172 235 IVEQGPTAELfaapqhpyTRKLLAAEPRGDPRPV------PPDAPPLLEARDLKvwfpiKRGLFrrtvghvkavDGVSLT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 276 VRRGEILGVAGLVGAGRSEVMESLFGMERFdSGEVLIDGQPV----------------II--D-----SP--SVA--IEK 328
Cdd:COG4172 309 LRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLdglsrralrplrrrmqVVfqDpfgslSPrmTVGqiIAE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 329 GMALL-----TEDRKKsglfLVLSVMENmsiVNMPEyigksgfvkhmkmaqdcmeqirrlniktPTMDQIINNLSGGNQQ 403
Cdd:COG4172 388 GLRVHgpglsAAERRA----RVAEALEE---VGLDP----------------------------AARHRYPHEFSGGQRQ 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 404 KVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-217 |
1.37e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 138.31 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqdtmDALRA 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV------TGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 ---GISMIHQELNLVPHMTVAENIwlgREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:COG3842 75 ekrNVGMVFQDYALFPHLTVAENV---AFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 158 WNADIVIMDEPTSAL-------TESEVAHLftiirdLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG3842 152 PEPRVLLLDEPLSALdaklreeMREELRRL------QRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-217 |
4.85e-36 |
|
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: 132.65 E-value: 4.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDT-MDALRAGISM 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKnINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEIsVFRDG 217
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRV-IFMDD 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
257-487 |
9.52e-36 |
|
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: 133.06 E-value: 9.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSRKgY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVaiEKGMA 331
Cdd:COG4555 1 MIEVENLSKK-YgkvpaLKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA--RRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEDRkksGLFLVLSVMENMsivnmpEYIGKSGFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWL 411
Cdd:COG4555 78 VLPDER---GLYDRLTVRENI------RYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDEADQET 487
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-217 |
1.40e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.08 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmdalRAGISM 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-----RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENI-WLGRepMKyGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIV 163
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvYLAR--LK-G-LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 164 IMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-217 |
2.06e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.04 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDT-MDALRAGISM 84
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLA--PIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 165 MDEPTSAL---TESEVahLfTIIRDLREQGKAIIYISHKMDeiFA--ITDEIsVFRDG 217
Cdd:COG1126 160 FDEPTSALdpeLVGEV--L-DVMRDLAKEGMTMVVVTHEMG--FAreVADRV-VFMDG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-222 |
2.29e-35 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 130.80 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpvQFQDTMDALRAGISMI 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 hQELNLVPHMTvaeniwlGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03268 79 -EAPGFYPNLT-------ARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGS 222
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-217 |
2.70e-35 |
|
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: 132.09 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAgISM 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGREPMKYGF----VDHRQLARQTqtlLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLGLFgrpsAEDREAVEEA---LERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 161 DIVIMDEPTSALtesEVAH---LFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG1120 157 PLLLLDEPTSHL---DLAHqleVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-217 |
3.03e-35 |
|
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: 131.16 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQD--TMDALR 79
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 AGISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVAL---PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 160 ADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-217 |
4.95e-35 |
|
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: 130.18 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFF----PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDAlRAG 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEA-RRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 82 ISMIHQELNLVPHMTVAENI-WLGRepmKYGFVDHRQLARqTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLeYFAG---LYGLKGDELTAR-LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
258-474 |
6.09e-35 |
|
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: 128.67 E-value: 6.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPviIDSPSVAIEKGMAL 332
Cdd:cd03230 1 IEVRNLS-KRYgkktaLDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--IKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEDrkkSGLFLVLSVMENMsivnmpeyigksgfvkhmkmaqdcmeqirrlniktptmdqiinNLSGGNQQKVLIARWLL 412
Cdd:cd03230 78 LPEE---PSLYENLTVRENL-------------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 413 AQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-218 |
7.78e-35 |
|
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: 127.75 E-value: 7.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIH 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QelnlvphmtvaeniwlgrepmkygfvdhrqlarqtqtllnklnirLSAdrlvGElsiaaQQMVEIAKAVSWNADIVIMD 166
Cdd:cd00267 80 Q---------------------------------------------LSG----GQ-----RQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 167 EPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-199 |
9.78e-35 |
|
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: 129.14 E-value: 9.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmDALRAGISMI 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR--EDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENI--WLGRepmkYGFVDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIV 163
Cdd:COG4133 81 GHADGLKPELTVRENLrfWAAL----YGLRADREAIDE---ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 490997255 164 IMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISH 199
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-220 |
3.85e-34 |
|
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: 128.57 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGV-KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMdALRAGISM 84
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTQTLLNkLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVG-LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 165 MDEPTSAL---TESEVAHLFTIIRdlREQGKAIIYISHKMDEIFAITDEISVFRDGTWV 220
Cdd:cd03295 159 MDEPFGALdpiTRDQLQEEFKRLQ--QELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-214 |
8.90e-34 |
|
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: 126.82 E-value: 8.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdtmdALRAG 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 82 ISMIHQELNLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNAD 161
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALG---LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 162 IVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVF 214
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-217 |
9.91e-34 |
|
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: 125.62 E-value: 9.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISkffpGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISM 84
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 I----HQELnLVPHMTVAENIWLGREpmkygfvdhrqlarqtqtllnklnirlsadrlvgeLSIAAQQMVEIAKAVSWNA 160
Cdd:cd03215 80 VpedrKREG-LVLDLSVAENIALSSL-----------------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
1.12e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQdtmdalRA 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLVPH--MTVAENIWLGREPMKyGFV-----DHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIA 153
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDVVLMGRYGRR-GLFrrpsrADREAVDE---ALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 154 KAVSWNADIVIMDEPTSAL-TESEvAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEI 211
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVdAATE-EALYELLRELRREGKTILVVTHDLGAVREYFDRV 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-209 |
2.00e-33 |
|
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: 126.25 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTqTLLNKLNIRLsaDRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVY-ELFPRLKERR--RQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITD 209
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIAD 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
255-474 |
2.00e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLSRkGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVA---- 325
Cdd:COG1121 4 MPAIELENLTV-SYggrpvLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGyvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 326 ---IEKGMALLTED------RKKSGLFLVLS------VMENMSIVNMPEYIGKSgfvkhmkmaqdcmeqirrlniktptm 390
Cdd:COG1121 83 raeVDWDFPITVRDvvlmgrYGRRGLFRRPSradreaVDEALERVGLEDLADRP-------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 391 dqiINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMH 470
Cdd:COG1121 137 ---IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN 213
|
....
gi 490997255 471 EGRI 474
Cdd:COG1121 214 RGLV 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-218 |
2.15e-33 |
|
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: 125.70 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQdtMDALRAGIS 83
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD--RKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVPHMTVAENIWL-----GREpmkygfvdHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSW 158
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyarlkGLP--------KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 159 NADIVIMDEPTSALteSEVA--HLFTIIRDLReQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd03263 151 GPSVLLLDEPTSGL--DPASrrAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-217 |
3.12e-33 |
|
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: 126.08 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQ--FQDTMDALRAGIS 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVPHMTVAENI--WLgREpmkYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNAD 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVafPL-RE---HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 162 IVIMDEPTSAL---TESEVAHLftiIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03261 157 LLLYDEPTAGLdpiASGVIDDL---IRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
258-474 |
7.89e-33 |
|
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: 124.47 E-value: 7.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMAL 332
Cdd:cd03224 1 LEVENLN-AGYgksqiLFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEDRkksGLFLVLSVMENMSivnMPEYIGKSGFVKHMkmaqdcMEQI---------RRlniktptmDQIINNLSGGNQQ 403
Cdd:cd03224 80 VPEGR---RIFPELTVEENLL---LGAYARRRAKRKAR------LERVyelfprlkeRR--------KQLAGTLSGGEQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 404 KVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
7.99e-33 |
|
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: 125.09 E-value: 7.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQF--QDTMDAL 78
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 79 RAGISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQT-QTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAF---PLREHTDLSEAEIRELvLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 158 WNADIVIMDEPTSAL---TESEVAHLftiIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDGT--WVGSRQ 224
Cdd:COG1127 158 LDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKiiAEGTPE 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-211 |
1.05e-32 |
|
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: 123.80 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQdtmdalRAGISMIH 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QELNL---VPhMTVAENIWLGREPMKYGF----VDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLYGHKGLFrrlsKADKAKVDE---ALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 160 ADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEI 211
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
272-491 |
1.06e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.15 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKG--------MalltedrkksgLF 343
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGigmvhqhfM-----------LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 LVLSVMENMsIVNMPEyiGKSGFVKHMKMAQDCMEQIRRLNIKTPtMDQIINNLSGGNQQKVLIARWLLAQPKILILDEP 423
Cdd:COG3845 93 PNLTVAENI-VLGLEP--TKGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 424 TRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDEADQETILSL 491
Cdd:COG3845 169 TAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAEL 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-217 |
2.19e-32 |
|
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: 122.69 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGtVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQdtMDALRAGISMI 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENI----WLGRepmkygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNAD 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiaWLKG-------IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 162 IVIMDEPTSALTESEVAHLFTIIRDLREqGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-199 |
2.74e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 122.85 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDA-----LR 79
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS---RLKRreipyLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 AGISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVAL---PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490997255 160 ADIVIMDEPTSAL---TESEVAHLFtiiRDLREQGKAIIYISH 199
Cdd:COG2884 156 PELLLADEPTGNLdpeTSWEIMELL---EEINRRGTTVLIATH 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-217 |
4.96e-32 |
|
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: 123.52 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 3 AFALEAEG-----ISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMD- 76
Cdd:cd03294 17 AFKLLAKGkskeeILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA---AMSr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 -ALRA----GISMIHQELNLVPHMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVE 151
Cdd:cd03294 94 kELRElrrkKISMVFQSFALLPHRTVLENVAFGLEVQG---VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVG 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 152 IAKAVSWNADIVIMDEPTSALTEsevahlfTIIRDL--------REQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03294 171 LARALAVDPDILLMDEAFSALDP-------LIRREMqdellrlqAELQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
258-474 |
8.71e-32 |
|
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: 121.78 E-value: 8.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRKgyF------EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMA 331
Cdd:cd03219 1 LEVRGLTKR--FgglvalDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 lltedRK--KSGLFLVLSVMENMSI---VNMPEYIGKSGFVKHMKMAQD-CMEQIRRLNIkTPTMDQIINNLSGGNQQKV 405
Cdd:cd03219 79 -----RTfqIPRLFPELTVLENVMVaaqARTGSGLLLARARREEREARErAEELLERVGL-ADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 406 LIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-217 |
2.61e-31 |
|
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: 120.05 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqDTMDALRAGISMI 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIwlgREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03301 78 FQNYALYPHMTVYDNI---AFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 166 DEPTSAL-TESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03301 155 DEPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-494 |
6.51e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 125.59 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 22 DNVSLRVRPGTVHALMGENGAGKS-TLMKCLIGIYRPD----KGAIRVKGEPVQFQD--TMDALRAG-ISMIHQE--LNL 91
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASeqTLRGVRGNkIAMIFQEpmVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 92 VPHMTV----AENIWLGREpMKygfvdhRQLAR-QTQTLLNKLNIRLSADRLVG---ELSIAAQQMVEIAKAVSWNADIV 163
Cdd:PRK15134 106 NPLHTLekqlYEVLSLHRG-MR------REAARgEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 164 IMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGE--------FTRQSLI 234
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATlfsapthpYTQKLLN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 235 TQMVGRELtqlfPKFNNTigEEVLTVRNLS-----RKGYF----------EEVNFSVRRGEILGVAGLVGAGRSEVMESL 299
Cdd:PRK15134 259 SEPSGDPV----PLPEPA--SPLLDVEQLQvafpiRKGILkrtvdhnvvvKNISFTLRPGETLGLVGESGSGKSTTGLAL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 300 FGMERfDSGEVLIDGQPviidspsvaiekgmaLLTEDRKKsglflVLSVMENMSIV------------NMPEYIGKSGFV 367
Cdd:PRK15134 333 LRLIN-SQGEIWFDGQP---------------LHNLNRRQ-----LLPVRHRIQVVfqdpnsslnprlNVLQIIEEGLRV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 368 KHMKMA-----QDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL 442
Cdd:PRK15134 392 HQPTLSaaqreQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 443 ANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITgildkDEADQETILSLASH 494
Cdd:PRK15134 472 QQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVV-----EQGDCERVFAAPQQ 519
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-217 |
1.01e-30 |
|
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: 117.10 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGIS 83
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVpHMTVAENIwlgrepmkygfvdhrqlarqtqtllnklnirLSAdrlvGElsiaaQQMVEIAKAVSWNADIV 163
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI-------------------------------LSG----GQ-----RQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 164 IMDEPTSAL-TESEvAHLFTIIRDLReQGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:cd03228 119 ILDEATSALdPETE-ALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-217 |
1.03e-30 |
|
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: 118.98 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKaLDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDALRAGISMI 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT---NLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG---LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 166 DEPTSAL---TESEVAHLFTIIRdlREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03299 154 DEPFSALdvrTKEKLREELKKIR--KEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-217 |
1.41e-30 |
|
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: 118.17 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVR---PGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPvqFQDTMDAL-----RAGISMIHQELN 90
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV--LFDSRKKInlppqQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 91 LVPHMTVAENIWLGrepmkYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:cd03297 86 LFPHLNVRENLAFG-----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 171 ALTEsevaHLFTIIRDLREQGKAI-----IYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03297 161 ALDR----ALRLQLLPELKQIKKNlnipvIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-218 |
1.71e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.94 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRA 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLVPHMTVAENIWLGR-EPMKYGFV-------DHRQLARQTQ----TLLNKLNIRLSADRLVGELSIAAQQ 148
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQhQQLKTGLFsgllktpAFRRAESEALdraaTWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 149 MVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-213 |
1.85e-30 |
|
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: 120.54 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRP---DKGAIRVKGEPVQF--QDTMD 76
Cdd:COG0444 2 LEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 ALRAG-ISMIHQE----LNlvPHMTVAENIwlgREPMKY-GFVDHRQLARQTQTLLNKLNIRLSADRLV---GELSIAAQ 147
Cdd:COG0444 82 KIRGReIQMIFQDpmtsLN--PVMTVGDQI---AEPLRIhGGLSKAEARERAIELLERVGLPDPERRLDrypHELSGGMR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 148 QMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISV 213
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
257-474 |
2.07e-30 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 117.99 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLS-----RKGYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiek 328
Cdd:cd03257 1 LLEVKNLSvsfptGGGSVkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 329 gmaLLTEDRKKSGLflvlsVMEN-MSIVN--MPeyIGKS---GFVKHMKMAQDCMEQIRRLNIKT--PTMDQIINN---- 396
Cdd:cd03257 76 ---LRKIRRKEIQM-----VFQDpMSSLNprMT--IGEQiaePLRIHGKLSKKEARKEAVLLLLVgvGLPEEVLNRyphe 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAN-RGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
258-474 |
5.18e-30 |
|
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: 116.46 E-value: 5.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIidspSVAIEK-GMA 331
Cdd:cd03259 1 LELKGLS-KTYgsvraLDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT----GVPPERrNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEDRkksGLFLVLSVMENMSivnmpeYIGKSGFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWL 411
Cdd:cd03259 76 MVFQDY---ALFPHLTVAENIA------FGLKLRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
255-475 |
7.93e-30 |
|
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: 116.62 E-value: 7.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKG 329
Cdd:COG0410 1 MPMLEVENLH-AGYggihvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 330 MALLTEDRkksGLFLVLSVMENMSivnMPEYIGKSGfvkhmKMAQDCMEQI---------RRlniktptmDQIINNLSGG 400
Cdd:COG0410 80 IGYVPEGR---RIFPSLTVEENLL---LGAYARRDR-----AEVRADLERVyelfprlkeRR--------RQRAGTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 401 NQQKVLIARWLLAQPKILILDEPTRGIdvgakA-----EIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-218 |
8.23e-30 |
|
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: 114.84 E-value: 8.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdtmdalragiSMIH 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA------------SLSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QELnlvphmtvAENIwlgrepmkyGFVdhrqlarqtQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMD 166
Cdd:cd03214 69 KEL--------ARKI---------AYV---------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 167 EPTSALtesEVAH---LFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd03214 123 EPTSHL---DIAHqieLLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-217 |
1.13e-29 |
|
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: 116.10 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDA-LRAGISM 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKrARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
260-487 |
1.14e-29 |
|
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: 116.06 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 260 VRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPS--VAIEKGMAL 332
Cdd:cd03261 3 LRGLT-KSFggrtvLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEDrkkSGLFLVLSVMENMSiVNMPEYigkSGFVKHMkMAQDCMEQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLL 412
Cdd:cd03261 82 LFQS---GALFDSLTVFENVA-FPLREH---TRLSEEE-IREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 413 AQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDEADQET 487
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
258-494 |
1.14e-29 |
|
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: 116.44 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY---------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIiDSPSVAIEK 328
Cdd:COG1124 2 LEVRNLS-VSYgqggrrvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT-RRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 329 GMALLTED-------RKKsglfLVLSVMENMSIVNMPEyigksgfvkhmkMAQDCMEQIRRLNIKTPTMDQIINNLSGGN 401
Cdd:COG1124 80 RVQMVFQDpyaslhpRHT----VDRILAEPLRIHGLPD------------REERIAELLEQVGLPPSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 402 QQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDK 480
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
250
....*....|....
gi 490997255 481 DEadqetILSLASH 494
Cdd:COG1124 224 AD-----LLAGPKH 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-217 |
2.42e-29 |
|
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: 115.03 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDALRAGISMI 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03300 78 FQNYALFPHLTVFENIAFG---LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 166 DEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-227 |
3.73e-29 |
|
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: 114.39 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqFQDTMDaLRAGISMI 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPRE-VRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENI-WLGRepmKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:cd03265 79 FQDLSVDDELTGWENLyIHAR---LYG-VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGE 227
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-217 |
6.44e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.78 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGE------PVQ-------FQ 72
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlPPRerrvgfvFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 73 DTMdalragismihqelnLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKlnIRLS--ADRLVGELSIAAQQMV 150
Cdd:COG1118 83 HYA---------------LFPHMTVAENIAFG---LRVRPPSKAEIRARVEELLEL--VQLEglADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 151 EIAKAVSWNADIVIMDEPTSALTesevAHLFTIIRD-----LREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALD----AKVRKELRRwlrrlHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
258-473 |
7.26e-29 |
|
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: 112.28 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGYFE-----EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEK---G 329
Cdd:cd03229 1 LELKNVS-KRYGQktvlnDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrriG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 330 MALltedrKKSGLFLVLSVMENMSIVnmpeyigksgfvkhmkmaqdcmeqirrlniktptmdqiinnLSGGNQQKVLIAR 409
Cdd:cd03229 80 MVF-----QDFALFPHLTVLENIALG-----------------------------------------LSGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 410 WLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
258-469 |
8.80e-29 |
|
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: 113.01 E-value: 8.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRnLSRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVA-------IEKGM 330
Cdd:cd03235 5 LTVS-YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGyvpqrrsIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 ALLTEDrkksglfLVLsvMENMSIVNMPEYIGKsgfvKHMKMAQDCMEQIRRLNIKtptmDQIINNLSGGNQQKVLIARW 410
Cdd:cd03235 84 PISVRD-------VVL--MGLYGHKGLFRRLSK----ADKAKVDEALERVGLSELA----DRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 411 LLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVM 469
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
259-475 |
9.50e-29 |
|
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: 111.76 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 259 TVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALl 333
Cdd:cd03214 1 EVENLS-VGYggrtvLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD-LASLSPKELARKIAY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 tedrkksglflVLSVMENMSIvnmpeyigksgfvKHMKmaqdcmeqirrlniktptmDQIINNLSGGNQQKVLIARWLLA 413
Cdd:cd03214 78 -----------VPQALELLGL-------------AHLA-------------------DRPFNELSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELAN-RGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-246 |
9.88e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.29 E-value: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRA 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GIsmIHQELNLVPHMTVAENIWL-GRepmkYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:PRK13537 83 GV--VPQFDNLDPDFTVRENLLVfGR----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 160 ADIVIMDEPTSALtESEVAHL-FTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGtwvgsRQTGEFTRQSLITQMV 238
Cdd:PRK13537 157 PDVLVLDEPTTGL-DPQARHLmWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG-----RKIAEGAPHALIESEI 230
|
....*...
gi 490997255 239 GRELTQLF 246
Cdd:PRK13537 231 GCDVIEIY 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-228 |
1.02e-28 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 113.43 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCL-----IGIYRPDKGAIRVKGEPV-QFQDTMDALR 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 AGISMIHQELNLVPhMTVAENIWLGrePMKYGFVDHRQLARQTQTLLNKLNI-RLSADRLVG-ELSIAAQQMVEIAKAVS 157
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 158 WNADIVIMDEPTSALTESEVAHLFTIIRDLREQgKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEF 228
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-217 |
1.75e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.56 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 9 EGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepvqfQDTMD-------A 77
Cdd:COG1135 5 ENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG-----VDLTAlserelrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 78 LRAGISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVAL---PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 158 WNADIVIMDEPTSAL---TESEVAHLftiIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG1135 157 NNPKVLLCDEATSALdpeTTRSILDL---LKDINRElGLTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-476 |
2.00e-28 |
|
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: 110.21 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALltedrkksglflvlsvmen 351
Cdd:cd03216 19 VSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 msivnmpeyigksgfvkhmkmaqdcmeqirrlniktptmdqiINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGA 431
Cdd:cd03216 80 ------------------------------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 432 KAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITG 476
Cdd:cd03216 118 VERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-477 |
6.71e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 117.26 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKS----TLMKCLI---GIYRPDKGAIRVKGEPV-----QFQDTMDALR-AGISM 84
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVQCDKMLLRRRSRQVielseQSAAQMRHVRgADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQE--LNLVPHMTVAENIwlgREPMK-YGFVDHRQLARQTQTLLNKLNIRLSA---DRLVGELSIAAQQMVEIAKAVSW 158
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQI---AESIRlHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 159 NADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTR------- 230
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHapqhpyt 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 231 QSLIT------QMVGRELTQLFPKFN-------------NTI--GEEVLTVRNLS-----RKGYF----------EEVNF 274
Cdd:PRK10261 266 RALLAavpqlgAMKGLDYPRRFPLISlehpakqeppieqDTVvdGEPILQVRNLVtrfplRSGLLnrvtrevhavEKVSF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 275 SVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSV--AIEKGMALLTED-------RKKSGlflv 345
Cdd:PRK10261 346 DLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqALRRDIQFIFQDpyasldpRQTVG---- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 346 LSVMENMSIvnmpeyigkSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTR 425
Cdd:PRK10261 422 DSIMEPLRV---------HGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 426 GIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITGI 477
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-482 |
7.06e-28 |
|
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: 116.44 E-value: 7.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGI--YRPDKGAI--------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 63 -------RVKGEPVQFQDTMDALRAGIS-----MIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQtqtLLNKLN 130
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVD---LIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 131 IRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALtESEVAHLF--TIIRDLREQGKAIIYISHKMDEIFAIT 208
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTL-DPQTAKLVhnALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 209 DEisvfrdGTWVgsrQTGEFTRQSLITQMVGR--ELTQLFPKFNNT-IGEEVLTVRNLSRKGY---------FEEVNFSV 276
Cdd:TIGR03269 237 DK------AIWL---ENGEIKEEGTPDEVVAVfmEGVSEVEKECEVeVGEPIIKVRNVSKRYIsvdrgvvkaVDNVSLEV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 277 RRGEILGVAGLVGAGRSEVMESLFGMERFDSGE--VLIDGQPVIIDSPSVaIEKG-----MALLtedRKKSGLFLVLSVM 349
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGP-DGRGrakryIGIL---HQEYDLYPHRTVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENM--SI-VNMPEYIGKSGFVKHMKMAQDCMEQIRRLniktptMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRG 426
Cdd:TIGR03269 384 DNLteAIgLELPDELARMKAVITLKMVGFDEEKAEEI------LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 427 ID----VGAKAEIYHLISELanrGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:TIGR03269 458 MDpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
270-474 |
7.14e-28 |
|
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: 110.45 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspSVAIEKGMALLTEDRkksGLFLVLSVM 349
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYLPEER---GLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSivnmpeYIGKSGFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:cd03269 89 DQLV------YLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 430 GAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03269 162 VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-217 |
8.22e-28 |
|
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: 110.37 E-value: 8.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDaLRAGI 82
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVpHMTVAENIWLGREPMKygfvDHRQLARQTQTLLNKLNIRLSA--DRLVGE----LSIAAQQMVEIAKAV 156
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAPLAD----DERILRAAELAGVTDFVNKHPNglDLQIGErgrgLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 157 SWNADIVIMDEPTSALTESEVAHLFTIIRDLREqGKAIIYISHKMdEIFAITDEISVFRDG 217
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-208 |
9.94e-28 |
|
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: 110.19 E-value: 9.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQ--FQDTMDALRAGI 82
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADI 162
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAF---ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490997255 163 VIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKmDEIFAIT 208
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA-KELVDTT 202
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-218 |
1.07e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 109.65 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGIS-KFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmdaLRAGISMI 85
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE----RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHM-TVAENIWLGREPMKYGfvdhrqlARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:cd03226 77 MQDVDYQLFTdSVREELLLGLKELDAG-------NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-217 |
1.90e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.86 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqDTMDALRAGISM 84
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:COG3839 80 VFQSYALYPHMTVYENIAF---PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 165 MDEPTSAL-------TESEVAHLFtiirdlREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG3839 157 LDEPLSNLdaklrveMRAEIKRLH------RRLGTTTIYVTHDQVEAMTLADRIAVMNDG 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
254-474 |
3.47e-27 |
|
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: 109.74 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNLSRKgyF------EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIE 327
Cdd:COG0411 1 SDPLLEVRGLTKR--FgglvavDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 328 KGMAlltedRK--KSGLFLVLSVMENMSIVnmPEYIGKSGFVKHM-----------KMAQDCMEQIRRLNIkTPTMDQII 394
Cdd:COG0411 79 LGIA-----RTfqNPRLFPELTVLENVLVA--AHARLGRGLLAALlrlprarreerEARERAEELLERVGL-ADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 395 NNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
.
gi 490997255 474 I 474
Cdd:COG0411 231 V 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
272-474 |
3.81e-27 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 108.73 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsvaiEKGMALLTedRKKSG-------LFL 344
Cdd:cd03255 23 VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLS-----EKELAAFR--RRHIGfvfqsfnLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 345 VLSVMENmsiVNMPEYIGKsgfVKHMKMAQDCMEQIRRLNIKTpTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:cd03255 96 DLTALEN---VELPLLLAG---VPKKERRERAEELLERVGLGD-RLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 425 RGIDVGAKAEIYHLISELA-NRGVAVIMVSSElPEILGMSDRVMVMHEGRI 474
Cdd:cd03255 169 GNLDSETGKEVMELLRELNkEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-424 |
8.36e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 8 AEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepvqfqdtmdalRAGISMIHQ 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 88 ELNLVPHMTVAENIWLG----------------------REPMKYGFVDHR-------QLARQTQTLLNKLNIRLS-ADR 137
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGdaelraleaeleeleaklaepdEDLERLAELQEEfealggwEAEARAEEILSGLGFPEEdLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 138 LVGELSiAAQQM-VEIAKAVSWNADIVIMDEPTSaltesevaHLftiirD----------LREQGKAIIYISHkmDEIF- 205
Cdd:COG0488 149 PVSELS-GGWRRrVALARALLSEPDLLLLDEPTN--------HL-----DlesiewleefLKNYPGTVLVVSH--DRYFl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 206 -AITDEISVFRDGT---WVGS-------------RQTGEFTRQ------------------SLITQMVGRE------LTQ 244
Cdd:COG0488 213 dRVATRILELDRGKltlYPGNysayleqraerleQEAAAYAKQqkkiakeeefirrfrakaRKAKQAQSRIkaleklERE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 245 LFPKFNNTI----------GEEVLTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGE 309
Cdd:COG0488 293 EPPRRDKTVeirfppperlGKKVLELEGLS-KSYgdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 310 VLIdGQPVIIdspsvaiekgmALLTEDRkkSGLFLVLSVMENMSivnmpeyigksgfvkhmKMAQDCMEQ-IR----RLN 384
Cdd:COG0488 372 VKL-GETVKI-----------GYFDQHQ--EELDPDKTVLDELR-----------------DGAPGGTEQeVRgylgRFL 420
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 490997255 385 IKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:COG0488 421 FSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-217 |
8.42e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.72 E-value: 8.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVpHM 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR-DLTLESLRRQIGVVPQDTFLF-SG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIWLGREP---------MK----YGFVdhRQLARQTQTLLNKLNIRLSAdrlvGElsiaaQQMVEIAKAVSWNADI 162
Cdd:COG1132 429 TIRENIRYGRPDatdeeveeaAKaaqaHEFI--EALPDGYDTVVGERGVNLSG----GQ-----RQRIAIARALLKDPPI 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 163 VIMDEPTSAL-TESEvAHLFTIIRDLReQGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:COG1132 498 LILDEATSALdTETE-ALIQEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDG 550
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-246 |
1.41e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQdtMDALRA 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR--ARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLVPHMTVAENIWL-GRepmkYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVfGR----YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 160 ADIVIMDEPTSALtESEVAHL-FTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGtwvgsRQTGEFTRQSLITQMV 238
Cdd:PRK13536 191 PQLLILDEPTTGL-DPHARHLiWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG-----RKIAEGRPHALIDEHI 264
|
....*...
gi 490997255 239 GRELTQLF 246
Cdd:PRK13536 265 GCQVIEIY 272
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
2.05e-26 |
|
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: 112.54 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 2 NAFALEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRA 80
Cdd:COG4988 333 GPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQElNLVPHMTVAENIWLGREpmkyGFVDH--RQLARQTQ--TLLNKLNIRLsaDRLVGE----LSIAAQQMVEI 152
Cdd:COG4988 412 QIAWVPQN-PYLFAGTIRENLRLGRP----DASDEelEAALEAAGldEFVAALPDGL--DTPLGEggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 153 AKAVSWNADIVIMDEPTSAL-TESEvAHLFTIIRDLReQGKAIIYISHKMDEIfAITDEISVFRDGTWVGS 222
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLdAETE-AEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQ 552
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
259-473 |
2.14e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 104.63 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 259 TVRNLSRKGY----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLT 334
Cdd:cd00267 1 EIENLSFRYGgrtaLDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD-IAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 335 EdrkksglflvlsvmenmsivnmpeyigksgfvkhmkmaqdcmeqirrlniktptmdqiinnLSGGNQQKVLIARWLLAQ 414
Cdd:cd00267 80 Q-------------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 415 PKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-201 |
2.22e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDAL-RAGISM 84
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFG--PLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 490997255 165 MDEPTSALtESEVAH-LFTIIRDLREQGKAIIYISHKM 201
Cdd:PRK09493 160 FDEPTSAL-DPELRHeVLKVMQDLAEEGMTMVIVTHEI 196
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-201 |
2.31e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.53 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRV------KGEPV-QFQDTMDA 77
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLsQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 78 LRAGISMIHQELNLVPHMTVAENIWLGrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEG--PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490997255 158 WNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKM 201
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-202 |
2.56e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDA-----LR 79
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDkaireLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 AGISMIHQELNLVPHMTVAENiwLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQN--LIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490997255 160 ADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMD 202
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
257-461 |
2.84e-26 |
|
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: 105.64 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLS-RKGY---FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPviIDSPSVAIEKGMAL 332
Cdd:COG4133 2 MLEAENLScRRGErllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP--IRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEDrkkSGLFLVLSVMENMSIVnmpeyigkSGFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLL 412
Cdd:COG4133 80 LGHA---DGLKPELTVRENLRFW--------AALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 413 AQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILG 461
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA 196
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
254-474 |
4.73e-26 |
|
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: 106.22 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspSVAIEK 328
Cdd:COG1127 2 SEPMIEVRNLT-KSFgdrvvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI-----TGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 329 GMALLtedRKK-------SGLFLVLSVMENmsiVNMPEYigksgfvKHMKMAQDCMEQIRRLNIK----TPTMDQIINNL 397
Cdd:COG1127 76 ELYEL---RRRigmlfqgGALFDSLTVFEN---VAFPLR-------EHTDLSEAEIRELVLEKLElvglPGAADKMPSEL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 398 SGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-217 |
7.06e-26 |
|
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: 105.50 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDALRAGISM 84
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT---DVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLG-REPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIV 163
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 164 IMDEPTSALTESEVAHLFTIIRDLR-EQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
257-474 |
9.21e-26 |
|
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: 105.90 E-value: 9.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMA 331
Cdd:COG1120 1 MLEAENLS-VGYggrpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD-LASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEDRKKSGLFlvlSVMEnmsIVNM---PeYIGKSGFVKhmkmAQD---CMEQIRRLNIkTPTMDQIINNLSGGNQQKV 405
Cdd:COG1120 79 YVPQEPPAPFGL---TVRE---LVALgryP-HLGLFGRPS----AEDreaVEEALERTGL-EHLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 406 LIARwLLAQ-PKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG1120 147 LIAR-ALAQePPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-217 |
9.82e-26 |
|
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: 111.08 E-value: 9.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGI 82
Cdd:COG2274 473 DIELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVpHMTVAENIWLGREpmkygFVDHRQL---ARQT------QTLLNKLnirlsaDRLVGE----LSIAAQQM 149
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLGDP-----DATDEEIieaARLAglhdfiEALPMGY------DTVVGEggsnLSGGQRQR 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 150 VEIAKAVSWNADIVIMDEPTSAL-TESEvAHLFTIIRDLReQGKAIIYISHKMdEIFAITDEISVFRDG 217
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALdAETE-AIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKG 685
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-232 |
1.12e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.84 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 25 SLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPvqfqdtMDALRAG---ISMIHQELNLVPHMTVAENI 101
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD------LTALPPAerpVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 102 WLGREP-MKYGFVDHRQLarqtQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHL 180
Cdd:COG3840 93 GLGLRPgLKLTAEQRAQV----EQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 181 FTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQS 232
Cdd:COG3840 169 LDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-199 |
1.34e-25 |
|
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: 109.68 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 3 AFALEAEGISKFFPGV-KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAG 81
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-DADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 82 ISMIHQelnlVPHM---TVAENIWLGRepmKYGFVDH-RQLARQT--QTLLNKLniRLSADRLVGE----LSIAAQQMVE 151
Cdd:TIGR02857 398 IAWVPQ----HPFLfagTIAENIRLAR---PDASDAEiREALERAglDEFVAAL--PQGLDTPIGEggagLSGGQAQRLA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 152 IAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLReQGKAIIYISH 199
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
258-474 |
1.90e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.45 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSR----KGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpvIIDSPSVAIEKGMALL 333
Cdd:cd03268 1 LKTNDLTKtygkKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEdrkkSGLFLVLSVMENMSIvnmpeyigksGFVKHMKMAQDCMEQIRRLNIKTpTMDQIINNLSGGNQQKVLIARWLLA 413
Cdd:cd03268 79 EA----PGFYPNLTARENLRL----------LARLLGIRKKRIDEVLDVVGLKD-SAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
269-473 |
2.03e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 103.70 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsvaiekgmalLTEDRKKSGLflvlsV 348
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS-----------LKELRRKVGL-----V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MENmsivnmPEyigkSGFV------------KHMKMAQDCMEQI-----RRLNIKtPTMDQIINNLSGGNQQKVLIARWL 411
Cdd:cd03225 81 FQN------PD----DQFFgptveeevafglENLGLPEEEIEERveealELVGLE-GLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
255-474 |
2.06e-25 |
|
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: 109.22 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLS---RKGYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFD---SGEVLIDGQPVIIDSPSVa 325
Cdd:COG1123 2 TPLLEVRDLSvryPGGDVpavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 326 IEKGMALLTEDRKKSglFLVLSVMENmsIVNMPEYIGKSgfvkHMKMAQDCMEQIRRLNIKTPtMDQIINNLSGGNQQKV 405
Cdd:COG1123 81 RGRRIGMVFQDPMTQ--LNPVTVGDQ--IAEALENLGLS----RAEARARVLELLEAVGLERR-LDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 406 LIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
258-482 |
3.04e-25 |
|
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: 103.95 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRK-GYFE--EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPsvaIEKGMALLT 334
Cdd:cd03299 1 LKVENLSKDwKEFKlkNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 335 EDRkksGLFLVLSVMENMsivnmpEYIGKSGFVKHMKMAQDCMEQIRRLNIktptmDQIIN----NLSGGNQQKVLIARW 410
Cdd:cd03299 78 QNY---ALFPHMTVYKNI------AYGLKKRKVDKKEIERKVLEIAEMLGI-----DHLLNrkpeTLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 411 LLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
255-476 |
3.65e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.20 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLSRKgY---------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsva 325
Cdd:COG1136 2 SPLLELRNLTKS-YgtgegevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 326 iEKGMALLtedRKKS--------GLFLVLSVMENmsiVNMPEYIGKsgfVKHMKMAQDCMEQIRRLNIkTPTMDQIINNL 397
Cdd:COG1136 77 -ERELARL---RRRHigfvfqffNLLPELTALEN---VALPLLLAG---VSRKERRERARELLERVGL-GDRLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 398 SGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVIMVSSElPEILGMSDRVMVMHEGRITG 476
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
258-474 |
3.75e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 102.59 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRKGY----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALL 333
Cdd:COG4619 1 LELEGLSFRVGgkpiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP-LSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 tedRKKSGLFLVlSVMENMSivnmpeyigksgFVKHMKMAQDCMEQIR----RLNIKTPTMDQIINNLSGGNQQKVLIAR 409
Cdd:COG4619 80 ---PQEPALWGG-TVRDNLP------------FPFQLRERKFDRERALelleRLGLPPDILDKPVERLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 410 WLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-217 |
9.38e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.88 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMD--ALRA 80
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVAL---PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
269-475 |
1.24e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.67 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspsVAI-EKGMALLtedRKKSG------ 341
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL------SRLkRREIPYL---RRRIGvvfqdf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 342 -LFLVLSVMENMSIVnMpEYIGKSgfvkHMKMAQDCMEQIRRLNIKTpTMDQIINNLSGGNQQKVLIARWLLAQPKILIL 420
Cdd:COG2884 89 rLLPDRTVYENVALP-L-RVTGKS----RKEIRRRVREVLDLVGLSD-KAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 421 DEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
258-474 |
2.28e-24 |
|
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: 101.08 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS----RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALL 333
Cdd:cd03218 1 LRAENLSkrygKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDrkkSGLFLVLSVMENMSIVnmPEYIGKSGFVKHMKMAqdcmEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLA 413
Cdd:cd03218 81 PQE---ASIFRKLTVEENILAV--LEIRGLSKKEREEKLE----ELLEEFHI-THLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-199 |
2.87e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPV-QFQ-DTMDALRAgi 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSpAELARRRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 sMIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQ--TQTLLNKLnirlsADRLVGELSIAAQQMVEIAKAVS--W 158
Cdd:PRK13548 80 -VLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAalAQVDLAHL-----AGRDYPQLSGGEQQRVQLARVLAqlW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 159 NAD----IVIMDEPTSALtesEVAH---LFTIIRDL-REQGKAIIYISH 199
Cdd:PRK13548 154 EPDgpprWLLLDEPTSAL---DLAHqhhVLRLARQLaHERGLAVIVVLH 199
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
269-474 |
3.25e-24 |
|
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: 100.87 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsvaiekgmalLTEDRKKSGLflvlsV 348
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN-----------LRELRRKVGL-----V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MEN--MSIVNM---------PEYIGKSG-FVKhmKMAQDCMEQIRRLNIKtptmDQIINNLSGGNQQKVLIARWLLAQPK 416
Cdd:COG1122 81 FQNpdDQLFAPtveedvafgPENLGLPReEIR--ERVEEALELVGLEHLA----DRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 417 ILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-199 |
3.67e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.35 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMD--ALRAgis 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQ--TQTLLNKLnirlsADRLVGELSIAAQQMVEIAKAVS--WN 159
Cdd:COG4559 79 VLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREalALVGLAHL-----AGRSYQTLSGGEQQRVQLARVLAqlWE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 160 AD-----IVIMDEPTSALtesEVAH---LFTIIRDLREQGKAIIYISH 199
Cdd:COG4559 154 PVdggprWLFLDEPTSAL---DLAHqhaVLRLARQLARRGGGVVAVLH 198
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-267 |
3.97e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 3 AFALEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAG 81
Cdd:PRK13647 2 DNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 82 ISMIHQEL-NLVPHMTVAENIWLGrePMKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:PRK13647 81 VGLVFQDPdDQVFSSTVWDDVAFG--PVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVGR 240
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGLR 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 490997255 241 E--LTQLF---PKFNN-----TIGEEVLTVRNLSRKG 267
Cdd:PRK13647 238 LplVAQIFedlPELGQsklplTVKEAVQIIRKLLTKG 274
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-202 |
6.13e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.81 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQF------------QDTMDALRAGISMIH 86
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QELNLVPHMTVAENIWlgREPMKYGFVDHRQLARQTQTLLNKLNIRLSA-DRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PRK10619 99 QHFNLWSHMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMD 202
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
270-474 |
6.31e-24 |
|
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: 99.75 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsVAIEKGMALLTEDRkksGLFLVLSVM 349
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARRRLGFVSDST---GLYDRLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMsivnmpEYIGKSGFVKHMKMAQDCMEQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:cd03266 97 ENL------EYFAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 430 GAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-236 |
8.37e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELnLVPH-MTVAE 99
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS-MLSSRQLARRLALLPQHH-LTPEgITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 NIWLGREPMK--YGFVDHRQLARQTQTLlNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEV 177
Cdd:PRK11231 96 LVAYGRSPWLslWGRLSAEDNARVNQAM-EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 178 AHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQ 236
Cdd:PRK11231 175 VELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
258-481 |
1.52e-23 |
|
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: 98.70 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY---------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIek 328
Cdd:cd03293 1 LEVRNVS-KTYgggggavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 329 gmaLLTEDRkksgLFLVLSVMEN----MSIVNMP------------EYIGKSGFVKHMkmaqdcmeqirrlniktPTMdq 392
Cdd:cd03293 78 ---VFQQDA----LLPWLTVLDNvalgLELQGVPkaeareraeellELVGLSGFENAY-----------------PHQ-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 393 iinnLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVM-- 469
Cdd:cd03293 132 ----LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsa 207
|
250
....*....|..
gi 490997255 470 HEGRITGILDKD 481
Cdd:cd03293 208 RPGRIVAEVEVD 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-217 |
1.64e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.90 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKA--LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtMDALRAGIS 83
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD-PNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVPHmTVAENIwlgrepmkygfvdhrqlarqtqtllnklnirlsadrlvgeLSIAAQQMVEIAKAVSWNADIV 163
Cdd:cd03246 80 YLPQDDELFSG-SIAENI----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 164 IMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMdEIFAITDEISVFRDG 217
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDG 171
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
272-488 |
1.73e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 98.75 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALLTEDRKksgLFLVLSVMEN 351
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGRE---IFPRLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 MsivnmpeyigKSGFVKHMKMAQDCMEQIRRLnikTPTMDQIIN----NLSGGNQQKVLIARWLLAQPKILILDEPTRGI 427
Cdd:TIGR03410 96 L----------LTGLAALPRRSRKIPDEIYEL---FPVLKEMLGrrggDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 428 DVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDEADQETI 488
Cdd:TIGR03410 163 QPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
279-477 |
1.76e-23 |
|
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: 98.14 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 279 GEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpVIIDSpsvaiEKGMALLTEDRKKSGLFLVLSVMENMSIVNMP 358
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDS-----RKKINLPPQQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 359 EYIGKsgFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHL 438
Cdd:cd03297 97 AFGLK--RKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 439 ISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGI 477
Cdd:cd03297 174 LKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-217 |
2.02e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAgISMI 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQ-TQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-217 |
2.17e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 103.65 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFaLEAEGISKFFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTmD 76
Cdd:PRK10535 1 MTAL-LELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA-D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 AL----RAGISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEI 152
Cdd:PRK10535 79 ALaqlrREHFGFIFQRYHLLSHLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 153 AKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKmDEIFAITDEISVFRDG 217
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDG 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-217 |
2.74e-23 |
|
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: 98.46 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVpHM 95
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-EVTLDSLRRAIGVVPQDTVLF-ND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIwlgrepmKYGFVDH-----RQLARQTQTLLNKLNIRLSADRLVGE----LSIAAQQMVEIAKAVSWNADIVIMD 166
Cdd:cd03253 90 TIGYNI-------RYGRPDAtdeevIEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 167 EPTSAL-TESEvAHLFTIIRDLReQGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:cd03253 163 EATSALdTHTE-REIQAALRDVS-KGRTTIVIAHRLSTI-VNADKIIVLKDG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-218 |
4.98e-23 |
|
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: 96.79 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 25 SLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFqdtMDALRAGISMIHQELNLVPHMTVAENIWLG 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA---APPADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 105 REP-MKYGFVDHRQLArqtqTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTI 183
Cdd:cd03298 95 LSPgLKLTAEDRQAIE----VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 490997255 184 IRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
272-424 |
1.16e-22 |
|
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: 93.87 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvAIEKGMALLTEDrkkSGLFLVLSVMEN 351
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQD---PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 352 MSIVNMPEYIGKsgfvKHMKM-AQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:pfam00005 80 LRLGLLLKGLSK----REKDArAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-468 |
1.68e-22 |
|
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: 100.63 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 29 RPGTVHALMGENGAGKSTLMKCLIGIYRPDKGaiRVKGEP-----------VQFQDTMDALRAG-ISMIH--QELNLVPH 94
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLG--DYDEEPswdevlkrfrgTELQDYFKKLANGeIKVAHkpQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 95 M---TVaeniwlgREPMKYgfVDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSA 171
Cdd:COG1245 175 VfkgTV-------RELLEK--VDERGKLDE---LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 172 LTESE---VAHLftiIRDLREQGKAIIYISHKM-------DEIFAITDEISVF-----RDGTWVGSRQ--TG-------- 226
Cdd:COG1245 243 LDIYQrlnVARL---IRELAEEGKYVLVVEHDLaildylaDYVHILYGEPGVYgvvskPKSVRVGINQylDGylpeenvr 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 227 ------EFTRQSLITQMVGRELTQlFPKFNNTIGEEVLTVRnlsrKGYfeevnfsVRRGEILGVAGLVGAGRSEVMESLF 300
Cdd:COG1245 320 irdepiEFEVHAPRREKEEETLVE-YPDLTKSYGGFSLEVE----GGE-------IREGEVLGIVGPNGIGKTTFAKILA 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 301 GMERFDSGEVLID------GQPVIIDSPsvaiekgmalltedrkksglflvLSVMENMSIVNMPEYigKSGFVKHmkmaq 374
Cdd:COG1245 388 GVLKPDEGEVDEDlkisykPQYISPDYD-----------------------GTVEEFLRSANTDDF--GSSYYKT----- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 375 dcmEQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVIMVS 453
Cdd:COG1245 438 ---EIIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVD 513
|
490
....*....|....*
gi 490997255 454 SELPEILGMSDRVMV 468
Cdd:COG1245 514 HDIYLIDYISDRLMV 528
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
258-494 |
1.72e-22 |
|
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: 98.65 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRKGYFE-EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpVIIDSpsvaiEKGMALLTED 336
Cdd:TIGR02142 1 LSARFSKRLGDFSlDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDS-----RKGIFLPPEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 337 RK------KSGLFLVLSVMENMsivnmpEYIGKSGFVKHMKMAQDcmEQIRRLNIKtPTMDQIINNLSGGNQQKVLIARW 410
Cdd:TIGR02142 75 RRigyvfqEARLFPHLSVRGNL------RYGMKRARPSERRISFE--RVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 411 LLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDEADQETIL 489
Cdd:TIGR02142 146 LLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
....*
gi 490997255 490 SLASH 494
Cdd:TIGR02142 226 PWLAR 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
271-473 |
2.24e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.87 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFD---SGEVLIDGQPvIIDSPSVAIEK----GMALLTEDRKKSgLF 343
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGRE-ILNLPEKELNKlraeQISMIFQDPMTS-LN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 LVLSVMENMSIVNMpeyigksgFVKHMKMAQDCMEQIRRLN-IKTPT----MDQIINNLSGGNQQKVLIARWLLAQPKIL 418
Cdd:PRK09473 112 PYMRVGEQLMEVLM--------LHKGMSKAEAFEESVRMLDaVKMPEarkrMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 419 ILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
273-474 |
3.63e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.82 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 273 NFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiEKGMALLTEDrkkSGLFLVLSVMENM 352
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA---ERPVSMLFQE---NNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 353 SIvnmpeyigksGFVKHMKMAQDCMEQI----RRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGID 428
Cdd:COG3840 93 GL----------GLRPGLKLTAEQRAQVeqalERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490997255 429 VGAKAEIYHLISELA-NRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG3840 162 PALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-217 |
3.74e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.24 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVK--ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGIS 83
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS-EETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQEL-NLVPHMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADI 162
Cdd:PRK13635 85 MVFQNPdNQFVGATVQDDVAFGLENIG---VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 163 VIMDEPTSALTESEVAHLFTIIRDLREQGKA-IIYISHKMDEIfAITDEISVFRDG 217
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-217 |
4.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.83 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQEL-NLVPHMTVA 98
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-KENLKEIRKKIGIIFQNPdNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVA 178
Cdd:PRK13632 103 DDIAFGLENKK---VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 179 HLFTIIRDLREQG-KAIIYISHKMDEIFaITDEISVFRDG 217
Cdd:PRK13632 180 EIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
258-474 |
4.25e-22 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 94.49 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS---RKGYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpvIIDSPSVAIEKGMA 331
Cdd:cd03263 1 LQIRNLTktyKKGTKpavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEDRkksGLFLVLSVMENMSIVNMPeyigKSGFVKHMKMAQDCMeqIRRLNIkTPTMDQIINNLSGGNQQKVLIARWL 411
Cdd:cd03263 79 YCPQFD---ALFDELTVREHLRFYARL----KGLPKSEIKEEVELL--LRVLGL-TDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
270-474 |
4.40e-22 |
|
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: 94.96 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPsvaiekgmALLTEDRKKSGL----FLV 345
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSG--------KELRKARRRIGMifqhFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 346 LS---VMENmsiVNMPEYIGksgfvkHMKMAqdcmEQIRRLNiktPTMDQI---------INNLSGGNQQKVLIARWLLA 413
Cdd:cd03258 94 LSsrtVFEN---VALPLEIA------GVPKA----EIEERVL---ELLELVgledkadayPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-468 |
9.16e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 98.34 E-value: 9.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 28 VRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGaiRVKGEP-----------VQFQDTMDALRAG-ISMIH--QELNLVP 93
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLG--DYEEEPswdevlkrfrgTELQNYFKKLYNGeIKVVHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 94 HM---TVaeniwlgREPMKYgfVDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:PRK13409 174 KVfkgKV-------RELLKK--VDERGKLDE---VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 171 ALTESE---VAHLftiIRDLREqGKAIIYISHKM-------DEIFAITDEISVF-----RDGTWVGSRQ--TG------- 226
Cdd:PRK13409 242 YLDIRQrlnVARL---IRELAE-GKYVLVVEHDLavldylaDNVHIAYGEPGAYgvvskPKGVRVGINEylKGylpeenm 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 227 -------EFTRQSLITQMVGRELTQlFPKFNNTIGEEVLTVrnlsRKGYfeevnfsVRRGEILGVAGLVGAGRSEVMESL 299
Cdd:PRK13409 318 rirpepiEFEERPPRDESERETLVE-YPDLTKKLGDFSLEV----EGGE-------IYEGEVIGIVGPNGIGKTTFAKLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 300 FGMERFDSGEVLID------GQPVIIDSPsvaiekgmalltedrkksglflvLSVMENMSivNMPEYIGKSgFVKHmkma 373
Cdd:PRK13409 386 AGVLKPDEGEVDPElkisykPQYIKPDYD-----------------------GTVEDLLR--SITDDLGSS-YYKS---- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 374 qdcmEQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV-----GAKAeIYHLIselANRGVA 448
Cdd:PRK13409 436 ----EIIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlaVAKA-IRRIA---EEREAT 506
|
490 500
....*....|....*....|
gi 490997255 449 VIMVSSELPEILGMSDRVMV 468
Cdd:PRK13409 507 ALVVDHDIYMIDYISDRLMV 526
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
1.05e-21 |
|
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: 93.65 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAfALEAEGISKFFP-----GVK--ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVK--GEPV-- 69
Cdd:COG4778 1 MTT-LLEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 70 -QFQD-TMDALRAG-ISMIHQELNLVPHMT----VAeniwlgrEPMKYGFVDHRQLARQTQTLLNKLNIRlsaDRLV--- 139
Cdd:COG4778 80 aQASPrEILALRRRtIGYVSQFLRVIPRVSaldvVA-------EPLLERGVDREEARARARELLARLNLP---ERLWdlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 140 ------GElsiaaQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISV 213
Cdd:COG4778 150 patfsgGE-----QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVD 224
|
....*
gi 490997255 214 FRDGT 218
Cdd:COG4778 225 VTPFS 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
257-474 |
1.19e-21 |
|
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: 95.51 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLS-----RKGYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMER---FDSGEVLIDGQPVIIDSPSva 325
Cdd:COG0444 1 LLEVRNLKvyfptRRGVVkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 326 iekgmalltEDRKKSGlflvlsvmENMSIV--------NmPEY-IGKS---GFVKHMKM-AQDCMEQIRRL----NIKTP 388
Cdd:COG0444 79 ---------ELRKIRG--------REIQMIfqdpmtslN-PVMtVGDQiaePLRIHGGLsKAEARERAIELlervGLPDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 389 tmDQIINN----LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMS 463
Cdd:COG0444 141 --ERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIA 218
|
250
....*....|.
gi 490997255 464 DRVMVMHEGRI 474
Cdd:COG0444 219 DRVAVMYAGRI 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-231 |
1.24e-21 |
|
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: 97.95 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGA--IRVKGEPVQFQDTMDALRAG----ISMIHQELNL 91
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRGRakryIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 92 VPHMTVAENIwlgREPMKYGFVDHRQLARQTQTL----LNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDE 167
Cdd:TIGR03269 377 YPHRTVLDNL---TEAIGLELPDELARMKAVITLkmvgFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 168 PTSAL---TESEVAHlfTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQ 231
Cdd:TIGR03269 454 PTGTMdpiTKVDVTH--SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
257-474 |
1.40e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.79 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSRKgyF------EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspSVAIEKGM 330
Cdd:COG4152 1 MLELKGLTKR--FgdktavDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 ALLTEDRkksGLFLVLSVMENMsivnmpEYIGKsgfVKHMKmAQDCMEQIR----RLNIKTPTMDQiINNLSGGNQQKVL 406
Cdd:COG4152 74 GYLPEER---GLYPKMKVGEQL------VYLAR---LKGLS-KAEAKRRADewleRLGLGDRANKK-VEELSKGNQQKVQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 407 IARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-199 |
1.48e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGV---------KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDT-- 74
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRaq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 75 MDALRAGISMIHQE-LNLV-PHMTVAENIwlgREPMKY--GFVDHRQLARqTQTLLNKLNIRLS-ADRLVGELSIAAQQM 149
Cdd:PRK10419 84 RKAFRRDIQMVFQDsISAVnPRKTVREII---REPLRHllSLDKAERLAR-ASEMLRAVDLDDSvLDKRPPQLSGGQLQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 150 VEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISH 199
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITH 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
258-474 |
1.51e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 92.59 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRK-GYFE---EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAiekgmall 333
Cdd:cd03262 1 IEIKNLHKSfGDFHvlkGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIN-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 tEDRKKSG-------LFLVLSVMENMSIVNMpeyigksgFVKHMKMAQ---DCMEQIRRLNIKtPTMDQIINNLSGGNQQ 403
Cdd:cd03262 73 -ELRQKVGmvfqqfnLFPHLTVLENITLAPI--------KVKGMSKAEaeeRALELLEKVGLA-DKADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 404 KVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-209 |
1.65e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.17 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqdTMDAL----RAG 81
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THLPMhkraRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 82 ISMIHQELNLVPHMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNAD 161
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRK---LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 162 IVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITD 209
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICD 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
272-475 |
1.66e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 92.32 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidsPSVAIEKGMALLTEDrKKSGLFLVlSVMEN 351
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVMQD-VDYQLFTD-SVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 MSIVNMPEYIGKsgfvkhmkmaQDCMEQIRRLNIKTPtMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGA 431
Cdd:cd03226 93 LLLGLKELDAGN----------EQAETVLKDLDLYAL-KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490997255 432 KAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
269-474 |
1.96e-21 |
|
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: 91.12 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiEKGM---ALLTEDRKKSGlflv 345
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN---ELGDhvgYLPQDDELFSG---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 346 lSVMENMsivnmpeyigksgfvkhmkmaqdcmeqirrlniktptmdqiinnLSGGNQQKVLIARWLLAQPKILILDEPTR 425
Cdd:cd03246 91 -SIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 426 GIDVGAKAEIYHLISELANRGVAVIMVSSElPEILGMSDRVMVMHEGRI 474
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
260-474 |
2.86e-21 |
|
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: 92.05 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 260 VRNLSRK-GYFE---EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVaiekgmallte 335
Cdd:cd03265 3 VENLVKKyGDFEavrGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 336 dRKKSGL-FLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQ 414
Cdd:cd03265 72 -RRRIGIvFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 415 PKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
258-474 |
3.75e-21 |
|
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: 92.25 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVaiekgma 331
Cdd:cd03256 1 IEVENLS-KTYpngkkaLKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 lLTEDRKKSG-LF----LV--LSVMENmsiVNMPEYIGKS-------GFVKHMKmaQDCMEQIRRLNIKTpTMDQIINNL 397
Cdd:cd03256 73 -LRQLRRQIGmIFqqfnLIerLSVLEN---VLSGRLGRRStwrslfgLFPKEEK--QRALAALERVGLLD-KAYQRADQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 398 SGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-225 |
3.82e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.16 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTmDALRAGISMIHQElNLVPHMTVAE 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQE-NVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 NIWLGREPMKYGFVDhrQLARQTQTLLNKLNIRLSADRLVGE----LSIAAQQMVEIAKAVSWNADIVIMDEPTSAL-TE 174
Cdd:cd03252 95 NIALADPGMSMERVI--EAAKLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALdYE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 175 SEVAhlftIIRDLRE--QGKAIIYISHKMDEIFAiTDEISVFRDGTWV--GSRQT 225
Cdd:cd03252 173 SEHA----IMRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVeqGSHDE 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-218 |
3.84e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 91.90 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVPHm 95
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIWLGREPMKygfvDHRQLARQTQTLLNKLNIRLSA--DRLVGE----LSIAAQQMVEIAKAVSWNADIVIMDEPT 169
Cdd:cd03254 92 TIMENIRLGRPNAT----DEEVIEAAKEAGAHDFIMKLPNgyDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 170 SAL-TESEVAhlftIIRDLRE--QGKAIIYISHKMDEI-FAitDEISVFRDGT 218
Cdd:cd03254 168 SNIdTETEKL----IQEALEKlmKGRTSIIIAHRLSTIkNA--DKILVLDDGK 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-217 |
7.88e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 7.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGrepmkyGFVDHRQLARQTQTLLNKLNIRLSADRL--VGELSIAAQQMVEIAKAVSWNADIV 163
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYELFPRLHERRIqrAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 164 IMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
271-477 |
8.19e-21 |
|
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: 93.63 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpVIIDSpsvaiEKGMALLTEDRK------KSGLFL 344
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDS-----ARGIFLPPHRRRigyvfqEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 345 VLSVMENMsivnmpEYIGKSGFVKHMKMAQDcmEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:COG4148 91 HLSVRGNL------LYGRKRAPRAERRISFD--EVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 425 RGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITGI 477
Cdd:COG4148 162 AALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-222 |
9.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 9.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQF-QDTMDALRAGIS 83
Cdd:PRK13639 2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELN---LVPhmTVAENIWLGrePMKYGFvDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:PRK13639 82 IVFQNPDdqlFAP--TVEEDVAFG--PLNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGS 222
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-211 |
1.24e-20 |
|
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: 89.53 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIG--IYRPDKGAIRVKGEPVqfqdTMDALRAGISMIHQELNLVPHMTVA 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL----DKRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 EniwlgrepmkygfvdhrqlarqtqTLLNKLNIR-LSAdrlvGE---LSIAaqqmVEIAkavsWNADIVIMDEPTSALTE 174
Cdd:cd03213 101 E------------------------TLMFAAKLRgLSG----GErkrVSIA----LELV----SNPSLLFLDEPTSGLDS 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 490997255 175 SEVAHLFTIIRDLREQGKAIIYISHKM-DEIFAITDEI 211
Cdd:cd03213 145 SSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKL 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-236 |
2.03e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDT-MDALRAGISMIHQELNL-VPHMTVA 98
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgLLALRQQVATVFQDPEQqIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVA 178
Cdd:PRK13638 97 SDIAFSLRNLG---VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 179 HLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGE-FTRQSLITQ 236
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEvFACTEAMEQ 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
257-474 |
2.17e-20 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 90.12 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSrKGY------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVaiekgm 330
Cdd:COG3638 2 MLELRNLS-KRYpggtpaLDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 alLTEDRKKSGL-F----LV--LSVMENmsiVNMPeYIGKSGFVKHM------KMAQDCMEQIRRLNIkTPTMDQIINNL 397
Cdd:COG3638 75 --LRRLRRRIGMiFqqfnLVprLSVLTN---VLAG-RLGRTSTWRSLlglfppEDRERALEALERVGL-ADKAYQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 398 SGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
257-474 |
2.22e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 90.05 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLsRKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAiekgma 331
Cdd:COG1126 1 MIEIENL-HKSFgdlevLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 lltEDRKKSG-------LFLVLSVMENMSIvnmpeyigksGFVKHMKMAQD-----CMEQIRRLNI--KtptMDQIINNL 397
Cdd:COG1126 74 ---KLRRKVGmvfqqfnLFPHLTVLENVTL----------APIKVKKMSKAeaeerAMELLERVGLadK---ADAYPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 398 SGGNQQKVLIARWLLAQPKILILDEPTRGID---VGakaEIYHLISELANRGVAVIMVSSElpeilgM------SDRVMV 468
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHE------MgfarevADRVVF 208
|
....*.
gi 490997255 469 MHEGRI 474
Cdd:COG1126 209 MDGGRI 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
226-474 |
2.64e-20 |
|
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: 90.40 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 226 GEFTRQSLITQMVGRELTQLFPKFNNTIGeevltVRNlsrkgyfeeVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERF 305
Cdd:cd03294 11 GKNPQKAFKLLAKGKSKEEILKKTGQTVG-----VND---------VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 306 DSGEVLIDGQPVIidspsvAIEKGmALLTEDRKKSGL-FLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLN 384
Cdd:cd03294 77 TSGKVLIDGQDIA------AMSRK-ELRELRRKKISMvFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 385 IKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMS 463
Cdd:cd03294 150 LE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLG 228
|
250
....*....|.
gi 490997255 464 DRVMVMHEGRI 474
Cdd:cd03294 229 DRIAIMKDGRL 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
272-474 |
2.85e-20 |
|
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: 89.00 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPV--IIDSPSVAIEKGMALLTEDRKksgLFLVLSVM 349
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGRAIPYLRRKIGVVFQDFR---LLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIVnmPEYIGksgfVKHMKMAQDCMEQIRRLNIKTPTmDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:cd03292 97 ENVAFA--LEVTG----VPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 430 GAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03292 170 DTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
272-474 |
2.94e-20 |
|
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: 89.60 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPsvAIEKGMALLTEdrkKSGLFLVLSVMEN 351
Cdd:cd03300 19 VSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-ITNLP--PHKRPVNTVFQ---NYALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 ----MSIVNMPEYIGKSGFVKHMKMAQdcMEQIRRLNIktptmdqiiNNLSGGNQQKVLIARWLLAQPKILILDEPTRGI 427
Cdd:cd03300 93 iafgLRLKKLPKAEIKERVAEALDLVQ--LEGYANRKP---------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 428 DVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03300 162 DLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-217 |
2.96e-20 |
|
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: 89.52 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtMDALRAGISMIHQELNLVPhM 95
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIWLGREPMKygFVDHRQLARQT------QTLLNKLnirlsaDRLVGE----LSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03249 92 TIAENIRYGKPDAT--DEEVEEAAKKAnihdfiMSLPDGY------DTLVGErgsqLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 166 DEPTSAL-TESEvahlfTIIR---DLREQGKAIIYISHKMDEIFAiTDEISVFRDG 217
Cdd:cd03249 164 DEATSALdAESE-----KLVQealDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
252-479 |
3.35e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.15 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 252 TIGEEVLTVRNLSrKGY---------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSP 322
Cdd:COG1116 2 SAAAPALELRGVS-KRFptggggvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 323 SVAIekgmaLLTEDRkksgLFLVLSVMEN----MSIVNMP---------EYIGK---SGFVKHMkmaqdcmeqirrlnik 386
Cdd:COG1116 81 DRGV-----VFQEPA----LLPWLTVLDNvalgLELRGVPkaerrerarELLELvglAGFEDAY---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 387 tPtmdqiiNNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDR 465
Cdd:COG1116 136 -P------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADR 208
|
250
....*....|....*.
gi 490997255 466 VMVMHE--GRITGILD 479
Cdd:COG1116 209 VVVLSArpGRIVEEID 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-227 |
3.94e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.82 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDALRAGISMI 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS---HVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDGTWVgsrQTGE 227
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV---QIGE 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
269-473 |
4.45e-20 |
|
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: 87.44 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDrkkSGLFlvlsv 348
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRDLDLESLRKNIAYVPQD---PFLF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 meNMSIvnmpeyigksgfvkhmkmaqdcmeqirRLNIktptmdqiinnLSGGNQQKVLIARWLLAQPKILILDEPTRGID 428
Cdd:cd03228 89 --SGTI---------------------------RENI-----------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 429 VGAKAEIYHLISELAnRGVAVIMVSSELPEILgMSDRVMVMHEGR 473
Cdd:cd03228 129 PETEALILEALRALA-KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
258-482 |
6.46e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 88.39 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLsRKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERF-----DSGEVLIDGQPVIIDSPSVaie 327
Cdd:cd03260 1 IELRDL-NVYYgdkhaLKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 328 kgmallTEDRKKSG-LF-----LVLSVMENMSIVnmPEYIGKSGFVKHMKMAQDCMEQI-------RRLNIKtptmdqii 394
Cdd:cd03260 77 ------LELRRRVGmVFqkpnpFPGSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAalwdevkDRLHAL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 395 nNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRgVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03260 141 -GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
....*...
gi 490997255 475 TGILDKDE 482
Cdd:cd03260 219 VEFGPTEQ 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-236 |
7.79e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.48 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQEL-NLVPHMT 96
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT-KENIREVRKFVGLVFQNPdDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGrePMKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESE 176
Cdd:PRK13652 96 VEQDIAFG--PINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 177 VAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGE-FTRQSLITQ 236
Cdd:PRK13652 173 VKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEiFLQPDLLAR 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-218 |
8.10e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 8.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPV-----QFQDtmdalra 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrsiQQRD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 gISMIHQELNLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNA 160
Cdd:PRK11432 80 -ICMVFQSYALFPHMSLGENVGYG---LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
272-474 |
9.11e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.34 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpviidspsVAIEKGMALLTEDRKKSGLF-------- 343
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG---------VDITDKKVKLSDIRKKVGLVfqypeyql 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 ---------------LVLS-------VMENMSIVNMP--EYIGKSGFvkhmkmaqdcmeqirrlniktptmdqiinNLSG 399
Cdd:PRK13637 97 feetiekdiafgpinLGLSeeeienrVKRAMNIVGLDyeDYKDKSPF-----------------------------ELSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 400 GNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
241-475 |
1.04e-19 |
|
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: 88.16 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 241 ELTQLFPKFNNTIGEEVL--TVRNLSRKGYFE-----EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLID 313
Cdd:cd03267 2 EVSNLSKSYRVYSKEPGLigSLKSLFKRKYREvealkGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 314 GqpVIIDSPSVAIEKGMALLTEdrKKSGLFLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQirrlnikTPTMDQI 393
Cdd:cd03267 82 G--LVPWKRRKKFLRRIGVVFG--QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-------EELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 394 INNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
...
gi 490997255 473 RIT 475
Cdd:cd03267 231 RLL 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-217 |
1.25e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.03 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMI 85
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKYgfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-225 |
1.37e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.72 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 25 SLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPvqFQDTMDALRAgISMIHQELNLVPHMTVAENIWLG 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRP-VSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 105 REP-MKygfVDHRQlARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTI 183
Cdd:PRK10771 96 LNPgLK---LNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 184 IRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGT--WVGSRQT 225
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRiaWDGPTDE 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-217 |
1.49e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.01 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqDTMDALRAGISMI 85
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI---THVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQK---TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 166 DEPTSAL-------TESEVAHLftiirdLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK09452 169 DESLSALdyklrkqMQNELKAL------QRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
270-477 |
1.62e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpSVAIEKGMALLTEDRKKSGLFLVLSVM 349
Cdd:PRK09536 20 DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 EnmsivnMPEYIGKSGFVKHMKMAQDCMEQ-IRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGID 428
Cdd:PRK09536 99 E------MGRTPHRSRFDTWTETDRAAVERaMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 429 VGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGI 477
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAA 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-217 |
1.70e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.83 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGA-IRVKGEPVQfQDTMDALRAGIS 83
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRG-GEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQEL--NLVPHMTVAE--------NIWLGREPMKygfvDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIA 153
Cdd:COG1119 82 LVSPALqlRFPRDETVLDvvlsgffdSIGLYREPTD----EQRERARE---LLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 154 KAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQG-KAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
271-474 |
1.74e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPviIDSPSVAIEKGMALLtedRKKSG-------LF 343
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH--FDFSKTPSDKAIREL---RRNVGmvfqqynLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 LVLSVMENMsiVNMPEYIgkSGFVKHMKMAQdCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEP 423
Cdd:PRK11124 95 PHLTVQQNL--IEAPCRV--LGLSKDQALAR-AEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 424 TRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
269-482 |
2.07e-19 |
|
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: 91.43 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPV-IIDSPSVaiekgmalltedRKKSGLFL--- 344
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrQIDPASL------------RRQIGVVLqdv 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 345 VL---SVMENMSIVNmpEYIGKSGFVKHMKMAQdCMEQIRRLniktPT-MDQII----NNLSGGNQQKVLIARWLLAQPK 416
Cdd:COG2274 559 FLfsgTIRENITLGD--PDATDEEIIEAARLAG-LHDFIEAL----PMgYDTVVgeggSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 417 ILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELpEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEE 695
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-264 |
3.44e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.37 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG-----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVK----GEPVQFQDTMD 76
Cdd:PRK13631 22 LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 A-----------LRAGISMIHQ--ELNLVPHmTVAENIWLGREPMKYGFVDHRQLARQtqtLLNKLNIRLS-ADRLVGEL 142
Cdd:PRK13631 102 NpyskkiknfkeLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKF---YLNKMGLDDSyLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 143 SIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGS 222
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 223 RQTGE-FTRQSLITQM---------VGRELTQLFPKFNNTIGEEVLTVRNLS 264
Cdd:PRK13631 258 GTPYEiFTDQHIINSTsiqvprviqVINDLIKKDPKYKKLYQKQPRTIEQLA 309
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-271 |
5.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQ---DTMDALRAGISMIHQ--ELNLVP 93
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnKNLKKLRKKVSLVFQfpEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 94 HmTVAENIWLGrePMKYGFVDhrQLAR-QTQTLLNKLNIRLS-ADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSA 171
Cdd:PRK13641 101 N-TVLKDVEFG--PKNFGFSE--DEAKeKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 172 LTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEI---------------SVFRDGTWVGSRQTGEFTrqsliTQ 236
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVlvlehgklikhaspkEIFSDKEWLKKHYLDEPA-----TS 250
|
250 260 270
....*....|....*....|....*....|....*...
gi 490997255 237 MVGRELTQL---FPKFNNTIGEEVLTVRNlSRKGYFEE 271
Cdd:PRK13641 251 RFASKLEKGgfkFSEMPLTIDELVDGIKN-NLKGGFHE 287
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-220 |
6.32e-19 |
|
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: 85.75 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVpHMT 96
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR-DYTLASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGREPMKYGFVdhRQLARQTQTLLNKLNIRLSADRLVGE----LSIAAQQMVEIAKAVSWNADIVIMDEPTSAL 172
Cdd:cd03251 92 VAENIAYGRPGATREEV--EEAARAANAHEFIMELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 173 -TESEVAhlftIIRDLRE--QGKAIIYISHKMDEIfAITDEISVFRDGTWV 220
Cdd:cd03251 170 dTESERL----VQAALERlmKNRTTFVIAHRLSTI-ENADRIVVLEDGKIV 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-230 |
8.69e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.73 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKC---LIGIYRPDK--GAIRVKGEPVqFQDTMDALRA 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARvsGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLVPHMTVAENIWLGREpMKYGFVDHRQLARQTQTLLNKLNI------RLSADrlVGELSIAAQQMVEIAK 154
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLK-LNRLVKSKKELQERVRWALEKAQLwdevkdRLDAP--AGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 155 AVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQgKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGE-FTR 230
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREvFTN 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
255-473 |
8.92e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLS-RKGYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAI-EKG 329
Cdd:PRK11300 3 QPLLSVSGLMmRFGGLlavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH-IEGLPGHQIaRMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 330 MALLTEDRKksgLFLVLSVMENMsIVNMPEYIgKSGFVKHM-------KMAQDCMEQ----IRRLNIkTPTMDQIINNLS 398
Cdd:PRK11300 82 VVRTFQHVR---LFREMTVIENL-LVAQHQQL-KTGLFSGLlktpafrRAESEALDRaatwLERVGL-LEHANRQAGNLA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 399 GGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-209 |
9.64e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqDTMDALRAgisM 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---EGPGAERG---V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQ---MLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 165 MDEPTSAL---TESEVAHLftIIRDLREQGKAIIYISHKMDE-IFAITD 209
Cdd:PRK11248 152 LDEPFGALdafTREQMQTL--LLKLWQETGKQVLLITHDIEEaVFMATE 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-250 |
9.82e-19 |
|
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: 90.07 E-value: 9.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVK--ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpvqfqdtmdALRAGIS 83
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVPHMTVAENIWLGREPM----KYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:TIGR01257 2009 DVHQNMGYCPQFDAIDDLLTGREHLylyaRLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 160 ADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTW--VGSRQ--TGEFTRQSLIT 235
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFqcLGTIQhlKSKFGDGYIVT 2168
|
250
....*....|....*
gi 490997255 236 QMVGRELTQLFPKFN 250
Cdd:TIGR01257 2169 MKIKSPKDDLLPDLN 2183
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-217 |
1.02e-18 |
|
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: 83.52 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfQDTMDALRAGISMIHQElnlvPHMtva 98
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLISVLNQR----PYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 eniwlgrepmkygFVDhrqlarqtqTLLNKLNIRLSAdrlvGElsiaaQQMVEIAKAVSWNADIVIMDEPTSAL---TES 175
Cdd:cd03247 87 -------------FDT---------TLRNNLGRRFSG----GE-----RQRLALARILLQDAPIVLLDEPTVGLdpiTER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 176 EVahLFTIIRDLREqgKAIIYISHKMDEIFAItDEISVFRDG 217
Cdd:cd03247 136 QL--LSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENG 172
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
275-474 |
1.03e-18 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 84.47 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 275 SVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiEKGMALLTEDrkkSGLFLVLSVMENMSI 354
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQE---NNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 355 vnmpeyiGKSGFVKHMKMAQDCMEQI-RRLNIKTpTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKA 433
Cdd:cd03298 94 -------GLSPGLKLTAEDRQAIEVAlARVGLAG-LEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 434 EIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03298 166 EMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-220 |
1.06e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkGEPVQF----QDtmdalrag 81
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyfdQH-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 82 ismiHQELNlvPHMTVAENIWLGREPMKygfvdhRQLARQtqtLLNKLNirLSADRL---VGELS------IAaqqmveI 152
Cdd:COG0488 387 ----QEELD--PDKTVLDELRDGAPGGT------EQEVRG---YLGRFL--FSGDDAfkpVGVLSggekarLA------L 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 153 AKAVSWNADIVIMDEPT--------SALTESevahlftiirdLRE-QGkAIIYISHkmDEIF--AITDEISVFRDGTWV 220
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTnhldietlEALEEA-----------LDDfPG-TVLLVSH--DRYFldRVATRILEFEDGGVR 508
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-217 |
1.49e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGA---IRVKGEPVQ----FQDTMDAL 78
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQregrLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 79 RAGISMIHQELNLVPHMTVAENIWLG--------REPMKYGFVDHRQLARQTqtlLNKLNIRLSADRLVGELSIAAQQMV 150
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGalgstpfwRTCFSWFTREQKQRALQA---LTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 151 EIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-222 |
2.00e-18 |
|
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: 83.35 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGI--YRPDKGAIRVKGEPVQFQDTMDALRAGISMIHQELNLVPH 94
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 95 MTVAEniwlgrepmkygfvdhrqlarqtqtLLNKLNIRLSAdrlvGElsiaaQQMVEIAKAVSWNADIVIMDEPTSALTE 174
Cdd:cd03217 92 VKNAD-------------------------FLRYVNEGFSG----GE-----KKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490997255 175 SEVAHLFTIIRDLREQGKAIIYISHKmDEIFA--ITDEISVFRDGTWVGS 222
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHY-QRLLDyiKPDRVHVLYDGRIVKS 186
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
272-474 |
2.01e-18 |
|
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: 84.24 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFD---SGEVLIDGQPVIIDSpsvaIEKGMALLTEDrkksGLFL-VLS 347
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQ----FQKCVAYVRQD----DILLpGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 VMEN---MSIVNMPEYigKSGFVKHMKMAQdcmEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:cd03234 98 VRETltyTAILRLPRK--SSDAIRKKRVED---VLLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 425 RGIDVGAKAEIYHLISELANRGVAVIM-VSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
258-479 |
2.30e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.59 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS-----RKGyFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLI---DGQPVIIDSPSVAiEKG 329
Cdd:PRK11701 7 LSVRGLTklygpRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEA-ERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 330 MALLTE-----DRKKSGLFLVLSVMENMSIVNMPeyIGKSGFVKHMKMAQDCMEqirRLNIKTPTMDQIINNLSGGNQQK 404
Cdd:PRK11701 85 RLLRTEwgfvhQHPRDGLRMQVSAGGNIGERLMA--VGARHYGDIRATAGDWLE---RVEIDAARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 405 VLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI--TGILD 479
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVveSGLTD 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
272-474 |
2.69e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPviIDSPSVAIEKGMALLtedRKKSG-------LFL 344
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ--FDFSQKPSEKAIRLL---RQKVGmvfqqynLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 345 VLSVMENMsiVNMPeyigksgfVKHMKMAQD-----CMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILI 419
Cdd:COG4161 96 HLTVMENL--IEAP--------CKVLGLSKEqarekAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 420 LDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
270-475 |
2.98e-18 |
|
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: 83.40 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEIL---------GVAGLVG---AGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsVAIEKGMALLTEDr 337
Cdd:cd03264 4 ENLTKRYGKKRALdgvsltlgpGMYGLLGpngAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--QKLRRRIGYLPQE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 338 kksglflvLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKI 417
Cdd:cd03264 81 --------FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 418 LILDEPTRGIDVGAKAEIYHLISELA-NRgvaVIMVSSELPE-ILGMSDRVMVMHEGRIT 475
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGeDR---IVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
257-474 |
3.29e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLsRKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMA 331
Cdd:COG1137 3 TLEAENL-VKSYgkrtvVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEDrkkSGLFLVLSVMEN-MSIVnmpEYIGKSGfvkhmKMAQDCMEQ-IRRLNI----KTPTMdqiinNLSGGNQQKV 405
Cdd:COG1137 82 YLPQE---ASIFRKLTVEDNiLAVL---ELRKLSK-----KEREERLEElLEEFGIthlrKSKAY-----SLSGGERRRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 406 LIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIM----VSselpEILGMSDRVMVMHEGRI 474
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLItdhnVR----ETLGICDRAYIISEGKV 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-172 |
4.56e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.93 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKC------LIGIYRPDkGAIRVKGEPVqFQDTMD-- 76
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGARVE-GEILLDGEDI-YDPDVDvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 ALRAGISMIHQELNLVPhMTVAENIWLGrePMKYGFVDHRQLARQTQTLLNKLNI------RLsaDRLVGELSIAAQQMV 150
Cdd:COG1117 89 ELRRRVGMVFQKPNPFP-KSIYDNVAYG--LRLHGIKSKSELDEIVEESLRKAALwdevkdRL--KKSALGLSGGQQQRL 163
|
170 180
....*....|....*....|..
gi 490997255 151 EIAKAVSWNADIVIMDEPTSAL 172
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSAL 185
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-217 |
4.96e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDALRAGISM 84
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS---RLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQELNLVPHMTVAENIWLG------RE-PMKYgfvdhrQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltvlprRErPNAA------AIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 158 WNADIVIMDEPTSALTESEVAHLFTIIRDLREQGK-AIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
254-474 |
5.98e-18 |
|
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: 82.64 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNlsrkgyfeeVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVaIEKGMALL 333
Cdd:cd03245 14 NQEIPALDN---------VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDrkkSGLFLVlSVMENMS----------IVNMPEYIGKSGFVKHMKMAQDCM--EQIRrlniktptmdqiinNLSGGN 401
Cdd:cd03245 84 PQD---VTLFYG-TLRDNITlgapladderILRAAELAGVTDFVNKHPNGLDLQigERGR--------------GLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 402 QQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPeILGMSDRVMVMHEGRI 474
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
257-474 |
6.11e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSR--KG--YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMAL 332
Cdd:PRK10895 3 TLTAKNLAKayKGrrVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEDrkkSGLFLVLSVMEN-MSIVNMPEYIGKSgfvKHMKMAQDCMEQIRRLNIKtptmDQIINNLSGGNQQKVLIARWL 411
Cdd:PRK10895 83 LPQE---ASIFRRLSVYDNlMAVLQIRDDLSAE---QREDRANELMEEFHIEHLR----DSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-223 |
6.15e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 9 EGISK-FFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAI--------RVKGEPVQFqdtmdaLR 79
Cdd:PRK10908 5 EHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditRLKNREVPF------LR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 AGISMIHQELNLVPHMTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAI---PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 160 ADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSR 223
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-237 |
6.45e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.38 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIG-IY-RPDKGAIRVKGEPVQFQDTMDALRAGISMI---HQELN 90
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYgRNISGTVFKDGKEVDVSTVSDAIDAGLAYVtedRKGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 91 LVPHMTVAENIWLGREP--MKYGFVDHRQLARQTQTLLNKLNIRL-SADRLVGELSIAAQQMVEIAKAVSWNADIVIMDE 167
Cdd:NF040905 351 LNLIDDIKRNITLANLGkvSRRGVIDENEEIKVAEEYRKKMNIKTpSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 168 PT-----SALTEsevahLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQM 237
Cdd:NF040905 431 PTrgidvGAKYE-----IYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-213 |
1.02e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.99 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDT--MDALRAGISMIHQE----LNlv 92
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSDIQMIFQDplasLN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 PHMTVAENIwlgREPMKygfVDHRQLARQT-----QTLLNKLNIRLSA-DRLVGELSIAAQQMVEIAKAVSWNADIVIMD 166
Cdd:PRK15079 113 PRMTIGEII---AEPLR---TYHPKLSRQEvkdrvKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 167 EPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISV 213
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLV 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-211 |
1.08e-17 |
|
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: 81.93 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDK---GAIRVKGEPV---QFQDTmdalragISMIHQELNL 91
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRkpdQFQKC-------VAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 92 VPHMTVAENI-WLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:cd03234 93 LPGLTVRETLtYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 171 ALTESEVAHLFTIIRDLREQGKAIIYISHK-MDEIFAITDEI 211
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRI 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
258-475 |
1.32e-17 |
|
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: 85.58 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDr 337
Cdd:COG4988 342 VSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD-LSDLDPASWRRQIAWVPQN- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 338 kkSGLFlVLSVMENMSIVNmPEyigksgfvkhmkmAQDcmEQIRRLnIKTPTMDQIIN---------------NLSGGNQ 402
Cdd:COG4988 420 --PYLF-AGTIRENLRLGR-PD-------------ASD--EELEAA-LEAAGLDEFVAalpdgldtplgeggrGLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 403 QKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGMsDRVMVMHEGRIT 475
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQA-DRILVLDDGRIV 550
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-218 |
1.48e-17 |
|
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: 82.00 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpVQFQDTmDALRAGISMIH-QELNLVPHMT 96
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRR-KKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGREpmKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESE 176
Cdd:cd03267 112 VIDSFYLLAA--IYD-LPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490997255 177 VAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:cd03267 189 QENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
258-451 |
1.51e-17 |
|
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: 81.00 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNL--SRKG--YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAieKGMALL 333
Cdd:cd03231 1 LEADELtcERDGraLFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA--RGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEdrkKSGLFLVLSVMENMSivnmpeyigksgFVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLA 413
Cdd:cd03231 79 GH---APGIKTTLSVLENLR------------FWHADHSDEQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLS 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIM 451
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVL 180
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
240-474 |
1.62e-17 |
|
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: 80.67 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 240 RELTQLFPKFNNTIGEEVLTvrnlsrkgyfeEVNFSVRRGEILGVAGLVGAGRSEVMESLFG--MERFDSGEVLIDGQPV 317
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLK-----------NVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 318 IIDSPsvaiekgmalltedRKKSG-------LFLVLSVMENMSivnmpeyigksgFVKHMKmaqdcmeqirrlniktptm 390
Cdd:cd03213 76 DKRSF--------------RKIIGyvpqddiLHPTLTVRETLM------------FAAKLR------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 391 dqiinNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMV----SSelpEILGMSDRV 466
Cdd:cd03213 111 -----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKL 182
|
....*...
gi 490997255 467 MVMHEGRI 474
Cdd:cd03213 183 LLLSQGRV 190
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-176 |
2.00e-17 |
|
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: 81.36 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTmDALRAGISMIHQELNLVPHm 95
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH-KYLHSKVSLVGQEPVLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIWLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADrlVGE----LSIAAQQMVEIAKAVSWNADIVIMDEPTSA 171
Cdd:cd03248 103 SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTE--VGEkgsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
....*.
gi 490997255 172 L-TESE 176
Cdd:cd03248 181 LdAESE 186
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-217 |
2.39e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCL--IGIYRPD---KGAIRVKGEPV--QFQDTMDaL 78
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysPRTDTVD-L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 79 RAGISMIHQELNLVPhMTVAENIWLGREPMkyGFVDHRQLARQTQTLLNKLNI------RLSaDRLVGeLSIAAQQMVEI 152
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLK--GIKDKQVLDEAVEKSLKGASIwdevkdRLH-DSALG-LSGGQQQRVCI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 153 AKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQgKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-199 |
2.39e-17 |
|
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: 84.72 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG-VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTmDALRAGISM 84
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ-DEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQElnlvPHM---TVAENIWLGR-----EPM-----KYGFVDH-RQLARQTQTLLNKLNIRLSAdrlvGELsiaaqQMV 150
Cdd:TIGR02868 414 CAQD----AHLfdtTVRENLRLARpdatdEELwaaleRVGLADWlRALPDGLDTVLGEGGARLSG----GER-----QRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 151 EIAKAVSWNADIVIMDEPTS---ALTESEvahlftIIRDLR--EQGKAIIYISH 199
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEhldAETADE------LLEDLLaaLSGRTVVLITH 528
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
271-474 |
2.88e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.08 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALLTEDRKksgLFLVLSVME 350
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMSIvnmpeyigkSGFVKHMKMAQdcmEQIRRLNIKTPTM----DQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRG 426
Cdd:PRK11614 100 NLAM---------GGFFAERDQFQ---ERIKWVYELFPRLherrIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 427 IDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-217 |
3.70e-17 |
|
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: 85.07 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfQDTMDALRAGISMIHQELNLVPHMT 96
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIwLGREPMKYGFVDHRQLarQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESE 176
Cdd:TIGR01257 1020 VAEHI-LFYAQLKGRSWEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490997255 177 VAHLFTIIRDLReQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:TIGR01257 1097 RRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-213 |
4.46e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.32 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFP---G-------VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQ 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 71 FQD--TMDALRAGISMIHQ----ELNlvPHMTVAENIwlgREPMKYgfvdHRQLAR-----QTQTLLNKLNIRLS-ADRL 138
Cdd:PRK11308 81 KADpeAQKLLRQKIQIVFQnpygSLN--PRKKVGQIL---EEPLLI----NTSLSAaerreKALAMMAKVGLRPEhYDRY 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 139 VGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISV 213
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMV 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
391-490 |
4.47e-17 |
|
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: 80.90 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 391 DQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRG-VAVIMVSSELPEILGMSDRVMVM 469
Cdd:COG1119 137 DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLL 216
|
90 100
....*....|....*....|.
gi 490997255 470 HEGRITGILDKDEADQETILS 490
Cdd:COG1119 217 KDGRVVAAGPKEEVLTSENLS 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
258-474 |
4.96e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.45 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIidspSVAIEK---G 329
Cdd:COG3842 6 LELENVS-KRYgdvtaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPPEKrnvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 330 M-----AL---LT----------------EDRKKSglflvlsVMENMSIVNMPEYIGKSgfvkhmkmaqdcmeqirrlni 385
Cdd:COG3842 81 MvfqdyALfphLTvaenvafglrmrgvpkAEIRAR-------VAELLELVGLEGLADRY--------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 386 ktptmdqiINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAK----AEIYHLISELanrGVAVIMVSSELPEILG 461
Cdd:COG3842 133 --------PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLReemrEELRRLQREL---GITFIYVTHDQEEALA 201
|
250
....*....|...
gi 490997255 462 MSDRVMVMHEGRI 474
Cdd:COG3842 202 LADRIAVMNDGRI 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
258-482 |
5.23e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 80.46 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRK-GYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiEKGMALL 333
Cdd:cd03296 3 IEVRNVSKRfGDFvalDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDRkksGLFLVLSVMENMSIvnmpeyigksGF-VKHMKMAQDCMEQIRRLNIKTPTM------DQIINNLSGGNQQKVL 406
Cdd:cd03296 80 FQHY---ALFRHMTVFDNVAF----------GLrVKPRSERPPEAEIRAKVHELLKLVqldwlaDRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 407 IARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
265-474 |
5.72e-17 |
|
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: 80.62 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 265 RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSV--AIEKGMALLTEDRKKSgl 342
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrAFRRDVQLVFQDSPSA-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 343 flvlsVMENMSIvnmPEYIGKSgfVKHMkMAQDCMEQIRR-------LNIKTPTMDQIINNLSGGNQQKVLIARWLLAQP 415
Cdd:TIGR02769 101 -----VNPRMTV---RQIIGEP--LRHL-TSLDESEQKARiaelldmVGLRSEDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 416 KILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-217 |
7.11e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.93 E-value: 7.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDaLRAGISMIHQEL-NLVPHMTVAE 99
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 NIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAH 179
Cdd:PRK13650 102 DVAFGLENKG---IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 490997255 180 LFTIIRDLREQ-GKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:PRK13650 179 LIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-251 |
7.34e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDkGAIRVKGEpVQF--------QDTMD 76
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGR-VEFfnqniyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 ALRAGISMIHQELNLVPhMTVAENIWLGREPM----KYGFVDHRQLARQTQTLLNKLNIRLSADRLvgELSIAAQQMVEI 152
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDIVESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 153 AKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGK-AIIYISHKMDEIFAITDEISVFRdgtwvgsrqtgefTRQ 231
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFK-------------GNE 228
|
250 260
....*....|....*....|
gi 490997255 232 SLITQMVGRELTQLFpkFNN 251
Cdd:PRK14258 229 NRIGQLVEFGLTKKI--FNS 246
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
257-482 |
8.52e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSR----KGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQ----------PV--IID 320
Cdd:PRK11607 19 LLEIRNLTKsfdgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrPInmMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 321 S----PSVAIEKGMAL-LTEDRKKSGLfLVLSVMENMSIVNMPEYIGKsgfvkhmKMAQdcmeqirrlniktptmdqiin 395
Cdd:PRK11607 99 SyalfPHMTVEQNIAFgLKQDKLPKAE-IASRVNEMLGLVHMQEFAKR-------KPHQ--------------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 396 nLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11607 150 -LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
....*...
gi 490997255 475 TGILDKDE 482
Cdd:PRK11607 229 VQIGEPEE 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
8.74e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQD---TMDA--LRAGISMIHQELNLVPHM 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifQIDAikLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIwlgREPMK-YGFVDHRQLARQTQTLLNKLNI-RLSADRL---VGELSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:PRK14246 106 SIYDNI---AYPLKsHGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490997255 171 ALTESEVAHLFTIIRDLREQgKAIIYISHKMDEIFAITDEISVFRDGTWV 220
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-220 |
9.56e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.00 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKffpGVKaldNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKG---EPVQFQDTMDALRAGI 82
Cdd:PRK10070 35 LEKTGLSL---GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVPHMTVAENIWLGREPMKYGFVDHRQLARQTqtlLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADI 162
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDA---LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 163 VIMDEPTSA---LTESEVAHlfTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWV 220
Cdd:PRK10070 186 LLMDEAFSAldpLIRTEMQD--ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
257-474 |
1.26e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpVIIDSPSvaiekgma 331
Cdd:PRK09452 14 LVELRGIS-KSFdgkevISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ-DITHVPA-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 lltEDR------KKSGLFLVLSVMENMsivnmpeyigksGFvkHMKMAQDCMEQIRRLNIKTPTMDQI-------INNLS 398
Cdd:PRK09452 84 ---ENRhvntvfQSYALFPHMTVFENV------------AF--GLRMQKTPAAEITPRVMEALRMVQLeefaqrkPHQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 399 GGNQQKVLIARWLLAQPKILILDEPTRGID----VGAKAEIYHLISELanrGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-199 |
1.35e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDA-------- 77
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 78 LRAGISMIHQ--ELNLVPHMTVAENIwlGREPMKYGFVDHRQLARQTQTLLNKLNIRLS-ADRLVGELSIAAQQMVEIAK 154
Cdd:PRK11701 87 LRTEWGFVHQhpRDGLRMQVSAGGNI--GERLMAVGARHYGDIRATAGDWLERVEIDAArIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490997255 155 AVSWNADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISH 199
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTH 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-217 |
1.35e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 9 EGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISMIHQ 87
Cdd:PRK13644 5 ENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 88 --ELNLVPHmTVAENIWLGREPMKYGFVDHRQLARQTqtlLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PRK13644 85 npETQFVGR-TVEEDLAFGPENLCLPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAiTDEISVFRDG 217
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
256-474 |
1.43e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 256 EVLTVRNLS----RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMA 331
Cdd:PRK13548 1 AMLEARNLSvrlgGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLtedRKKSGLFLVLSVMEnmsIVNMPEYIGKSGFVKHMKMAQDCMEQI-------RRLniktPTmdqiinnLSGGNQQK 404
Cdd:PRK13548 80 VL---PQHSSLSFPFTVEE---VVAMGRAPHGLSRAEDDALVAAALAQVdlahlagRDY----PQ-------LSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 405 VLIARwLLAQ-------PKILILDEPTRGIDvgakaeIYH------LISELAN-RGVAVIMVSSELPEILGMSDRVMVMH 470
Cdd:PRK13548 143 VQLAR-VLAQlwepdgpPRWLLLDEPTSALD------LAHqhhvlrLARQLAHeRGLAVIVVLHDLNLAARYADRIVLLH 215
|
....
gi 490997255 471 EGRI 474
Cdd:PRK13548 216 QGRL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
272-475 |
1.44e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.98 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViiDSPSVAI-----EKGMALltedrKKSGLFLVL 346
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDErlirqEAGMVF-----QQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 347 SVMENMSIvnmpeyigksGFVKHMKMA-QDCMEQIRRLNIK---TPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDE 422
Cdd:PRK09493 93 TALENVMF----------GPLRVRGASkEEAEKQARELLAKvglAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 423 PTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
258-473 |
1.45e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.21 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFdSGEVLIDGQPVIiDSPSVAIEKGMALLTEdr 337
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLE-AWSAAELARHRAYLSQ-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 338 kksglflvlsvmENMSIVNMP--EYIGKSGFVK-HMKMAQDCMEQI-RRLNI--KTPTMdqiINNLSGGNQQKVLIAR-- 409
Cdd:PRK03695 77 ------------QQTPPFAMPvfQYLTLHQPDKtRTEAVASALNEVaEALGLddKLGRS---VNQLSGGEWQRVRLAAvv 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 410 ---WLLAQP--KILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:PRK03695 142 lqvWPDINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
272-482 |
1.62e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.52 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVI--IDSPSVAIEKGMALLTEDRkksglflVLSVM 349
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmKDDEWRAVRSDIQMIFQDP-------LASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIvnmPEYIGKSGFVKHMKM-AQDCMEQIRRLNIKTPTMDQIIN----NLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:PRK15079 113 PRMTI---GEIIAEPLRTYHPKLsRQEVKDRVKAMMLKVGLLPNLINryphEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 425 RGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-239 |
1.68e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 4 FALEaeGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTmDALRAGIS 83
Cdd:PRK10575 12 FALR--NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS-KAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVPHMTVAENIWLGREPM-----KYGFVDHRQLaRQTQTLlnkLNIRLSADRLVGELSIAAQQMVEIAKAVSW 158
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRYPWhgalgRFGAADREKV-EEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 159 NADIVIMDEPTSALtesEVAH----LFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLI 234
Cdd:PRK10575 165 DSRCLLLDEPTSAL---DIAHqvdvLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
....*
gi 490997255 235 TQMVG 239
Cdd:PRK10575 242 EQIYG 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-204 |
1.83e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFP----------------------GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAI 62
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 63 RVKGEPVqfqdtmdalragiSMIhqELN--LVPHMTvaeniwlGREpmkygfvdhrqlarqtqtllnklNIRLSAdRLVG 140
Cdd:COG1134 84 EVNGRVS-------------ALL--ELGagFHPELT-------GRE-----------------------NIYLNG-RLLG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 141 eLSIA--AQQMVEIAK---------------------------AVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQG 191
Cdd:COG1134 118 -LSRKeiDEKFDEIVEfaelgdfidqpvktyssgmrarlafavATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESG 196
|
250
....*....|...
gi 490997255 192 KAIIYISHKMDEI 204
Cdd:COG1134 197 RTVIFVSHSMGAV 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
270-481 |
1.87e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 78.66 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPsvaiekgmallteDR----KKSGLFLV 345
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-------------DRmvvfQNYSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 346 LSVMENMsivnmpeYIGKSGFVKHMKMAQDcmEQIRRLNIK----TPTMDQIINNLSGGNQQKVLIARWLLAQPKILILD 421
Cdd:TIGR01184 69 LTVRENI-------ALAVDRVLPDLSKSER--RAIVEEHIAlvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 422 EPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEG---RITGILDKD 481
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEVP 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
272-474 |
1.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPviIDSPSVAIEK-----GMALLTEDRKksgLFLVl 346
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP--IDYSRKGLMKlresvGMVFQDPDNQ---LFSA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 347 SVMENMSIVNMpeyigksgfvkHMKMAQD-CMEQIRRLNIKT---PTMDQIINNLSGGNQQKVLIARWLLAQPKILILDE 422
Cdd:PRK13636 99 SVYQDVSFGAV-----------NLKLPEDeVRKRVDNALKRTgieHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 423 PTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
258-474 |
2.36e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 80.19 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRK-GYF---EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPsvAIEKGMALL 333
Cdd:COG1118 3 IEVRNISKRfGSFtllDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP--PRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDrkkSGLFLVLSVMEN----MSIVNMPEyigksgfvkhMKMAQDCMEQIRRLNiktptMDQIIN----NLSGGNQQKV 405
Cdd:COG1118 81 FQH---YALFPHMTVAENiafgLRVRPPSK----------AEIRARVEELLELVQ-----LEGLADrypsQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 406 LIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
270-474 |
2.41e-16 |
|
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: 78.30 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPV-IIDSPSVAIEKGMALltedrkKSGLFLVLSV 348
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVL------QENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRlniktpTMDQIIN----NLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHDFISELPE------GYDTIVGeqgaGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490997255 425 RGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:cd03252 167 SALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
272-474 |
2.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.97 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiekgmalLTEDRKKSGL--------F 343
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS---------LLEVRKTVGIvfqnpddqL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 LVLSVMENMSIVNMpeyigksgfvkHMKMAQDCMEQIRRLNIKTPTMDQIIN----NLSGGNQQKVLIARWLLAQPKILI 419
Cdd:PRK13639 92 FAPTVEEDVAFGPL-----------NLGLSKEEVEKRVKEALKAVGMEGFENkpphHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 420 LDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-172 |
2.94e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISK-FFPG----VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQ---------- 70
Cdd:COG1101 2 LELKNLSKtFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 71 ----FQDTMdalrAGISmihqelnlvPHMTVAENIWL----GRepmKYGF---VDHRQLARqTQTLLNKLNIRLsADRL- 138
Cdd:COG1101 82 igrvFQDPM----MGTA---------PSMTIEENLALayrrGK---RRGLrrgLTKKRREL-FRELLATLGLGL-ENRLd 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 490997255 139 --VGELSIAAQQMVEIAKAVSWNADIVIMDEPTSAL 172
Cdd:COG1101 144 tkVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAAL 179
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
263-474 |
3.85e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.72 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 263 LSRKGyFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpviidspSVAIEKGMALLTEDRKKSGL 342
Cdd:PRK13641 18 MEKKG-LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY-------HITPETGNKNLKKLRKKVSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 343 ---FLVLSVMENMSIVNMpEYIGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILI 419
Cdd:PRK13641 90 vfqFPEAQLFENTVLKDV-EFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 420 LDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
247-473 |
5.02e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 247 PKFNNTIGEEVLTVRNLS--------RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVI 318
Cdd:PRK10261 2 PHSDELDARDVLAVENLNiafmqeqqKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 319 IDSPSVaIEKGMALLTEDRKKSGLFLVLSVMENMSIVN----MPEYIGKSGFVKHMKMAQDCMEQIRRL--NIKTPTMDQ 392
Cdd:PRK10261 82 RRSRQV-IELSEQSAAQMRHVRGADMAMIFQEPMTSLNpvftVGEQIAESIRLHQGASREEAMVEAKRMldQVRIPEAQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 393 II----NNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVM 467
Cdd:PRK10261 161 ILsrypHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVL 240
|
....*.
gi 490997255 468 VMHEGR 473
Cdd:PRK10261 241 VMYQGE 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-251 |
6.85e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkGE---PVQFQDTMDA--LRAGISMIHQ--ELNL 91
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDyaiPANLKKIKEVkrLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 92 VPHmTVAENIWLGrePMKYGfVDHRQLARQTQTLLNKLNI-RLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:PRK13645 104 FQE-TIEKDIAFG--PVNLG-ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 171 ALT---ESEVAHLFtiIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGE-FTRQSLIT--QMVGRELTQ 244
Cdd:PRK13645 180 GLDpkgEEDFINLF--ERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEiFSNQELLTkiEIDPPKLYQ 257
|
....*..
gi 490997255 245 LFPKFNN 251
Cdd:PRK13645 258 LMYKLKN 264
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
272-475 |
8.17e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 76.70 E-value: 8.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPviidspsvaiekgMALLTED------RKKSG---- 341
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD-------------LFALDEDararlrARHVGfvfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 342 ---LFLVLSVMENmsiVNMP-EYIGKSGfvkHMKMAQDCMEQI---RRLNiKTPtmdqiiNNLSGGNQQKVLIARWLLAQ 414
Cdd:COG4181 98 sfqLLPTLTALEN---VMLPlELAGRRD---ARARARALLERVglgHRLD-HYP------AQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 415 PKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSElPEILGMSDRVMVMHEGRIT 475
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHD-PALAARCDRVLRLRAGRLV 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
269-475 |
8.43e-16 |
|
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: 79.81 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDrkkSGLFLVlSV 348
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD-LRDLDEDDLRRRIAVVPQR---PHLFDT-TL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MENMSIVNmPEyigksgfvkhmkmAQDcmEQIR------RLniktptmDQIIN---------------NLSGGNQQKVLI 407
Cdd:COG4987 426 RENLRLAR-PD-------------ATD--EELWaalervGL-------GDWLAalpdgldtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 408 ARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEiLGMSDRVMVMHEGRIT 475
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAG-LERMDRILVLEDGRIV 548
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
254-474 |
1.02e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNLSR-------KGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGM-ERFDS-----GEVLIDGQPVI-I 319
Cdd:PRK14246 4 GKSAEDVFNISRlylyindKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFqI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 320 DSPSVAIEKGMALltedrKKSGLFLVLSVMENMSivnmpeYIGKSGFVKHMKMAQDCMEQ-IRRLNIKTPTMDQI---IN 395
Cdd:PRK14246 84 DAIKLRKEVGMVF-----QQPNPFPHLSIYDNIA------YPLKSHGIKEKREIKKIVEEcLRKVGLWKEVYDRLnspAS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 396 NLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRgVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-217 |
1.10e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.66 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMD-ALRagISMI 85
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElAKR--LAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKYGFV---DHRQLARQtqtlLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADI 162
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLtaeDREIIDEA----IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 163 VIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHkmDEIFAIT--DEISVFRDG 217
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH--DINFASCyaDHIVAMKDG 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-217 |
1.14e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepVQFQD-TMDALRAGI 82
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDLRDyTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVpHMTVAENIWLGREPmKYGFVDHRQLARQTQTL--LNKLNIRLsaDRLVGE----LSIAAQQMVEIAKAV 156
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYARTE-QYSREQIEEAARMAYAMdfINKMDNGL--DTVIGEngvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 157 SWNADIVIMDEPTSAL-TESEVAhlftIIRDLRE--QGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:PRK11176 496 LRDSPILILDEATSALdTESERA----IQAALDElqKNRTSLVIAHRLSTI-EKADEILVVEDG 554
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
272-476 |
1.20e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.07 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPV--IIDSPSVAIEKGMALLTEDRKksgLFLVLSVM 349
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrLKNREVPFLRRQIGMIFQDHH---LLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENmsiVNMPEYI-GKSGfvkhmkmaqdcmEQIRR-----LNiKTPTMDQIIN---NLSGGNQQKVLIARWLLAQPKILIL 420
Cdd:PRK10908 98 DN---VAIPLIIaGASG------------DDIRRrvsaaLD-KVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 421 DEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITG 476
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-429 |
1.24e-15 |
|
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: 79.21 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 10 GISKFFPGVKA-LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkgepvqfqdtMDALRAGisMIHQE 88
Cdd:TIGR03719 9 RVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP----------QPGIKVG--YLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 89 LNLVPHMTVAENIWLGREP------------MKYGFVD---HRQLARQTQ-----------TLLNKLNIRLSADRL---- 138
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAEikdaldrfneisAKYAEPDadfDKLAAEQAElqeiidaadawDLDSQLEIAMDALRCppwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 139 --VGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLftiIRDLREQGKAIIYISH----------------- 199
Cdd:TIGR03719 157 adVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL---ERHLQEYPGTVVAVTHdryfldnvagwileldr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 200 ---------------KMDEIFAITDEISVFRDGT------WVGS----RQTGEFTRQSLITQMVGREltqlFPKFNNT-- 252
Cdd:TIGR03719 234 grgipwegnysswleQKQKRLEQEEKEESARQKTlkreleWVRQspkgRQAKSKARLARYEELLSQE----FQKRNETae 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 253 --------IGEEVLTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIdGQPVII 319
Cdd:TIGR03719 310 iyippgprLGDKVIEAENLT-KAFgdkllIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 320 DSPsvaiekgmallteDRKKSGLFLVLSVMENMS-----------IVNMPEYIGksgfvkhmkmaqdcmeqirRLNIKTP 388
Cdd:TIGR03719 388 AYV-------------DQSRDALDPNKTVWEEISggldiiklgkrEIPSRAYVG-------------------RFNFKGS 435
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 490997255 389 TMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:TIGR03719 436 DQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-220 |
1.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 76.74 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQdTMDA----LRAGISMIHQelnlVPH 94
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK-TKDKyirpVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 95 MTVAENIwLGREpMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELS---IAAQQMVEIA--KAVSWNADIVIMDEPT 169
Cdd:PRK13646 96 SQLFEDT-VERE-IIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAivSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 170 SALTESEVAHLFTIIRDLR-EQGKAIIYISHKMDEIFAITDEISVFRDGTWV 220
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
266-473 |
1.65e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 266 KGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidsPSVA--IEKGMALLTE-DRkksgL 342
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARArlARARIGVVPQfDN----L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 343 FLVLSVMENMSIVNmpEYIGKSgfVKHMKMAQDCMEQIRRLNIKTptmDQIINNLSGGNQQKVLIARWLLAQPKILILDE 422
Cdd:PRK13536 126 DLEFTVRENLLVFG--RYFGMS--TREIEAVIPSLLEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 423 PTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
254-482 |
1.84e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.46 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNLS-----RKGYF----------EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVi 318
Cdd:COG4608 4 AEPLLEVRDLKkhfpvRGGLFgrtvgvvkavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 319 idspSVAIEKGMALLtedRKKsglflvlsvmenMSIV--------N--MPeyIGKS---GFVKH-MKMAQDCMEQIRRLn 384
Cdd:COG4608 83 ----TGLSGRELRPL---RRR------------MQMVfqdpyaslNprMT--VGDIiaePLRIHgLASKAERRERVAEL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 385 iktptMDQI------INN----LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVS 453
Cdd:COG4608 141 -----LELVglrpehADRypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFIS 215
|
250 260
....*....|....*....|....*....
gi 490997255 454 SELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:COG4608 216 HDLSVVRHISDRVAVMYLGKIVEIAPRDE 244
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
258-453 |
1.89e-15 |
|
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: 74.70 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNL--SRKG--YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAieKGMALL 333
Cdd:TIGR01189 1 LAARNLacSRGErmLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPH--ENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEdrkKSGLFLVLSVMENMSIVNmpeYIGKSgfvkHMKMAQDCMEQIRRLNIKtptmDQIINNLSGGNQQKVLIARWLLA 413
Cdd:TIGR01189 79 GH---LPGLKPELSALENLHFWA---AIHGG----AQRTIEDALAAVGLTGFE----DLPAAQLSAGQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVS 453
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTT 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
271-471 |
1.92e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALLTEDRkksglFLVLsvme 350
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNR-----FLRL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 nmsivnmpeyigKSGFVKhmkmaQDCMEQIRRLNiKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVG 430
Cdd:PRK09544 93 ------------RPGTKK-----EDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 431 AKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHE 471
Cdd:PRK09544 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-218 |
2.22e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDaLRAGISMIHQEL-NLVPHMTVA 98
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK-LRKHIGIVFQNPdNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVA 178
Cdd:PRK13648 103 YDVAFGLENHA---VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490997255 179 HLFTIIRDLREQGK-AIIYISHKMDEIFAiTDEISVFRDGT 218
Cdd:PRK13648 180 NLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGT 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
272-493 |
2.53e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.21 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPviidspsvaiekgmalLTED-----RKKSGL---- 342
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV----------------LSEEtvwdvRRQVGMvfqn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 343 ----FLVLSVMENmsIVNMPEYIGksgfVKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKIL 418
Cdd:PRK13635 90 pdnqFVGATVQDD--VAFGLENIG----VPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 419 ILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILgMSDRVMVMHEGRITgildkDEADQETILSLAS 493
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAA-QADRVIVMNKGEIL-----EEGTPEEIFKSGH 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
258-479 |
2.54e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS----RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDsGEVLIDGQPVI----IDSPSVAIEKG 329
Cdd:PRK14258 8 IKVNNLSfyydTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFfnqnIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 330 MALLTEDRKKSGLFlVLSVMENMS----IVNMPEYIGKSGFVKHMKMAQDCMEQIRRlNIKTPTMDqiinnLSGGNQQKV 405
Cdd:PRK14258 87 RRQVSMVHPKPNLF-PMSVYDNVAygvkIVGWRPKLEIDDIVESALKDADLWDEIKH-KIHKSALD-----LSGGQQQRL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 406 LIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRG-VAVIMVSSELPEILGMSDRVMVMH--EGRITGILD 479
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKgnENRIGQLVE 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
255-473 |
2.99e-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: 74.78 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLSrKGY------------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDsp 322
Cdd:COG4778 2 TTLLEVENLS-KTFtlhlqggkrlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 323 svaiekgMALLTEDR----KKSGLFLV---LSVMENMS---IVNMPeyigksgfVKHMKMAQDCMEQ-----IRRLNIKT 387
Cdd:COG4778 79 -------LAQASPREilalRRRTIGYVsqfLRVIPRVSaldVVAEP--------LLERGVDREEARArarelLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 388 PTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVM 467
Cdd:COG4778 144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVV 223
|
....*.
gi 490997255 468 VMHEGR 473
Cdd:COG4778 224 DVTPFS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-199 |
3.14e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMD-----ALRA-GISMIHQELNLVPH 94
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLH---QMDeearaKLRAkHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 95 MTVAENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSAL-- 172
Cdd:PRK10584 103 LNALENVEL---PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLdr 179
|
170 180
....*....|....*....|....*....
gi 490997255 173 -TESEVAH-LFTIIRDlreQGKAIIYISH 199
Cdd:PRK10584 180 qTGDKIADlLFSLNRE---HGTTLILVTH 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
270-474 |
3.70e-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: 74.21 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiEKGMALLTEDrkkSGLFLVLSVM 349
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMVFQN---YALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSivnmpeyigksgF-VKHMKMAQDCMEQIRRLNIKTPTMDQIINN----LSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:cd03301 91 DNIA------------FgLKLRKVPKDEIDERVREVAELLQIEHLLDRkpkqLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 425 RGID----VGAKAEIYHLISELanrGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:cd03301 159 SNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-233 |
4.00e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdtmDALRAG-ISMIHQ--ELNLVP 93
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNlVAYVPQseEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 94 HMTVAENIWLGRepmkYGFVD--HRQLARQTQTL---LNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEP 168
Cdd:PRK15056 94 PVLVEDVVMMGR----YGHMGwlRRAKKRDRQIVtaaLARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 169 TSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDeISVFRDGTWVGSRQT-GEFTRQSL 233
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTeTTFTAENL 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
269-477 |
4.07e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 77.90 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMeSLfgMERF---DSGEVLIDGQPViidsPSVAIE---KGMALLTEDrkkSGL 342
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLV-NL--LLRFydpTSGRILIDGVDI----RDLTLEslrRQIGVVPQD---TFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 343 FlVLSVMENMSIvnmpeyiGKSGF----VKH-MKMAQdCMEQIRRLNIKtptMDQII----NNLSGGNQQKVLIARWLLA 413
Cdd:COG1132 426 F-SGTIRENIRY-------GRPDAtdeeVEEaAKAAQ-AHEFIEALPDG---YDTVVgergVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGMsDRVMVMHEGRITGI 477
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQ 555
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
270-482 |
4.08e-15 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 75.03 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEdrkKSGLFLVLSVM 349
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED-IREQDPVELRRKIGYVIQ---QIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIVnmPEYIGksgfVKHMKMAQDCMEQIRRLNIKTPT-MDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGID 428
Cdd:cd03295 94 ENIALV--PKLLK----WPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 429 VGAKA----EIYHLISELanrGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:cd03295 168 PITRDqlqeEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-201 |
4.12e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.85 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPV-QFQDTMDA-LR-AGISMIHQELNLVPHMTV 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAeLRnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 98 AENIWLgrePMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEV 177
Cdd:PRK11629 105 LENVAM---PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|....*
gi 490997255 178 AHLFTIIRDL-REQGKAIIYISHKM 201
Cdd:PRK11629 182 DSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
271-474 |
4.33e-15 |
|
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: 74.57 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDrkkSGLFlVLSVME 350
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID-IRDISRKSLRSMIGVVLQD---TFLF-SGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMSIVNmpEYIGKSGFVKHMKMAQdCMEQIRRLnikTPTMDQIIN----NLSGGNQQKVLIARWLLAQPKILILDEPTRG 426
Cdd:cd03254 96 NIRLGR--PNATDEEVIEAAKEAG-AHDFIMKL---PNGYDTVLGenggNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 427 IDVGAKAEIYHLISELaNRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:cd03254 170 IDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-242 |
5.96e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.45 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQElNLVPHMTVAEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQD-PVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 101 IWLGR---EPMKYGFVDHRQLARQTQTLLNKLNIRLsadrlvGE----LSIAAQQMVEIAKAVSWNADIVIMDEPTSAL- 172
Cdd:PRK10790 435 VTLGRdisEEQVWQALETVQLAELARSLPDGLYTPL------GEqgnnLSVGQKQLLALARVLVQTPQILILDEATANId 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 173 --TESEVAHLFTIIRdlreQGKAIIYISHKMDEIFAiTDEISVFRDGTWV--GSRQT-----GEFTrQSLITQMVGREL 242
Cdd:PRK10790 509 sgTEQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVeqGTHQQllaaqGRYW-QMYQLQLAGEEL 581
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
257-473 |
6.06e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLsRKGYFEEV-----NFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMA 331
Cdd:PRK13537 7 PIDFRNV-EKRYGDKLvvdglSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 L----LTEDrkksglflvLSVMENMSIVNmpEYIGKSgfvkhmkmAQDCMEQI------RRLNIKTptmDQIINNLSGGN 401
Cdd:PRK13537 86 PqfdnLDPD---------FTVRENLLVFG--RYFGLS--------AAAARALVppllefAKLENKA---DAKVGELSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 402 QQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
7.44e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.88 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQF-QDTMDAL 78
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 79 RAGISMIHQEL-NLVPHMTVAENIWLGrePMKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:PRK13636 81 RESVGMVFQDPdNQLFSASVYQDVSFG--AVNLK-LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 158 WNADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWV 220
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
270-476 |
9.75e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.45 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsvaiekgmalLTEDRKKSGLFL----- 344
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN-----------IREVRKFVGLVFqnpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 345 -VLSVMENMSIVNMPEYIGksgfVKHMKMAQDCMEQIRRLNIKTpTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEP 423
Cdd:PRK13652 90 qIFSPTVEQDIAFGPINLG----LDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 424 TRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRITG 476
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
272-474 |
1.06e-14 |
|
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: 73.42 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFgmeRF---DSGEVLIDGQPV-IIDSPSVaiekgmalltedRKKSGLFLVLS 347
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLF---RFydvSSGSILIDGQDIrEVTLDSL------------RRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 VMENMSIVNMPEYiGKSGfvkhmkmAQDcmEQIRRLNIKTPTMDQIIN--------------NLSGGNQQKVLIARWLLA 413
Cdd:cd03253 85 VLFNDTIGYNIRY-GRPD-------ATD--EEVIEAAKAAQIHDKIMRfpdgydtivgerglKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
258-474 |
1.11e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.11 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiEKGMAL 332
Cdd:COG3839 4 LELENVS-KSYggveaLKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEDrkkSGLFLVLSVMENMsivnmpeyigksGF-VKHMKMAQDcmeQIRR--------LNIkTPTMDQIINNLSGGNQQ 403
Cdd:COG3839 80 VFQS---YALYPHMTVYENI------------AFpLKLRKVPKA---EIDRrvreaaelLGL-EDLLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 404 KVLIARWLLAQPKILILDEPTRGIDvgAK------AEIYHLISELanrGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLD--AKlrvemrAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-217 |
1.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.45 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKFFPGVK--ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPD---KGAIRVKGEPVQfQDTM 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLT-AKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 76 DALRAGISMIHQEL-NLVPHMTVAENIWLGREpmkygfvdHRQLARQ-----TQTLLNKLNIRLSADRLVGELSIAAQQM 149
Cdd:PRK13640 80 WDIREKVGIVFQNPdNQFVGATVGDDVAFGLE--------NRAVPRPemikiVRDVLADVGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 150 VEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDG 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
270-474 |
1.49e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspsvaiekgMALLTEDRKKSGLFLVLSVM 349
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL------------AKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIVNMPEYIGKS--GFVKHMkMAQDCMEQIRRL-------NIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILIL 420
Cdd:PRK10419 97 DSISAVNPRKTVREIirEPLRHL-LSLDKAERLARAsemlravDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 421 DEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-224 |
1.51e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqdTMDALRAGISMIHQELNLVPHM--- 95
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI----TSTSKNKDIKQIRKKVGLVFQFpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 -----TVAENIWLGrePMKYGF--VDHRQLARQtqtllnKLNIRLSADRLVG----ELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:PRK13649 97 qlfeeTVLKDVAFG--PQNFGVsqEEAEALARE------KLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQ 224
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
255-474 |
1.69e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLS-----RKGYF--------EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPV---- 317
Cdd:PRK15112 2 ETLLEVRNLSktfryRTGWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 318 ----------IIDSPSVAIEKgmalltedRKKSGLFLVLSVMENMSIvnmpeyigksgfvKHMKMAQDCMEQIRRLNIKT 387
Cdd:PRK15112 82 ysyrsqrirmIFQDPSTSLNP--------RQRISQILDFPLRLNTDL-------------EPEQREKQIIETLRQVGLLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 388 PTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRV 466
Cdd:PRK15112 141 DHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQV 220
|
....*...
gi 490997255 467 MVMHEGRI 474
Cdd:PRK15112 221 LVMHQGEV 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-220 |
1.75e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 3 AFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCL------IGIYRPdKGAIRVKGEPV-QFQDTM 75
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRY-SGDVLLGGRSIfNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 76 DaLRAGISMIHQELNLVPhMTVAENIWLGREPMKygFVDHRQLARQTQTLLNKLNIRLSA-DRLVG---ELSIAAQQMVE 151
Cdd:PRK14271 98 E-FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLWDAVkDRLSDspfRLSGGQQQLLC 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 152 IAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIyISHKMDEIFAITDEISVFRDGTWV 220
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVII-VTHNLAQAARISDRAALFFDGRLV 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-218 |
1.95e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.54 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpvqfqDTMDAlRAGISMIHQELNLV---PHM 95
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGV-----DITDK-KVKLSDIRKKVGLVfqyPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 -----TVAENIWLGrePMKYGFVDHRQLARQTQTL-LNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPT 169
Cdd:PRK13637 95 qlfeeTIEKDIAFG--PINLGLSEEEIENRVKRAMnIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490997255 170 SALTESEVAHLFTIIRDLREQGK-AIIYISHKMDEIFAITDEISVFRDGT 218
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
269-467 |
2.02e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.50 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDG---------QPVIIDSPSVAIEKGMALLTEDRKk 339
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqRSEVPDSLPLTVRDLVAMGRWARR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 340 sGLFLVLSVMENMSIVNMPEYIGKSGFVKhmkmaqdcmeqiRRLNiktptmdqiinNLSGGNQQKVLIARWLLAQPKILI 419
Cdd:NF040873 87 -GLWRRLTRDDRAAVDDALERVGLADLAG------------RQLG-----------ELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 420 LDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVM 467
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-209 |
2.56e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 22 DNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGE--PVQFQDTMDALRAGISMIHQELNLVPHMTVAE 99
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 NI-WLGREpmkygfvdHRQLARQT--QTLLNKLN---IRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALT 173
Cdd:PRK11831 104 NVaYPLRE--------HTQLPAPLlhSTVMMKLEavgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 490997255 174 ESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITD 209
Cdd:PRK11831 176 PITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIAD 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
271-491 |
2.76e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsvaiekgmalLTEDRKKSGLflVLSVME 350
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-----------FEKLRKHIGI--VFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NM---SIVNMPEYIGKSGF-VKHMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRG 426
Cdd:PRK13648 94 NQfvgSIVKYDVAFGLENHaVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 427 IDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGmSDRVMVMHEGRI------TGILDKDEADQETILSL 491
Cdd:PRK13648 173 LDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVykegtpTEIFDHAEELTRIGLDL 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
273-493 |
3.16e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 273 NFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPS---VAIekgmaLLTEDrkksGLFLVLSVM 349
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpVSM-----LFQEN----NLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIvnmpeyiGKSGFVKHMKMAQDCMEQI-RRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGID 428
Cdd:PRK10771 90 QNIGL-------GLNPGLKLNAAQREKLHAIaRQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 429 VGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI-----TGILDKDEADQETILSLAS 493
Cdd:PRK10771 162 PALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIawdgpTDELLSGKASASALLGIKS 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-244 |
3.50e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.51 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKC------LIGIYRPDkGAIRVKGEPVQFQDtMD--A 77
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGKNLYAPD-VDpvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 78 LRAGISMIHQELNLVPHmTVAENIWLGREPMKY-GFVDH---RQLaRQTqTLLNKLNIRLSADRLvgELSIAAQQMVEIA 153
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYkGDMDElveRSL-RQA-ALWDEVKDKLKQSGL--SLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 154 KAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQgKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTG---EFTR 230
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGylvEFDR 242
|
250
....*....|....
gi 490997255 231 QSLITQMVGRELTQ 244
Cdd:PRK14243 243 TEKIFNSPQQQATR 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-217 |
3.68e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.00 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVK-ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGIS 83
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 84 MIHQELNLVpHMTVAENIWLGREPMKYgfVDHRQLARQTQTLLNKLNIRLSADRLVGE----LSIAAQQMVEIAKAVSWN 159
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDNIRVGRPDATD--EEMRAAAERAQAHDFIERKPDGYDTVVGErgrqLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 160 ADIVIMDEPTSAL---TESEVAHLFTIIRdlreQGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:PRK13657 490 PPILILDEATSALdveTEAKVKAALDELM----KGRTTFIIAHRLSTV-RNADRILVFDNG 545
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-199 |
3.86e-14 |
|
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: 70.98 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmdalragiSMI 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR---------DSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPMKYGFVDHRQlaRQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03231 72 ARGLLYLGHAPGIKTTLSVLENLRFWHADHSD--EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISH 199
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
271-475 |
3.91e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALLTEDRKKSGLFLVLSVME 350
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NmsiVNMPEYIGKSGFVKHMKMAQDCMEQI---RRLNIKTptmdqiiNNLSGGNQQKVLIARWLLAQPKILILDEPTRGI 427
Cdd:PRK11629 107 N---VAMPLLIGKKKPAEINSRALEMLAAVgleHRANHRP-------SELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 428 DVGAKAEIYHLISELANR-GVAVIMVSSELpEILGMSDRVMVMHEGRIT 475
Cdd:PRK11629 177 DARNADSIFQLLGELNRLqGTAFLVVTHDL-QLAKRMSRQLEMRDGRLT 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-213 |
4.27e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.40 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDkgaIRVKGEPVQFQDtMDALR-----------AGISMIH 86
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN---WHVTADRFRWNG-IDLLKlsprerrkiigREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QELN--LVPHMTV----AENI--------WLGRepmkygfvdHRQLARQTQTLLNKLNIRLSADRLVG---ELSIAAQQM 149
Cdd:COG4170 96 QEPSscLDPSAKIgdqlIEAIpswtfkgkWWQR---------FKWRKKRAIELLHRVGIKDHKDIMNSyphELTEGECQK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 150 VEIAKAVSWNADIVIMDEPTSAL---TESEVAHLFTIIRDLreQGKAIIYISHKMDEIFAITDEISV 213
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMestTQAQIFRLLARLNQL--QGTSILLISHDLESISQWADTITV 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
272-474 |
5.32e-14 |
|
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: 70.90 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDRkksgLFLVLSVMEN 351
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID-ISTIPLEDLRSSLTIIPQDP----TLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 MSIVNMpeyigksgfvkhmkmaQDCMEQIRRLNIKTPTmdqiiNNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGA 431
Cdd:cd03369 102 LDPFDE----------------YSDEEIYGALRVSEGG-----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490997255 432 KAEIYHLISELANrGVAVIMVSSELPEILGMsDRVMVMHEGRI 474
Cdd:cd03369 161 DALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-204 |
5.33e-14 |
|
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: 71.02 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqdTMDALRAGISmihqelnlvPHMTV 97
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----SLLGLGGGFN---------PELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 98 AENIWLgrepmkygfvDHRQLARQTQTLLNKLN--IRLSA-----DRLVGELSiaAQQMVEIAKAVS--WNADIVIMDEP 168
Cdd:cd03220 102 RENIYL----------NGRLLGLSRKEIDEKIDeiIEFSElgdfiDLPVKTYS--SGMKARLAFAIAtaLEPDILLIDEV 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 490997255 169 TSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEI 204
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSI 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
265-474 |
5.62e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 265 RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLF-----GMERfdSGEVLIDGQPviIDSPSvaIEKGMALLTEDRKK 339
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKG--SGSVLLNGMP--IDAKE--MRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 340 SGLFLVLSVMENMSIVNMPEYIGKSgfvKHMKMAQDCMEQIRRLN-----IKTPTMdqiINNLSGGNQQKVLIARWLLAQ 414
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLRMPRRVTKK---EKRERVDEVLQALGLRKcantrIGVPGR---VKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 415 PKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMV----SSELPEILgmsDRVMVMHEGRI 474
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGRV 245
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
270-474 |
5.73e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSpsvaiekgmallTEDRKKSGLFLVLSVM 349
Cdd:PRK11432 23 DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------------IQQRDICMVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIVNMPEY------IGKSGFVKHMKMAqdcMEQIRRLNIKTPTMDQIinnlSGGNQQKVLIARWLLAQPKILILDEP 423
Cdd:PRK11432 91 PHMSLGENVGYglkmlgVPKEERKQRVKEA---LELVDLAGFEDRYVDQI----SGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 424 TRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
272-474 |
6.22e-14 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 70.99 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDRkksglflVL---SV 348
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVD-ISKIGLHDLRSRISIIPQDP-------VLfsgTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MENMSIVNM--PEYIGKSgfVKHMKMAQDCMEQIRRLNIKTPTMDqiiNNLSGGNQQKVLIARWLLAQPKILILDEPTRG 426
Cdd:cd03244 95 RSNLDPFGEysDEELWQA--LERVGLKEFVESLPGGLDTVVEEGG---ENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 427 IDVGAKAEIYHLI-SELANRgvAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:cd03244 170 VDPETDALIQKTIrEAFKDC--TVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-204 |
6.60e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPG--VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTmDALRAGI 82
Cdd:PRK11160 338 SLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVPHmTVAENIWLGREPMKygfvDHRQLARQTQTLLNKLnirLSAD-RL---VGE----LSIAAQQMVEIAK 154
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAPNAS----DEALIEVLQQVGLEKL---LEDDkGLnawLGEggrqLSGGEQRRLGIAR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 155 AVSWNADIVIMDEPTSAL---TESEVAHLftiirdLRE--QGKAIIYISH------KMDEI 204
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLdaeTERQILEL------LAEhaQNKTVLMITHrltgleQFDRI 543
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-239 |
6.64e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 22 DNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAgISMIHQELNLVPHMTVAENI 101
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 102 WLGREPMKYGFVDHRQLARQTQT-LLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHL 180
Cdd:PRK10253 103 ARGRYPHQPLFTRWRKEDEEAVTkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 181 FTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLITQMVG 239
Cdd:PRK10253 183 LELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-217 |
7.04e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.25 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGI--YRPDKGAIRVKGEPVQFQDTMDALRAGISMIHQ---ElnlVPHM 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAFQypvE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TV------AENIWLGREPMKYGFvdhRQLARQtqtLLNKLNIRLS-ADRLVGE-LSIAAQQMVEIAKAVSWNADIVIMDE 167
Cdd:COG0396 93 SVsnflrtALNARRGEELSAREF---LKLLKE---KMKELGLDEDfLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 168 PTSALtesEVAHLFTI---IRDLREQGKAIIYISHK---MDEIFAitDEISVFRDG 217
Cdd:COG0396 167 TDSGL---DIDALRIVaegVNKLRSPDRGILIITHYqriLDYIKP--DFVHVLVDG 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
251-474 |
9.21e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 251 NTIGEEVLTVRNLS-RKG---YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQ--PVIIDSPSV 324
Cdd:PRK11831 1 EQSVANLVDMRGVSfTRGnrcIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 325 AIEKGMALLTEdrkkSG-LFLVLSVMENMSI-----VNMPEYIGKSGFVkhMKMAQDCMEQIRRLniktptmdqIINNLS 398
Cdd:PRK11831 81 TVRKRMSMLFQ----SGaLFTDMNVFDNVAYplrehTQLPAPLLHSTVM--MKLEAVGLRGAAKL---------MPSELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 399 GGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11831 146 GGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-233 |
9.78e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVK-----------ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRpDKGAIRVKGEPVQFQD- 73
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 74 -TMDALRAGISMIHQELN--LVPHMTVAENIWLGREpmkygfVDHRQL---ARQTQTLLNKLNIRLSAD---RLVGELSI 144
Cdd:PRK15134 355 rQLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGLR------VHQPTLsaaQREQQVIAVMEEVGLDPEtrhRYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 145 AAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGK-AIIYISHKMDEIFAITDEISVFRDGTWV--G 221
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVeqG 508
|
250
....*....|....*...
gi 490997255 222 SRQT------GEFTRQSL 233
Cdd:PRK15134 509 DCERvfaapqQEYTRQLL 526
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-474 |
9.80e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALRAGISM 84
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 IHQEL--NLVPHMTVAENI-WLGRepmKYGFvDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNAD 161
Cdd:NF033858 81 MPQGLgkNLYPTLSVFENLdFFGR---LFGQ-DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 162 IVIMDEPTSAlteseV-----AHLFTIIRDLREQ--GKAIIYISHKMDE------IFAItDEISVFRDGtwvgsrqtgef 228
Cdd:NF033858 157 LLILDEPTTG-----VdplsrRQFWELIDRIRAErpGMSVLVATAYMEEaerfdwLVAM-DAGRVLATG----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 229 TRQSLITQMVGRELTQLF------------------PKFNNTIGEEVLTVRNLSRK-GYF---EEVNFSVRRGEILGVAG 286
Cdd:NF033858 220 TPAELLARTGADTLEAAFiallpeekrrghqpvvipPRPADDDDEPAIEARGLTMRfGDFtavDHVSFRIRRGEIFGFLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 287 LVGAGRSEVMESLFGMERFDSGEVLIDGQPViiDSpsvaieKGMALltedRKKSG-------LFLVLSVMENMS----IV 355
Cdd:NF033858 300 SNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DA------GDIAT----RRRVGymsqafsLYGELTVRQNLElharLF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 356 NMPEyigksgfvkhMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEI 435
Cdd:NF033858 368 HLPA----------AEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 490997255 436 YHLISELA-NRGVAvIMVSSELpeilgMS-----DRVMVMHEGRI 474
Cdd:NF033858 437 WRLLIELSrEDGVT-IFISTHF-----MNeaercDRISLMHAGRV 475
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
270-474 |
1.01e-13 |
|
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: 70.72 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLfgmERF---DSGEVLIDGQPVI-IDSPSvaIEKGMALLTEDrkksgLFLV 345
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLI---PRFydvDSGRILIDGHDVRdYTLAS--LRRQIGLVSQD-----VFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 346 L-SVMENMSIvnmpeyiGKSGF----VKHMKMAQDCMEQIRRLniktPT-MDQIIN----NLSGGNQQKVLIARWLLAQP 415
Cdd:cd03251 89 NdTVAENIAY-------GRPGAtreeVEEAARAANAHEFIMEL----PEgYDTVIGergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 416 KILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVImvSSELPEILGmSDRVMVMHEGRI 474
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLmKNRTTFVI--AHRLSTIEN-ADRIVVLEDGKI 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
1.04e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpVQFQDTMdALRAGISMIH-QELNLVPHMT 96
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VPFKRRK-EFARRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGREpmKYGfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIaAQQM-VEIAKAVSWNADIVIMDEPTSAL-TE 174
Cdd:COG4586 113 AIDSFRLLKA--IYR-IPDAEYKKRLDELVELLDLGELLDTPVRQLSL-GQRMrCELAAALLHRPKILFLDEPTIGLdVV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 175 SEVAhlftiIRDL-----REQGKAIIYISHKMDEIFAITDEI 211
Cdd:COG4586 189 SKEA-----IREFlkeynRERGTTILLTSHDMDDIEALCDRV 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
258-485 |
1.18e-13 |
|
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: 69.48 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS----RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERF--DSGEVLIDGQPVIidspsvaiekgmA 331
Cdd:cd03217 1 LEIKDLHvsvgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDIT------------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEDRKKSGLFlvlsvmenMSIVNMPEYIGksgfVKHMKMaqdcmeqIRRLNIktptmdqiinNLSGGNQQKVLIARWL 411
Cdd:cd03217 69 LPPEERARLGIF--------LAFQYPPEIPG----VKNADF-------LRYVNE----------GFSGGEKKRNEILQLL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVsSELPEILGM--SDRVMVMHEGRITGILDKDEADQ 485
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDYikPDRVHVLYDGRIVKSGDKELALE 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
271-475 |
1.86e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEkgmalltEDRKKSGL---FLVLS 347
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIK-------QIRKKVGLvfqFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 VMENMSIVNM---PEYIGksgfVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:PRK13649 98 LFEETVLKDVafgPQNFG----VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 425 RGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
269-490 |
1.89e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.40 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALLTEDRKKSglFLVLSV 348
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQ--FVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MENMSI--VNM---PEYIGKsgfVKHMKMAQDCMEQIRRLNIKTptmdqiinnLSGGNQQKVLIARWLLAQPKILILDEP 423
Cdd:PRK13644 96 EEDLAFgpENLclpPIEIRK---RVDRALAEIGLEKYRHRSPKT---------LSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 424 TRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEiLGMSDRVMVMHEGRItgildKDEADQETILS 490
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI-----VLEGEPENVLS 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-172 |
2.34e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.05 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPD---KGAIRVKGEPVqfqDTMDALRAGISMIHQELNLVPHMTV 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL---TALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 98 AENIWLGRePMKYGFVDHRQLARQTqtlLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSAL 172
Cdd:COG4136 94 GENLAFAL-PPTIGRAQRRARVEQA---LEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-218 |
2.44e-13 |
|
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: 68.65 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 12 SKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepvqfqdtmdalraGISMIHQE--- 88
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEpwi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 89 LNlvphMTVAENIWLGRE--PMKYGFV--------DHRQLARQTQTllnklnirlsadrLVGE----LSIAAQQMVEIAK 154
Cdd:cd03250 78 QN----GTIRENILFGKPfdEERYEKVikacalepDLEILPDGDLT-------------EIGEkginLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 155 AVSWNADIVIMDEPTSALtESEVA-HLFT-IIRDLREQGKAIIYISHKMdEIFAITDEISVFRDGT 218
Cdd:cd03250 141 AVYSDADIYLLDDPLSAV-DAHVGrHIFEnCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
272-474 |
3.10e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.88 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSevmeSLF----GMERFDSGEVLIDGQPViidspsvaiekgMAL----LTEDRKKSGL- 342
Cdd:COG1135 24 VSLTIEKGEIFGIIGYSGAGKS----TLIrcinLLERPTSGSVLVDGVDL------------TALsereLRAARRKIGMi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 343 ---FLVLS---VMENmsiVNMP-EYIGKSGfvkhmkmaqdcmEQIRR----------LNIKtptMDQIINNLSGGNQQKV 405
Cdd:COG1135 88 fqhFNLLSsrtVAEN---VALPlEIAGVPK------------AEIRKrvaellelvgLSDK---ADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 406 LIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELaNR--GVAVIMVSSElpeilgMS------DRVMVMHEGRI 474
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDI-NRelGLTIVLITHE------MDvvrricDRVAVLENGRI 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-217 |
3.69e-13 |
|
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: 71.77 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepvqfQD----TMDALRAGISMIHQELNLVpHMT 96
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG-----QDirdvTQASLRAAIGIVPQDTVLF-NDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGREPmkygfVDHRQLARQtqtllnklnIRLSA------------DRLVGE----LSIAAQQMVEIAKAVSWNA 160
Cdd:COG5265 448 IAYNIAYGRPD-----ASEEEVEAA---------ARAAQihdfieslpdgyDTRVGErglkLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 161 DIVIMDEPTSAL-TESEVAhlftIIRDLRE--QGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:COG5265 514 PILIFDEATSALdSRTERA----IQAALREvaRGRTTLVIAHRLSTI-VDADEILVLEAG 568
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
257-473 |
4.44e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.99 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLSR-----KGYFEE---------VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSP 322
Cdd:PRK11308 5 LLQAIDLKKhypvkRGLFKPerlvkaldgVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 323 SVAiekgmALLTED--------------RKKSGLFLVLSVMENMSIvNMPEYIGKsgfvkhmkmAQDCMeqiRRLNIKTP 388
Cdd:PRK11308 85 EAQ-----KLLRQKiqivfqnpygslnpRKKVGQILEEPLLINTSL-SAAERREK---------ALAMM---AKVGLRPE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 389 TMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVM 467
Cdd:PRK11308 147 HYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVM 226
|
....*.
gi 490997255 468 VMHEGR 473
Cdd:PRK11308 227 VMYLGR 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-214 |
4.62e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHA-----LMGENGAGKSTLMKCLIGIYRPDKGAIRVKgepvqfqdtmdaLRagISMIHQELNLV 92
Cdd:PRK13409 347 TKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------LK--ISYKPQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 PHMTVAEniWLGREPMKYG--FVDHRqlarqtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:PRK13409 413 YDGTVED--LLRSITDDLGssYYKSE--------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 171 AL-TESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVF 214
Cdd:PRK13409 483 HLdVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVF 527
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
272-474 |
4.65e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGM----ERFDSGEVLIDGQPViidSPSvaiekgmalltEDRKKsglfLVLS 347
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPV---APC-----------ALRGR----KIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 VMENmsivnmPeyigKSGFVKHMKMAQDCMEQIRRLNiKTPTMDQIINNL-------------------SGGNQQKVLIA 408
Cdd:PRK10418 84 IMQN------P----RSAFNPLHTMHTHARETCLALG-KPADDATLTAALeavglenaarvlklypfemSGGMLQRMMIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 409 RWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-217 |
4.97e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPvqfqdtMDALRAGISMI 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP------LAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQELNLVPHMTVAENIWLGREPmkygfvDHRQLARQTqtlLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKG------QWRDAALQA---LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 166 DEP---TSALTESEVAHLftIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK11247 158 DEPlgaLDALTRIEMQDL--IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
271-475 |
6.40e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGE-------------ILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpVIIDSpsvaiEKGMALLTEDR 337
Cdd:PRK11144 3 ELNFKQQLGDlcltvnltlpaqgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDA-----EKGICLPPEKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 338 K------KSGLFLVLSVMENMsivnmpeyigKSGFVKHMKmAQdcMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWL 411
Cdd:PRK11144 77 RigyvfqDARLFPHYKVRGNL----------RYGMAKSMV-AQ--FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:PRK11144 144 LTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-211 |
7.44e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 67.27 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGiyRPD----KGAIRVKGEPVQfqdtmDALRAGISMIHQELNLVPHMT 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTagviTGEILINGRPLD-----KNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VaeniwlgREPMkygfvdhrqlarqtqtllnklniRLSAdrLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESE 176
Cdd:cd03232 96 V-------REAL-----------------------RFSA--LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 490997255 177 VAHLFTIIRDLREQGKAII-YISHKMDEIFAITDEI 211
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRL 179
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-239 |
7.53e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIY----RPD----KGAIRVKGEPVQfqdTMDALRAGI--SMIHQELN 90
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRgarvTGDVTLNGEPLA---AIDAPRLARlrAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 91 LVPHMTVAENIWLGREP--MKYGFVDHRQLARQTQTLlnklnIRLSADRLVGE----LSIAAQQMVEIAKAVS--WNAD- 161
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPhaRRAGALTHRDGEIAWQAL-----ALAGATALVGRdvttLSGGELARVQFARVLAqlWPPHd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 162 ------IVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTRQSLI 234
Cdd:PRK13547 169 aaqpprYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHI 248
|
....*
gi 490997255 235 TQMVG 239
Cdd:PRK13547 249 ARCYG 253
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
7.63e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfQDTMDALRAGISMIHQELNLVPHMTVAEN 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 101 IWLGrepmkygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHL 180
Cdd:PRK13540 95 CLYD--------IHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|
gi 490997255 181 FTIIRDLREQGKAIIYISHK 200
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-217 |
8.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 8.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkGEPV----QFQDTMDALRAGISMIHQ--ELNLV 92
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVvsstSKQKEIKPVRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 PHmTVAENIWLGrePMKYGfVDHRQLARQTQTLLNKLNIRLSA-DRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSA 171
Cdd:PRK13643 99 EE-TVLKDVAFG--PQNFG-IPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490997255 172 LTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-217 |
9.28e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.58 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDaLRAGISMIHQEL-NLVPHMT 96
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGREpmKYGFVDHRQLARQTQTLLnKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESE 176
Cdd:PRK13642 99 VEDDVAFGME--NQGIPREEMIKRVDEALL-AVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 177 VAHLFTIIRDLREQGK-AIIYISHKMDEIfAITDEISVFRDG 217
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQlTVLSITHDLDEA-ASSDRILVMKAG 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-228 |
9.48e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 3 AFALEAEGISKFFP-GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGiYRPDKGAIRVKGepVQFQD-TMDALRA 80
Cdd:PRK11174 347 PVTIEAEDLEILSPdGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKING--IELRElDPESWRK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQELNLvPHMTVAENIWLGREPMKYGFVDhrQLARQTQTL--LNKLNIRLsaDRLVGE----LSIAAQQMVEIAK 154
Cdd:PRK11174 424 HLSWVGQNPQL-PHGTLRDNVLLGNPDASDEQLQ--QALENAWVSefLPLLPQGL--DTPIGDqaagLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 155 AVSWNADIVIMDEPTSAL-TESEVAhlftIIRDLRE--QGKAIIYISHKMDEIFAItDEISVFRDGTWVgsrQTGEF 228
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLdAHSEQL----VMQALNAasRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV---QQGDY 567
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
271-469 |
9.67e-13 |
|
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: 70.39 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEdrkkSGLFLVLSVME 350
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADADADSWRDQIAWVPQ----HPFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMSIvnmpeyiGKSGFVKHM------KMAQDCMEQIRRLNIKTPTMDQIiNNLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:TIGR02857 415 NIRL-------ARPDASDAEirealeRAGLDEFVAALPQGLDTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 425 RGIDVGAKAEIYHLISELAnRGVAVIMVSSElPEILGMSDRVMVM 469
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVVL 529
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
382-474 |
1.06e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.11 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 382 RLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILG 461
Cdd:PRK13631 162 KMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLE 241
|
90
....*....|...
gi 490997255 462 MSDRVMVMHEGRI 474
Cdd:PRK13631 242 VADEVIVMDKGKI 254
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
255-474 |
1.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.22 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLSRKgYFEE--------VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAI 326
Cdd:PRK13650 2 SNIIEVKNLTFK-YKEDqekytlndVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 327 EK-GMALLTEDRKKSGLFLVLSV---MEN--MSIVNMPEYIgksgfvkhmkmaQDCMEQIRRLNIKT--PTmdqiinNLS 398
Cdd:PRK13650 81 HKiGMVFQNPDNQFVGATVEDDVafgLENkgIPHEEMKERV------------NEALELVGMQDFKErePA------RLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 399 GGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEIlGMSDRVMVMHEGRI 474
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
270-474 |
1.34e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.09 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpVIIDSPSvaiekgmalLTEDRKKSGL------- 342
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG--ITISKEN---------LKEIRKKIGIifqnpdn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 343 -FLVLSV-------MENMSIV--NMPEYIGKSGFVKHMKMAQDcmeqirrlniKTPtmdqiiNNLSGGNQQKVLIARWLL 412
Cdd:PRK13632 95 qFIGATVeddiafgLENKKVPpkKMKDIIDDLAKKVGMEDYLD----------KEP------QNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 413 AQPKILILDEPTRGIDVGAKAEIYHLISELANRGV-AVIMVSSELPEILgMSDRVMVMHEGRI 474
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-238 |
1.41e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVPHm 95
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHHYLHRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIWLG--REPMKygfvDHRQLARQTQTLLNKLNIRLSADRLVGE----LSIAAQQMVEIAKAVSWNADIVIMDEPT 169
Cdd:TIGR00958 570 SVRENIAYGltDTPDE----EIMAAAKAANAHDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 170 SALtESEVAHLFTIIRDLreQGKAIIYISHKMDEIfAITDEISVFRDGTWVgsrQTGEF----TRQSLITQMV 238
Cdd:TIGR00958 646 SAL-DAECEQLLQESRSR--ASRTVLLIAHRLSTV-ERADQILVLKKGSVV---EMGTHkqlmEDQGCYKHLV 711
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
271-468 |
1.41e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspSVAIEKGM-ALLTEDRKKSGLFLVLsvM 349
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-----RQALQKNLvAYVPQSEEVDWSFPVL--V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENmsIVNMPEYiGKSGFVKHMKMA--QDCMEQIRRLNIKTPTMDQIiNNLSGGNQQKVLIARWLLAQPKILILDEPTRGI 427
Cdd:PRK15056 98 ED--VVMMGRY-GHMGWLRRAKKRdrQIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 428 DVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSD-RVMV 468
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDyTVMV 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
284-474 |
1.43e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 284 VAGLVGA---GRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSV-AIEKGMALLTEDRKKSGLFlvlsvmenmsiVNMPE 359
Cdd:PRK13638 29 VTGLVGAngcGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlALRQQVATVFQDPEQQIFY-----------TDIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 360 YIGKSgfVKHMKMAQDcmEQIRRLNIKTPTMD------QIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKA 433
Cdd:PRK13638 98 DIAFS--LRNLGVPEA--EITRRVDEALTLVDaqhfrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490997255 434 EIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
253-474 |
1.50e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.69 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 253 IGEEVLTVRNLsRKGYFEE-----VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPV--IIDSP--- 322
Cdd:PRK10619 1 MSENKLNVIDL-HKRYGEHevlkgVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlVRDKDgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 323 SVAIEKGMALL----TEDRKKSGLFLVLSVMENMsivnMPEYIGKSGFVKHmKMAQDCMEQIRRLNIKTPTMDQIINNLS 398
Cdd:PRK10619 80 KVADKNQLRLLrtrlTMVFQHFNLWSHMTVLENV----MEAPIQVLGLSKQ-EARERAVKYLAKVGIDERAQGKYPVHLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 399 GGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
1.54e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.12 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkGEPV----QFQDTMDALRAGISMIHQ--ELNLV 92
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagKKNKKLKPLRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 PHmTVAENIWLGrePMKYGFVDHRQLARQTQTLlnKLnIRLSADRLVG---ELSIAAQQMVEIAKAVSWNADIVIMDEPT 169
Cdd:PRK13634 100 EE-TVEKDICFG--PMNFGVSEEDAKQKAREMI--EL-VGLPEELLARspfELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 170 SALTES---EVAHLFTIIRdlREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGS 222
Cdd:PRK13634 174 AGLDPKgrkEMMEMFYKLH--KEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
259-474 |
1.57e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 259 TVRNLSrKGYFE-----EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIiDSPSVAIEKGMALl 333
Cdd:PRK11000 5 TLRNVT-KAYGDvviskDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 tedrKKSGLFLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMeQIRRLNIKTPtmdqiiNNLSGGNQQKVLIARWLLA 413
Cdd:PRK11000 82 ----QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVL-QLAHLLDRKP------KALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 414 QPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
272-482 |
1.68e-12 |
|
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: 69.39 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpviidspsvaiekgMALLTEDRKKSG---------- 341
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---------------ADLSQWDREELGrhigylpqdv 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 342 -LFlVLSVMEN---MSIVNmPEYIgksgfVKHMKMAqDCMEQIRRLN--IKTPtMDQIINNLSGGNQQKVLIARWLLAQP 415
Cdd:COG4618 416 eLF-DGTIAENiarFGDAD-PEKV-----VAAAKLA-GVHEMILRLPdgYDTR-IGEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 416 KILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVsSELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVI-THRPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
272-474 |
1.71e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.67 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspsvaiekgMAL----LTEDRKKSGL----F 343
Cdd:PRK11153 24 VSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL------------TALsekeLRKARRQIGMifqhF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 LVLS---VMENmsiVNMPeyigksgfvkhMKMAQDCMEQIRR----------LNIKtptMDQIINNLSGGNQQKVLIARW 410
Cdd:PRK11153 92 NLLSsrtVFDN---VALP-----------LELAGTPKAEIKArvtellelvgLSDK---ADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 411 LLAQPKILILDEPTRGIDVGAKAEIYHLISELaNR--GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDI-NRelGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
258-474 |
1.81e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSRKGYFEEV----NFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpVIIDSpSVAIEKGMALL 333
Cdd:PRK11264 4 IEVKNLVKKFHGQTVlhgiDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGD--ITIDT-ARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDRKKSG-------LFLVLSVMENmsIVNMPEYIGKSGFVKHMKMAQDCMEQIRrLNIKTptmDQIINNLSGGNQQKVL 406
Cdd:PRK11264 81 RQLRQHVGfvfqnfnLFPHRTVLEN--IIEGPVIVKGEPKEEATARARELLAKVG-LAGKE---TSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 407 IARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-199 |
1.87e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.17 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 4 FALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKC---LIGIYRPDK--GAIRVKGEPVQFQDtMDAL 78
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARveGEVRLFGRNIYSPD-VDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 79 --RAGISMIHQELNLVPHMTVAENIWLGrepMKY-------GFVDHR-QLARQTQTLLNKLNIRLsaDRLVGELSIAAQQ 148
Cdd:PRK14267 82 evRREVGMVFQYPNPFPHLTIYDNVAIG---VKLnglvkskKELDERvEWALKKAALWDEVKDRL--NDYPSNLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 149 MVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQgKAIIYISH 199
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-172 |
2.66e-12 |
|
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: 68.81 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkGEPV------QFQDTMDalr 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVklayvdQSRDALD--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 agismihqelnlvPHMTVAENIWLGREPMKYGFVDhrqlaRQTQTLLNKLNIRlSAD--RLVGELSIAAQQMVEIAKAVS 157
Cdd:TIGR03719 399 -------------PNKTVWEEISGGLDIIKLGKRE-----IPSRAYVGRFNFK-GSDqqKKVGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*
gi 490997255 158 WNADIVIMDEPTSAL 172
Cdd:TIGR03719 460 SGGNVLLLDEPTNDL 474
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
258-475 |
2.72e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMAL 332
Cdd:PRK11231 3 LRTENLT-VGYgtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP-ISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEdrkksglflVLSVMENMSIVNMPEYiGKSGFVKHM-KMAQDCMEQIRRLNIKTPTM---DQIINNLSGGNQQKVLIA 408
Cdd:PRK11231 81 LPQ---------HHLTPEGITVRELVAY-GRSPWLSLWgRLSAEDNARVNQAMEQTRINhlaDRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 409 RwLLAQ-PKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:PRK11231 151 M-VLAQdTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-199 |
2.88e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDALR-AGism 84
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 85 iHQElNLVPHMTVAENI--WlgrepmkygfvdhRQLARQTQTL----LNKLNIRLSADRLVGELSIAAQQMVEIAKAVSW 158
Cdd:PRK13539 80 -HRN-AMKPALTVAENLefW-------------AAFLGGEELDiaaaLEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490997255 159 NADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISH 199
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-218 |
3.03e-12 |
|
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: 64.01 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepvqfqdtmdalRAGISMI 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 HQelnlvphmtvaeniwlgrepmkygfvdhrqlarqtqtllnklnirLSAdrlvGElsiaaqQM-VEIAKAVSWNADIVI 164
Cdd:cd03221 69 EQ---------------------------------------------LSG----GE------KMrLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 165 MDEPTSAL-TESeVAHLftiIRDLREQGKAIIYISHkmDEIF--AITDEISVFRDGT 218
Cdd:cd03221 94 LDEPTNHLdLES-IEAL---EEALKEYPGTVILVSH--DRYFldQVATKIIELEDGK 144
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
259-479 |
3.29e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 259 TVRNLSRKGYFE-----EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpviidSPSvaiekgmall 333
Cdd:COG4586 23 ALKGLFRREYREveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-----VPF---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 tEDRK------------KSGLFLVLSVME----NMSIVNMPEyigkSGFVKHMKmaqdcmEQIRRLNIKtPTMDQIINNL 397
Cdd:COG4586 88 -KRRKefarrigvvfgqRSQLWWDLPAIDsfrlLKAIYRIPD----AEYKKRLD------ELVELLDLG-ELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 398 SGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRItg 476
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI-- 233
|
...
gi 490997255 477 ILD 479
Cdd:COG4586 234 IYD 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
257-451 |
3.70e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNL--SRKG--YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspsvaiekgmAL 332
Cdd:PRK13538 1 MLEARNLacERDEriLFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------------RR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEDRKKSGLFL--------VLSVMENMSIvnmpeYIGKSGFVKhmkmAQDCMEQIRRLNIKTpTMDQIINNLSGGNQQK 404
Cdd:PRK13538 68 QRDEYHQDLLYLghqpgiktELTALENLRF-----YQRLHGPGD----DEALWEALAQVGLAG-FEDVPVRQLSAGQQRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490997255 405 VLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIM 451
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-218 |
4.07e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVPHmTVAE 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 NIWLGREPMKYGFVDHrqLARQTQTLLNKLNIRLSADRLVGE----LSIAAQQMVEIAKAVSWNADIVIMDEPTSAL--- 172
Cdd:PRK10789 408 NIALGRPDATQQEIEH--VARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVdgr 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490997255 173 TESEvahlftIIRDLRE--QGKAIIYISHKMDeifAIT--DEISVFRDGT 218
Cdd:PRK10789 486 TEHQ------ILHNLRQwgEGRTVIISAHRLS---ALTeaSEILVMQHGH 526
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-237 |
5.05e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.13 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIyrpDKGAIRVKGEPVQFQDtMDALRA-----------GISMIH 86
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDD-IDLLRLsprerrklvghNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QELN--LVPHMTVAENI--------WLGREPMKYGFVDHRQLarqtqTLLNKLNIRLSADRLVG---ELSIAAQQMVEIA 153
Cdd:PRK15093 96 QEPQscLDPSERVGRQLmqnipgwtYKGRWWQRFGWRKRRAI-----ELLHRVGIKDHKDAMRSfpyELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 154 KAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQ-GKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEFTR-- 230
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTtp 250
|
250
....*....|..
gi 490997255 231 -----QSLITQM 237
Cdd:PRK15093 251 hhpytQALIRAI 262
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-214 |
6.50e-12 |
|
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: 67.89 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVH-----ALMGENGAGKSTLMKCLIGIYRPDKGAIRVKgepvqfqdtmdaLRagISMIHQELNLV 92
Cdd:COG1245 348 TKSYGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------LK--ISYKPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 PHMTVAENIwlgREPMKYGFVDHRQlarQTQtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSAL 172
Cdd:COG1245 414 YDGTVEEFL---RSANTDDFGSSYY---KTE-IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490997255 173 TESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVF 214
Cdd:COG1245 487 DVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
272-474 |
6.96e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.32 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVME------SLFGMERFdSGEVLIDGQPVIidspsvaiekGMALLTEDRKKSGLFLV 345
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRvfnrliELYPEARV-SGEVYLDGQDIF----------KMDVIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 346 LSVMENMSIV-NMPEYIGKSGFVKHMKMAQdcmEQIRRLNIKTPTMDQIIN-------NLSGGNQQKVLIARWLLAQPKI 417
Cdd:PRK14247 91 PNPIPNLSIFeNVALGLKLNRLVKSKKELQ---ERVRWALEKAQLWDEVKDrldapagKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 418 LILDEPTRGIDVGAKAEIYHLISELaNRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
258-475 |
7.27e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 63.87 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS------RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViiDSPSVAIEKGMA 331
Cdd:cd03247 1 LSINNVSfsypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEdrkKSGLFlvlsvmeNMSIVNmpeyigksgfvkhmkmaqdcmeqirrlNIKTPtmdqiinnLSGGNQQKVLIARWL 411
Cdd:cd03247 79 VLNQ---RPYLF-------DTTLRN---------------------------NLGRR--------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 412 LAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGMsDRVMVMHEGRIT 475
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-217 |
7.52e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPD---KGAIRVKGEPVqfqdTMDALRAGISMIHQELNLVPHMTV 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 98 AENIW------LGREPMKygfvDHRQLArqTQTLLNKLNIRLSADRLVGE------LSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:TIGR00955 117 REHLMfqahlrMPRRVTK----KEKRER--VDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHK-MDEIFAITDEISVFRDG 217
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEG 243
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-200 |
1.01e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.83 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGiyRPDKGAIR-----VKGEPVQ--FQdtmdalRAGISMIHQELNLvP 93
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITggdrlVNGRPLDssFQ------RSIGYVQQQDLHL-P 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 94 HMTVAENIWLG---REPM------KYGFVDHrqlarqtqtLLNKLNIRLSADRLVGE------------LSIAaqqmVE- 151
Cdd:TIGR00956 850 TSTVRESLRFSaylRQPKsvskseKMEYVEE---------VIKLLEMESYADAVVGVpgeglnveqrkrLTIG----VEl 916
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 152 IAKAVSwnadIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHK 200
Cdd:TIGR00956 917 VAKPKL----LLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
269-453 |
1.09e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQ---------PVIIDSPSV--AIEKGMALLTEDR 337
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqePPLDDDLTVldTVLDGDAELRALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 338 KKsglFLVLSVMENMSIVNMPEYiGKsgfvkhmkmAQDCME---------QIRR----LNIKTPTMDQIINNLSGGNQQK 404
Cdd:COG0488 94 AE---LEELEAKLAEPDEDLERL-AE---------LQEEFEalggweaeaRAEEilsgLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 405 VLIARWLLAQPKILILDEPTRGIDVGAkaeIYHLISELANRGVAVIMVS 453
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPGTVLVVS 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-211 |
1.10e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 9 EGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKgepvqfqdtmDALRagISMIHQE 88
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----------GKLR--IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 89 LNLVPHMTVAENIWLGREPmkygfvdhrqlARQTQTLLNKLNiRLSADRLVG----ELSIAAQQMVEIAKAVSWNADIVI 164
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLRP-----------GTKKEDILPALK-RVQAGHLIDapmqKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 165 MDEPTSALTESEVAHLFTIIRDLR-EQGKAIIYISHKMDEIFAITDEI 211
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
397-474 |
1.29e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.70 E-value: 1.29e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-204 |
1.32e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTM--DALRAGISMIHQELNLVPH 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS---TLkpEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 95 mTVAENI---WLGR--EPMKYGFVDHRQLARQTQTLLNKlNIRlsadrlvgELSIAAQQMVEIAKAVSWNADIVIMDEPT 169
Cdd:PRK10247 96 -TVYDNLifpWQIRnqQPDPAIFLDDLERFALPDTILTK-NIA--------ELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 490997255 170 SALTESEVAHLFTII-RDLREQGKAIIYISHKMDEI 204
Cdd:PRK10247 166 SALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEI 201
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
271-474 |
1.34e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpVIIDSPSVAIEkgmalLTEDRKKSGL---FLVLS 347
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGD--IVVSSTSKQKE-----IKPVRKKVGVvfqFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 VMENMSIVNMPeyIGKSGF-VKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRG 426
Cdd:PRK13643 97 LFEETVLKDVA--FGPQNFgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 427 IDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-199 |
1.39e-11 |
|
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: 66.75 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 24 VSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVPHMtvaeniwl 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-ADNREAYRQLFSAVFSDFHLFDRL-------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 104 grepmkYGfVDHRQLARQTQTLLNKLNI----RLSADRLVG-ELS---------IAAqqMVEiakavswNADIVIMDE-- 167
Cdd:COG4615 422 ------LG-LDGEADPARARELLERLELdhkvSVEDGRFSTtDLSqgqrkrlalLVA--LLE-------DRPILVFDEwa 485
|
170 180 190
....*....|....*....|....*....|....*...
gi 490997255 168 ----PtsaltesEVAHLF--TIIRDLREQGKAIIYISH 199
Cdd:COG4615 486 adqdP-------EFRRVFytELLPELKARGKTVIAISH 516
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
279-473 |
1.42e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 279 GEILGVAGLVGAGRSEVMESLFGMERFDS--GEVLIDGQpviidSPSVAIEKGMALLTEDrkkSGLFLVLSVMENM---S 353
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR-----KPTKQILKRTGFVTQD---DILYPHLTVRETLvfcS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 354 IVNMPEYIGKSgfvKHMKMAQDCMEQIRRLNIK-TPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAK 432
Cdd:PLN03211 166 LLRLPKSLTKQ---EKILVAESVISELGLTKCEnTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490997255 433 AEIYHLISELANRGvAVIMVSSELP--EILGMSDRVMVMHEGR 473
Cdd:PLN03211 243 YRLVLTLGSLAQKG-KTIVTSMHQPssRVYQMFDSVLVLSEGR 284
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-204 |
2.52e-11 |
|
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: 63.28 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMD--ALRAGISMIHQElnlvPHM-- 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS---KIGlhDLRSRISIIPQD----PVLfs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 -TVAENIwlgrEPMKYgFVDHR--------QLARQTQTLLNKLNIRLSADrlvGE-LSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:cd03244 92 gTIRSNL----DPFGE-YSDEElwqalervGLKEFVESLPGGLDTVVEEG---GEnLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 166 DEPTSAL-TESEvAHLFTIIRDlREQGKAIIYISHKMDEI 204
Cdd:cd03244 164 DEATASVdPETD-ALIQKTIRE-AFKDCTVLTIAHRLDTI 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-227 |
2.52e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFF---------PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTmd 76
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 ALRAG-ISMIHQE--LNLVPhmtvaeniwlgrepmkygfvdhRQLARQTQTLLNKLNIRLSAD----------RLVGELS 143
Cdd:PRK15112 83 SYRSQrIRMIFQDpsTSLNP----------------------RQRISQILDFPLRLNTDLEPEqrekqiietlRQVGLLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 144 IAA-----------QQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLRE-QGKAIIYISHKMDEIFAITDEI 211
Cdd:PRK15112 141 DHAsyyphmlapgqKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQV 220
|
250
....*....|....*.
gi 490997255 212 SVFRDGTWVGSRQTGE 227
Cdd:PRK15112 221 LVMHQGEVVERGSTAD 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
391-453 |
2.99e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.79 E-value: 2.99e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 391 DQII----NNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISElanRGVAVIMVS 453
Cdd:cd03223 82 EQLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE---LGITVISVG 145
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-217 |
3.38e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.95 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepvqfQDTMDA-----LRAGISMIHQEL-NLVP 93
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-----LDTSDEenlwdIRNKAGMVFQNPdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 94 HMTVAENIWLGREPMKygfVDHRQLARQTQTLLNKLNI---RLSADRLvgeLSIAAQQMVEIAKAVSWNADIVIMDEPTS 170
Cdd:PRK13633 100 ATIVEEDVAFGPENLG---IPPEEIRERVDESLKKVGMyeyRRHAPHL---LSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 171 ALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:PRK13633 174 MLDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSG 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
257-474 |
3.71e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLS-----RKGYFEEVN---FSVRRGEILGVAGLVGAGRSEVMESLFGMerfdsgevlidgqpviIDSPS-VAIE 327
Cdd:PRK11022 3 LLNVDKLSvhfgdESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGL----------------IDYPGrVMAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 328 K----GMALLT----EDRKKSGLFLVLSVMENMSIVNmPEYIGKSGFVKHMKMAQDCMEQIRR---------LNIKTPT- 389
Cdd:PRK11022 67 KlefnGQDLQRisekERRNLVGAEVAMIFQDPMTSLN-PCYTVGFQIMEAIKVHQGGNKKTRRqraidllnqVGIPDPAs 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 390 -MDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVM 467
Cdd:PRK11022 146 rLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKII 225
|
....*..
gi 490997255 468 VMHEGRI 474
Cdd:PRK11022 226 VMYAGQV 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-216 |
3.81e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 1 MNAFALEAEGISKffpgvKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIY--RPDKGAIRVKGEPvqfqdtmdal 78
Cdd:COG2401 31 LEAFGVELRVVER-----YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 79 ragismIHQELNLVphmtvaENIWLGREPmkygfvdhrqlaRQTQTLLN--KLNIRLSADRLVGELSIAAQQMVEIAKAV 156
Cdd:COG2401 96 ------FGREASLI------DAIGRKGDF------------KDAVELLNavGLSDAVLWLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 157 SWNADIVIMDEPTSAL---TESEVAHlftIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRD 216
Cdd:COG2401 152 AERPKLLVIDEFCSHLdrqTAKRVAR---NLQKLaRRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
270-482 |
3.82e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.67 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpviIDSPSVAiekgMALLTEDRKK--SGLFLVLS 347
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----VDIAKIS----DAELREVRRKkiAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 VMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIKTpTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGI 427
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLEN-YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 428 DVGAKAEIY-HLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGILDKDE 482
Cdd:PRK10070 196 DPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
264-477 |
4.05e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.87 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 264 SRKGYFE-----EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGevlidgQPVIIDSPSVAIEKGMALLTEDRK 338
Cdd:PRK13645 17 AKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG------QTIVGDYAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 339 KSGLflvlsvmenmsIVNMPEY------IGKSGFVKHMKMAQDCMEQIRrlniKTPTMDQIIN-----------NLSGGN 401
Cdd:PRK13645 91 EIGL-----------VFQFPEYqlfqetIEKDIAFGPVNLGENKQEAYK----KVPELLKLVQlpedyvkrspfELSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 402 QQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGI 477
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-217 |
4.50e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 11 ISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGI----YRPDkGAIRVKGEPvqFQDTMDALRAGISMIH 86
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIP--YKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QELNLVPHMTVAENIwlgrepmkygfvdhrqlarqtqtllnKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMD 166
Cdd:cd03233 90 EEDVHFPTLTVRETL--------------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 167 EPTSALTESEVAHLFTIIRDLREQGK--AIIYISHKMDEIFAITDEISVFRDG 217
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKttTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-218 |
5.28e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfQDTMDALRAGISMIHQELNLVPHMTVAE 99
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-AEQPEDYRKLFSAVFTDFHLFDQLLGPE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 N---------IWLGREPM--KYGFVDHRQlarqtqtllnkLNIRLSA---DRLVGELSIAAQQmveiakavswnaDIVIM 165
Cdd:PRK10522 417 GkpanpalveKWLERLKMahKLELEDGRI-----------SNLKLSKgqkKRLALLLALAEER------------DILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 166 DEpTSALTESEVAHLF--TIIRDLREQGKAIIYISHKmDEIFAITDEISVFRDGT 218
Cdd:PRK10522 474 DE-WAADQDPHFRREFyqVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
397-472 |
5.57e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.77 E-value: 5.57e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESISQWADTITVLYCG 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
270-474 |
5.64e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDRKKSGlflVLSVM 349
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH-IQHYASKEVARRIGLLAQNATTPG---DITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 EnmsIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:PRK10253 100 E---LVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490997255 430 GAKAEIYHLISELaNR--GVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK10253 177 SHQIDLLELLSEL-NRekGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
270-474 |
6.40e-11 |
|
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: 62.10 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDRKKSGLflvlSVM 349
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP-ISQYEHKYLHSKVSLVGQEPVLFAR----SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 EN----------MSIVNMPEYIGKSGFVkhMKMAQDCMEQIrrlniktptmDQIINNLSGGNQQKVLIARWLLAQPKILI 419
Cdd:cd03248 106 DNiayglqscsfECVKEAAQKAHAHSFI--SELASGYDTEV----------GEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 420 LDEPTRGIDVGAKAEIYHLISE-LANRGVAVIMVSSELPEilgMSDRVMVMHEGRI 474
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDwPERRTVLVIAHRLSTVE---RADQILVLDGGRI 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
229-474 |
6.48e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 229 TRQSLITQMV--GRELTQLFPKFNNTIGEEV-------LTVRNLS---RKG--YFEEVNFSVRRGEILGVAGLVGAGRSE 294
Cdd:PRK10790 303 TQQSMLQQAVvaGERVFELMDGPRQQYGNDDrplqsgrIDIDNVSfayRDDnlVLQNINLSVPSRGFVALVGHTGSGKST 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 295 VMESLFGMERFDSGEVLIDGQPVIIDSPSVaIEKGMALLTEDRkksgLFLVLSVMENmsiVNMPEYIGKSGFVKHMKMAQ 374
Cdd:PRK10790 383 LASLLMGYYPLTEGEIRLDGRPLSSLSHSV-LRQGVAMVQQDP----VVLADTFLAN---VTLGRDISEEQVWQALETVQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 375 dCMEQIRRL--NIKTPTMDQIiNNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVImV 452
Cdd:PRK10790 455 -LAELARSLpdGLYTPLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV-I 531
|
250 260
....*....|....*....|..
gi 490997255 453 SSELPEILGmSDRVMVMHEGRI 474
Cdd:PRK10790 532 AHRLSTIVE-ADTILVLHRGQA 552
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-218 |
6.73e-11 |
|
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: 61.96 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAI---RVKGEPVQFQDTMDALRAGISMIHQELNLV 92
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 pHMTVAENIWLGR--EPMKYGFV--------DHRQLARQTQTLLNKLNIRLSADRlvgelsiaaQQMVEIAKAVSWNADI 162
Cdd:cd03290 92 -NATVEENITFGSpfNKQRYKAVtdacslqpDIDLLPFGDQTEIGERGINLSGGQ---------RQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 163 VIMDEPTSALTESEVAHLFT--IIRDLREQGKAIIYISHKMdEIFAITDEISVFRDGT 218
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDGS 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
258-453 |
7.27e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 61.73 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS----RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGM--ERFD-SGEVLIDGQPvIIDSPsvAIEKGM 330
Cdd:COG4136 2 LSLENLTitlgGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRR-LTALP--AEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 ALLTEDrkkSGLFLVLSVMENMSIvNMPEYIGKSGfvkhmkmaqdcmeqiRRLNIKTpTMDQI---------INNLSGGN 401
Cdd:COG4136 79 GILFQD---DLLFPHLSVGENLAF-ALPPTIGRAQ---------------RRARVEQ-ALEEAglagfadrdPATLSGGQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 402 QQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLI-SELANRGVAVIMVS 453
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVT 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-217 |
7.28e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVR---PGT-VHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkGEPVQFQDTMD----ALRAGISMIHQELN 90
Cdd:PRK11144 8 QQLGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGiclpPEKRRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 91 LVPHMTVAENiwlgrepMKYGfvdhrqLARQTQTLLNK----LNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMD 166
Cdd:PRK11144 87 LFPHYKVRGN-------LRYG------MAKSMVAQFDKivalLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 167 EPTSALTESEVAHLFTIIRDLREQGK-AIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-199 |
8.04e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYrPDKGAIRVKGEPVQfQDTMDAL---RAgisMIHQELNLVPHMTV 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLS-DWSAAELarhRA---YLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 98 AENIWLGREPMkygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAV-----SWNAD--IVIMDEPTS 170
Cdd:COG4138 87 FQYLALHQPAG----ASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|..
gi 490997255 171 ALtesEVAH---LFTIIRDLREQGKAIIYISH 199
Cdd:COG4138 163 SL---DVAQqaaLDRLLRELCQQGITVVMSSH 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-428 |
8.73e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 25 SLRVRPGTVHALMGENGAGKSTLMKCLIGiyrpdkGAIRVKGEPV-QFQD----TMDALRAGISMIHQELN---LVPH-- 94
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG------ELPLLSGERQsQFSHitrlSFEQLQKLVSDEWQRNNtdmLSPGed 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 95 ---MTVAENIWLGrepmkygfVDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSA 171
Cdd:PRK10938 97 dtgRTTAEIIQDE--------VKDPARCEQ---LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 172 LTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWV--GSRQtgEFTRQSLITQMVGREL---TQLF 246
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAetGERE--EILQQALVAQLAHSEQlegVQLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 247 PKFNNTI------GEEVLTVRN----LSRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVME--------------SLFGM 302
Cdd:PRK10938 244 EPDEPSArhalpaNEPRIVLNNgvvsYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysndlTLFGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 303 ERfDSGEVLIDgqpviidspsvaIEKGMALLTedrkkSGLFLVLSVmeNMSIVNmpeyIGKSGFV-----------KHMK 371
Cdd:PRK10938 324 RR-GSGETIWD------------IKKHIGYVS-----SSLHLDYRV--STSVRN----VILSGFFdsigiyqavsdRQQK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 372 MAqdcMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGID 428
Cdd:PRK10938 380 LA---QQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-199 |
9.38e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 22 DNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmDALragismiHQELNLVPH------- 94
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR--DEY-------HQDLLYLGHqpgikte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 95 MTVAENI-WLGRepmkygfvDHRQLAR-QTQTLLNKLNIRLSADRLVGELSiAAQQMvEIAKAVSW--NADIVIMDEPTS 170
Cdd:PRK13538 89 LTALENLrFYQR--------LHGPGDDeALWEALAQVGLAGFEDVPVRQLS-AGQQR-RVALARLWltRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 490997255 171 ALTESEVAHLFTIIRDLREQGKAIIYISH 199
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-63 |
9.44e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.14 E-value: 9.44e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIR 63
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
272-474 |
1.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSP-SVAIEKGMALLTEDRKKSGLFLVLSVME 350
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMSIVNMPEYigksgfvKHMKMAQDCMEQIRRLNIKTPTMDQiinnLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVG 430
Cdd:PRK13642 106 GMENQGIPRE-------EMIKRVDEALLAVNMLDFKTREPAR----LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 431 AKAEIYHLISELANR-GVAVIMVSSELPEIlGMSDRVMVMHEGRI 474
Cdd:PRK13642 175 GRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-220 |
1.12e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.48 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGiyRPD----KGAIRVKGEPVQfQDTMdalrAGISMIHQELNL-VPHM 95
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKK-QETF----ARISGYCEQNDIhSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 96 TVAENIWLG---REPMKYGFVDHRQLARQTQTLLNKLNIRlsaDRLVG-----ELSIAAQQMVEIAKAVSWNADIVIMDE 167
Cdd:PLN03140 969 TVRESLIYSaflRLPKEVSKEEKMMFVDEVMELVELDNLK---DAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490997255 168 PTSALTESEVAHLFTIIRDLREQGKAIIYISHKMD-EIFAITDEISVFRDGTWV 220
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQV 1099
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-217 |
1.62e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGT-----VHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtmdalragismihQELNLV 92
Cdd:cd03237 7 KKTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-------------QYIKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 PHMTVaeniwlgrEPMKYGFVDHRQLARQTQT-LLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSA 171
Cdd:cd03237 74 YEGTV--------RDLLSSITKDFYTHPYFKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490997255 172 LTESEVAHLFTIIRDLREQGKAIIY-ISHkmDEIFA--ITDEISVFrDG 217
Cdd:cd03237 146 LDVEQRLMASKVIRRFAENNEKTAFvVEH--DIIMIdyLADRLIVF-EG 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-217 |
1.74e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.03 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAI-------RVKGEPVQFQDTMD--------------- 76
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKEKVLEklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 77 -ALRAGISMIHQ--ELNLVpHMTVAENIWLGrePMKYGFVDHRQLARQTQTLlnklnirlsadRLVG-----------EL 142
Cdd:PRK13651 101 kEIRRRVGVVFQfaEYQLF-EQTIEKDIIFG--PVSMGVSKEEAKKRAAKYI-----------ELVGldesylqrspfEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 143 SIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
266-494 |
1.81e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 266 KGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGME------RFdSGEVLIDGQPVIIDSPSVAIEKGMALLTEDRKK 339
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgyRY-SGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 340 sglfLVLSVMEN-MSIVNMPEYIGKSGFvkhMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKIL 418
Cdd:PRK14271 113 ----FPMSIMDNvLAGVRAHKLVPRKEF---RGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 419 ILDEPTRGIDVGAKAEIYHLISELANRgVAVIMVSSELPEILGMSDRVMVMHEGRITgildkDEADQETILSLASH 494
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV-----EEGPTEQLFSSPKH 255
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
396-474 |
1.96e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.03 E-value: 1.96e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 396 NLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
272-474 |
1.96e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.85 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERF--DSGEVLIDGQPViidspsvaiekgMALLTEDRKKSGLFLV---- 345
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDGEDI------------LELSPDERARAGIFLAfqyp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 346 -----LSVMENMSIV---NMPEYIGKSGFVKHMKmaqdcmEQIRRLNIKTPTMDQIIN-NLSGGNQQKVLIARWLLAQPK 416
Cdd:COG0396 87 veipgVSVSNFLRTAlnaRRGEELSAREFLKLLK------EKMKELGLDEDFLDRYVNeGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 417 ILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVsSELPEILGM--SDRVMVMHEGRI 474
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILII-THYQRILDYikPDFVHVLVDGRI 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
272-475 |
2.69e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.24 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIdspsvaIEKGMALLTEdrkksglflvLSVMEN 351
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL------LGLGGGFNPE----------LTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 MSIVNMpeYIGKSGfvkhmKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGA 431
Cdd:cd03220 105 IYLNGR--LLGLSR-----KEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490997255 432 KAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
254-474 |
3.10e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVrnlsrkgyFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpviidspSVAIEKGMALL 333
Cdd:PRK10535 17 GEEQVEV--------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ-------DVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 334 TEDRKKSG-------LFLVLSVMENmsiVNMPEYIGKSGFVKHMKMAQdcmEQIRRLNIKTpTMDQIINNLSGGNQQKVL 406
Cdd:PRK10535 82 QLRREHFGfifqryhLLSHLTAAQN---VEVPAVYAGLERKQRLLRAQ---ELLQRLGLED-RVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 407 IARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSElPEILGMSDRVMVMHEGRI 474
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
258-481 |
3.11e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 60.65 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLS--------RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViiDSPSVaiekg 329
Cdd:COG4525 4 LTVRHVSvrypgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGPGA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 330 mallteDR----KKSGLFLVLSVMENMSI------VNMPE----------YIGKSGFVKHMkmaqdcmeqirrlniktpt 389
Cdd:COG4525 77 ------DRgvvfQKDALLPWLNVLDNVAFglrlrgVPKAErraraeellaLVGLADFARRR------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 390 mdqiINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMV 468
Cdd:COG4525 132 ----IWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVV 207
|
250
....*....|....*
gi 490997255 469 M--HEGRITGILDKD 481
Cdd:COG4525 208 MspGPGRIVERLELD 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
397-474 |
3.90e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 3.90e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
270-474 |
4.15e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMAlltedRKKSGLFLVLSVM 349
Cdd:TIGR01257 947 DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC-----PQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMsiVNMPEYIGKSGFVKHMKMaqDCMEQIRRLNIKTptmDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:TIGR01257 1022 EHI--LFYAQLKGRSWEEAQLEM--EAMLEDTGLHHKR---NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 430 GAKAEIYHLISELANrGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-217 |
4.56e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 10 GISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqDTMDALRaGISMIHQEL 89
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAER-GVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 90 NLVPHMTVAENIWLGrepMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPT 169
Cdd:PRK11000 85 ALYPHLSVAENMSFG---LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 170 SALTES-EVAHLFTIIRDLREQGKAIIYISHkmDEIFAIT--DEISVFRDG 217
Cdd:PRK11000 162 SNLDAAlRVQMRIEISRLHKRLGRTMIYVTH--DQVEAMTlaDKIVVLDAG 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
270-474 |
5.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.49 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpviIDSpsvaieKGMALLTEDRKKSGLF------ 343
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG----LDT------SDEENLWDIRNKAGMVfqnpdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 -LVLSVMENmSIVNMPEYIGksgfVKHMKMAQDCMEQIRRLNI-----KTPTMdqiinnLSGGNQQKVLIARWLLAQPKI 417
Cdd:PRK13633 97 qIVATIVEE-DVAFGPENLG----IPPEEIRERVDESLKKVGMyeyrrHAPHL------LSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 418 LILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILgMSDRVMVMHEGRI 474
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAV-EADRIIVMDSGKV 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-472 |
5.76e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 276 VRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDspsvaiekgmalLTEDRKKSGLFLVLSVMENMSIV 355
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------------ISDVHQNMGYCPQFDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 356 NMPEYIgksgFVKHMKMAQDCMEQIRRLNIKTPTM----DQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGA 431
Cdd:TIGR01257 2030 REHLYL----YARLRGVPAEEIEKVANWSIQSLGLslyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490997255 432 KAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-212 |
5.95e-10 |
|
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: 59.69 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 28 VRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIrvkGEPVQFQDTMDALRA-------------GISMIH--QELNLV 92
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---DDPPDWDEILDEFRGselqnyftkllegDVKVIVkpQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 PHMTVAENIWLGREPMKYGFVDhrqlarqtqTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSAL 172
Cdd:cd03236 100 PKAVKGKVGELLKKKDERGKLD---------ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 173 TESEVAHLFTIIRDLREQGKAIIYISHKMdeifAITDEIS 212
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVEHDL----AVLDYLS 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
264-474 |
6.50e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 264 SRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMEslfgmerfdsgevLIDGQPVIIDSPSVAIEKGMALLTED-----RK 338
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISK-------------LINGLLLPDDNPNSKITVDGITLTAKtvwdiRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 339 KSGL--------FLVLSV-------MENMSiVNMPEYIgksgfvkhmKMAQDCMEQIRRLNIktptMDQIINNLSGGNQQ 403
Cdd:PRK13640 85 KVGIvfqnpdnqFVGATVgddvafgLENRA-VPRPEMI---------KIVRDVLADVGMLDY----IDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 404 KVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAN-RGVAVIMVSSELPEIlGMSDRVMVMHEGRI 474
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
272-474 |
6.91e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspSVAIEKGMALLtedRKKSGLFLVLSVM-- 349
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-----HQMDEEARAKL---RAKHVGFVFQSFMli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ------ENmsiVNMPEYIGKSGFVKHMKMAQDCMEQI---RRLniktptmDQIINNLSGGNQQKVLIARWLLAQPKILIL 420
Cdd:PRK10584 101 ptlnalEN---VELPALLRGESSRQSRNGAKALLEQLglgKRL-------DHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 421 DEPTRGIDVGAKAEIYHLISELaNR--GVAVIMVSSElPEILGMSDRVMVMHEGRI 474
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSL-NRehGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
257-451 |
7.42e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNLS--RKG--YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAiekgMAL 332
Cdd:PRK13539 2 MLEGEDLAcvRGGrvLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA----CHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 333 LTEdrkKSGLFLVLSVMENMSivnmpeyigksgFVKHMKMAQDC--MEQIRRLNIKtPTMDQIINNLSGGNQQKVLIARW 410
Cdd:PRK13539 78 LGH---RNAMKPALTVAENLE------------FWAAFLGGEELdiAAALEAVGLA-PLAHLPFGYLSAGQKRRVALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490997255 411 LLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIM 451
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
272-474 |
8.12e-10 |
|
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: 61.27 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLfgmERF---DSGEVLIDGQPvIIDSPSVAIEKGMALLTEDrkksglflvlSV 348
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLI---PRFyepDSGQILLDGHD-LADYTLASLRRQVALVSQD----------VV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MENMSIVNMpeyigksgfVKHMKMAQDCMEQIRRLNIKTPTMDQIIN--------------NLSGGNQQKVLIARWLLAQ 414
Cdd:TIGR02203 417 LFNDTIANN---------IAYGRTEQADRAEIERALAAAYAQDFVDKlplgldtpigengvLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 415 PKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
369-494 |
9.44e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 369 HMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVA 448
Cdd:PRK10938 109 EVKDPARCEQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGIT 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490997255 449 VIMVSSELPEILGMSDRVMVMHEGRITGILDKDEADQETILSLASH 494
Cdd:PRK10938 188 LVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAH 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
397-474 |
1.12e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.89 E-value: 1.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRgVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
397-474 |
1.19e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.61 E-value: 1.19e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGMsDRVMVMHEGRI 474
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
269-456 |
1.32e-09 |
|
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: 60.45 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIiDSPSVAIEKGMALLTEDrkkSGLFLVlSV 348
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRRRVSVCAQD---AHLFDT-TV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 MENMSIVNmPEYIGksgfvkhmkmaQDCMEQIRRLNIKTPT------MDQIINN----LSGGNQQKVLIARWLLAQPKIL 418
Cdd:TIGR02868 426 RENLRLAR-PDATD-----------EELWAALERVGLADWLralpdgLDTVLGEggarLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 490997255 419 ILDEPTRGIDVGAKAEIYHLISElANRGVAVIMVSSEL 456
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
391-475 |
1.45e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.66 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 391 DQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAN--RGVAVIMVSSELPEILGMSDRVMV 468
Cdd:cd03233 113 NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLV 192
|
....*..
gi 490997255 469 MHEGRIT 475
Cdd:cd03233 193 LYEGRQI 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
271-474 |
1.83e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.33 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViidspsvaiekgMALLTEDRK------KSGLFL 344
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV------------SRLHARDRKvgfvfqHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 345 VLSVMENMS--IVNMPEYIGKSGFVKHMKMAQDC-MEQIRRLNIKTPTmdqiinNLSGGNQQKVLIARWLLAQPKILILD 421
Cdd:PRK10851 88 HMTVFDNIAfgLTVLPRRERPNAAAIKAKVTQLLeMVQLAHLADRYPA------QLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 422 EPTRGIDVGAKAE----IYHLISELANRGVAVIMVSSELPEIlgmSDRVMVMHEGRI 474
Cdd:PRK10851 162 EPFGALDAQVRKElrrwLRQLHEELKFTSVFVTHDQEEAMEV---ADRVVVMSQGNI 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
361-453 |
2.18e-09 |
|
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: 55.92 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 361 IGKSGFVKHM--KMAQDCMEQIRRLNIKTPTMDQiinnLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAkaeIYHL 438
Cdd:cd03221 37 AGKSTLLKLIagELEPDEGIVTWGSTVKIGYFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEAL 109
|
90
....*....|....*
gi 490997255 439 ISELANRGVAVIMVS 453
Cdd:cd03221 110 EEALKEYPGTVILVS 124
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-76 |
3.01e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 3.01e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 6 LEAEGISKFFpGVKAL-DNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkGEPV------QFQDTMD 76
Cdd:PRK11819 325 IEAENLSKSF-GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVklayvdQSRDALD 400
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
269-474 |
3.02e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLfgmERF---DSGEVLIDGQPVI-IDSPS----VAIEKGMALLTEDRKKS 340
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALL---QNLyqpTGGQVLLDGVPLVqYDHHYlhrqVALVGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 341 GLFLVLSVMENMSIVNMPEYIGKSGFVkhMKMAQDCMEQIrrlniktptmDQIINNLSGGNQQKVLIARWLLAQPKILIL 420
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFI--MEFPNGYDTEV----------GEKGSQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 421 DEPTRGIDvgakAEIYHLISELANR-GVAVIMVSSELPeILGMSDRVMVMHEGRI 474
Cdd:TIGR00958 642 DEATSALD----AECEQLLQESRSRaSRTVLLIAHRLS-TVERADQILVLKKGSV 691
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-204 |
3.46e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPvqfqdTMDALRAGismihqelnLVPHMTVAE 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----ALIAISSG---------LNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 NIWLGREPMKygfVDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAH 179
Cdd:PRK13545 105 NIELKGLMMG---LTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|....*
gi 490997255 180 LFTIIRDLREQGKAIIYISHKMDEI 204
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
241-484 |
3.57e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 241 ELTQLFPKFNNTIGEEVLTVRNlsrkgyfeeVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViid 320
Cdd:COG1101 3 ELKNLSKTFNPGTVNEKRALDG---------LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 321 spsvaiekgmALLTEDRK-----------KSGLFLVLSVMENMSIVNMPeyiGKS---GFVKHMKMAQDCMEQIRRLNIK 386
Cdd:COG1101 71 ----------TKLPEYKRakyigrvfqdpMMGTAPSMTIEENLALAYRR---GKRrglRRGLTKKRRELFRELLATLGLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 387 TPT-MDQIINNLSGGNQQKV--LIArwLLAQPKILILDEPTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGM 462
Cdd:COG1101 138 LENrLDTKVGLLSGGQRQALslLMA--TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDY 215
|
250 260
....*....|....*....|..
gi 490997255 463 SDRVMVMHEGRItgILDKDEAD 484
Cdd:COG1101 216 GNRLIMMHEGRI--ILDVSGEE 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
397-453 |
3.59e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.05 E-value: 3.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLI-SELAnrGVAVIMVS 453
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELP--GTTVISVG 541
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
256-483 |
4.66e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.01 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 256 EVLTVRNLSRKGYFE---EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpviidspSVA--IEKGM 330
Cdd:COG1134 26 ELLLRRRRTRREEFWalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RVSalLELGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 ALLTEdrkksglflvLSVMEN----MSIVNMPEyigksgfvkhmkmaqdcmEQIRRLniktptMDQIIN----------- 395
Cdd:COG1134 98 GFHPE----------LTGRENiylnGRLLGLSR------------------KEIDEK------FDEIVEfaelgdfidqp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 396 --NLSGGNQqkvliARwlLA-------QPKILILDEptrGIDVG-----AKAeiYHLISELANRGVAVIMVSSELPEILG 461
Cdd:COG1134 144 vkTYSSGMR-----AR--LAfavatavDPDILLVDE---VLAVGdaafqKKC--LARIRELRESGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|..
gi 490997255 462 MSDRVMVMHEGRITGILDKDEA 483
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEEV 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
272-474 |
4.80e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpviIDSPSVAiekgmalLTEDRKKSGLFLVLSVMEN 351
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG----CDISKFG-------LMDLRKVLGIIPQAPVLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 MSI-VNMpeyigkSGFVKHMKMaqDCMEQIRRLNIKtptmDQIINN--------------LSGGNQQKVLIARWLLAQPK 416
Cdd:PLN03130 1327 GTVrFNL------DPFNEHNDA--DLWESLERAHLK----DVIRRNslgldaevseagenFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 417 ILILDEPTRGIDVGAKAEIYHLISElANRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
272-459 |
5.64e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.26 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPsvaiEKGMALLTEDRKKSGLFlVLSVMEN 351
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP----EIYRQQVSYCAQTPTLF-GDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 MSivnMPEYIGKSGfVKHMKMAQDCMeqirRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGA 431
Cdd:PRK10247 101 LI---FPWQIRNQQ-PDPAIFLDDLE----RFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180
....*....|....*....|....*....
gi 490997255 432 KAEIYHLISELA-NRGVAVIMVSSELPEI 459
Cdd:PRK10247 173 KHNVNEIIHRYVrEQNIAVLWVTHDKDEI 201
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
269-474 |
5.89e-09 |
|
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: 56.39 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 269 FEEVNFSVRRGEILGVAGLVGAGRSEVMESLfgmERF---DSGEVLIDGQpviiDSPSVAIEkgmalltEDRKKSG---- 341
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERFydpTSGEILLDGV----DIRDLNLR-------WLRSQIGlvsq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 342 ---LFLVlSVMENmsivnmpeyIGKSGFVKHMKMAqdcMEQIRRLNIktptmDQIINN---------------LSGGNQQ 403
Cdd:cd03249 85 epvLFDG-TIAEN---------IRYGKPDATDEEV---EEAAKKANI-----HDFIMSlpdgydtlvgergsqLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 404 KVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
270-473 |
5.99e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGME-----------RFDSgevlIDgqpVIIDSPSvaiekgmalltEDRK 338
Cdd:PRK15093 24 DRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwrvtadrmRFDD----ID---LLRLSPR-----------ERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 339 KSGLFLVLSVMENMSIVNMPEYIGKS------GFVKHMKMAQ-------DCMEQIRRLNIKTP--TMDQIINNLSGGNQQ 403
Cdd:PRK15093 86 LVGHNVSMIFQEPQSCLDPSERVGRQlmqnipGWTYKGRWWQrfgwrkrRAIELLHRVGIKDHkdAMRSFPYELTEGECQ 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 404 KVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGR 473
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
397-474 |
6.94e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 6.94e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-247 |
7.21e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.44 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 5 ALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAG--KSTLMKCLIGiyrPDKGAirvkgEPVQFQD---TMDALR 79
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR-----RPWRF*TwcaNRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 AGISmIHQELNLVPHMTVA--ENIWLGREPMKYGFVDHRQLARQtqtLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVS 157
Cdd:NF000106 85 RTIG-*HRPVR*GRRESFSgrENLYMIGR*LDLSRKDARARADE---LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 158 WNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISHKMDEIFAITDEISVFRDGTWVGSRQTGEftrqsLITQM 237
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE-----LKTKV 235
|
250
....*....|
gi 490997255 238 VGRELtQLFP 247
Cdd:NF000106 236 GGRTL-QIRP 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-217 |
8.83e-09 |
|
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: 55.50 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtMDALRAGISMIHQELNLVPHmTVA 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDLRSSLTIIPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENIwlgrEPM-KYGFVDHRQLARQTQTLLNklnirlsadrlvgeLSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEV 177
Cdd:cd03369 100 SNL----DPFdEYSDEEIYGALRVSEGGLN--------------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 178 AHLFTIIRDLReQGKAIIYISHKMDEIfAITDEISVFRDG 217
Cdd:cd03369 162 ALIQKTIREEF-TNSTILTIAHRLRTI-IDYDKILVMDAG 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-170 |
9.18e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 3 AFALEAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDtMDAlRAGI 82
Cdd:NF033858 264 EPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-IAT-RRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 83 SMIHQELNLVPHMTVAENIWLgrepmkygfvdHRQL--------ARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAK 154
Cdd:NF033858 342 GYMSQAFSLYGELTVRQNLEL-----------HARLfhlpaaeiAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170
....*....|....*.
gi 490997255 155 AVSWNADIVIMDEPTS 170
Cdd:NF033858 411 AVIHKPELLILDEPTS 426
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
279-474 |
9.31e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 9.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 279 GEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDrkksglflvLSVMENMSI---V 355
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-LESWSSKAFARKVAYLPQQ---------LPAAEGMTVrelV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 356 NMPEY-----IGKSGFVKHMKMAqdcmEQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVG 430
Cdd:PRK10575 107 AIGRYpwhgaLGRFGAADREKVE----EAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 431 AKAEIYHLISELAN-RGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK10575 182 HQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-429 |
9.46e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 9.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 10 GISKFFPGVKA-LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkgepvqfqdtMDALRAGISMihQE 88
Cdd:PRK11819 11 RVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP----------APGIKVGYLP--QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 89 LNLVPHMTVAENIWLGREP------------MKYGFVDHRQ---LARQTQ-----------TLLNKLNIRLSADRL---- 138
Cdd:PRK11819 79 PQLDPEKTVRENVEEGVAEvkaaldrfneiyAAYAEPDADFdalAAEQGElqeiidaadawDLDSQLEIAMDALRCppwd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 139 --VGELSIAAQQMVEIAKAVSWNADIVIMDEPTSAL-TESeVAHLftiIRDLREQGKAIIYISHkmDEIF---------- 205
Cdd:PRK11819 159 akVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLdAES-VAWL---EQFLHDYPGTVVAVTH--DRYFldnvagwile 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 206 ------------------------------------AITDEISvfrdgtWVGS----RQTGEFTRQSLITQMVGREltql 245
Cdd:PRK11819 233 ldrgrgipwegnysswleqkakrlaqeekqeaarqkALKRELE------WVRQspkaRQAKSKARLARYEELLSEE---- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 246 FPKFNNT----------IGEEVLTVRNLSrKGY-----FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEV 310
Cdd:PRK11819 303 YQKRNETneifippgprLGDKVIEAENLS-KSFgdrllIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 311 LIdGQPVII---DSPSVAIekgmallteDRKKsglflvlSVMENMS-----------IVNMPEYIGksgfvkhmkmaqdc 376
Cdd:PRK11819 382 KI-GETVKLayvDQSRDAL---------DPNK-------TVWEEISggldiikvgnrEIPSRAYVG-------------- 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 377 meqirRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:PRK11819 431 -----RFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-217 |
1.09e-08 |
|
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: 58.03 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGE----PVQFQDTMDALRagismihqelnlvphmt 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvPQQAWIQNDSLR----------------- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 vaENIWLGR--EPMKYgfvdhrQLARQTQTLLNKLNIRLSADRL-VGE----LSIAAQQMVEIAKAVSWNADIVIMDEPT 169
Cdd:TIGR00957 717 --ENILFGKalNEKYY------QQVLEACALLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490997255 170 SALTESEVAHLF--TIIRDLREQGKAIIYISHKMdEIFAITDEISVFRDG 217
Cdd:TIGR00957 789 SAVDAHVGKHIFehVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGG 837
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-278 |
1.20e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGiyrpdkgairvkgEPVQFQDTMDALRAGISMIHQeLNLVPHMTVAEN 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------------ELSHAETSSVVIRGSVAYVPQ-VSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 101 IWLGR--EPMKYGfvdhrqLARQTQTLLNKLNIRLSADRL-VGE----LSIAAQQMVEIAKAVSWNADIVIMDEPTSALt 173
Cdd:PLN03232 699 ILFGSdfESERYW------RAIDVTALQHDLDLLPGRDLTeIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL- 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 174 ESEVAH-LFTIIRDLREQGKAIIYISHK------MDEIFAITDEIsVFRDGTWVGSRQTGEFTrQSLITQMVGRELTQlf 246
Cdd:PLN03232 772 DAHVAHqVFDSCMKDELKGKTRVLVTNQlhflplMDRIILVSEGM-IKEEGTFAELSKSGSLF-KKLMENAGKMDATQ-- 847
|
250 260 270
....*....|....*....|....*....|..
gi 490997255 247 pkfnntigEEVLTVRNLSRKGYFEEVNFSVRR 278
Cdd:PLN03232 848 --------EVNTNDENILKLGPTVTIDVSERN 871
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
378-470 |
1.96e-08 |
|
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: 56.72 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 378 EQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELp 457
Cdd:COG1245 195 ELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL- 272
|
90
....*....|....
gi 490997255 458 EILGM-SDRVMVMH 470
Cdd:COG1245 273 AILDYlADYVHILY 286
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
272-474 |
2.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIidspsvaiEKGmalLTEDRKksglflVLSVMEN 351
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFG---LTDLRR------VLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 352 MSIVnmpeYIGK-----SGFVKHMKmaQDCMEQIRRLNIKtptmDQIINN--------------LSGGNQQKVLIARWLL 412
Cdd:PLN03232 1318 SPVL----FSGTvrfniDPFSEHND--ADLWEALERAHIK----DVIDRNpfgldaevseggenFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 413 AQPKILILDEPTRGIDVGAKAEIYHLISElANRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
270-474 |
2.38e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLfgmER-FD--SGEVLIDGqpviIDSPSVAIE---KGMALLTEDrkkSGLF 343
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLL---QRvFDpqSGRILIDG----TDIRTVTRAslrRNIAVVFQD---AGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 lVLSVMENMSIvnmpeyiGKSG-----FVKHMKMAQdCMEQIRRlniKTPTMDQII----NNLSGGNQQKVLIARWLLAQ 414
Cdd:PRK13657 422 -NRSIEDNIRV-------GRPDatdeeMRAAAERAQ-AHDFIER---KPDGYDTVVgergRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 415 PKILILDEPTRGIDVGAKAEIYHLISELA-NRGVAVImvSSELPEILGmSDRVMVMHEGRI 474
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMkGRTTFII--AHRLSTVRN-ADRILVFDNGRV 547
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-199 |
2.48e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.52 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIG-IYRPDkgaiRVKGEPVQFqDTMDALR-----------AGISMIH 86
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYPG----RVMAEKLEF-NGQDLQRisekerrnlvgAEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 87 QE--LNLVPHMTVAENIwlgREPMKYGFVDHRQLARQ-TQTLLNKLNIRLSADRL---VGELSIAAQQMVEIAKAVSWNA 160
Cdd:PRK11022 96 QDpmTSLNPCYTVGFQI---MEAIKVHQGGNKKTRRQrAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 161 DIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISH 199
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITH 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
396-474 |
2.65e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 2.65e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 396 NLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRgVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
396-490 |
3.18e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 396 NLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRIT 475
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRT 1437
|
90
....*....|....*
gi 490997255 476 GILDKDEADQETILS 490
Cdd:PTZ00265 1438 GSFVQAHGTHEELLS 1452
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
255-472 |
3.21e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 255 EEVLTVRNLS----RKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFD-----SGEVLIDGQPviIDSPSVA 325
Cdd:PRK14239 3 EPILQVSDLSvyynKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHN--IYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 326 IekgmallTEDRKKSGLFLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQ-IRRLNIKTPTMDQIINN---LSGGN 401
Cdd:PRK14239 81 T-------VDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKsLKGASIWDEVKDRLHDSalgLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 402 QQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRgVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-199 |
3.79e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.17 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 24 VSLRVRPGTVHALMGENGAGKSTLMKCLIGIYrPDKGAIRVKGEPVQfqdTMDA-----LRAGISmihQELNLVPHMTVA 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLE---AWSAaelarHRAYLS---QQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENIWLGREpmkygfvDHRQLArQTQTLLNKLNIRLSAD----RLVGELSIAAQQMVEIAKAV--SW-----NADIVIMDE 167
Cdd:PRK03695 88 QYLTLHQP-------DKTRTE-AVASALNEVAEALGLDdklgRSVNQLSGGEWQRVRLAAVVlqVWpdinpAGQLLLLDE 159
|
170 180 190
....*....|....*....|....*....|..
gi 490997255 168 PTSALTESEVAHLFTIIRDLREQGKAIIYISH 199
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
272-474 |
4.64e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.41 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSeVMESLFgmERF---DSGEVLIDGQPvIIDSPSVAIEKGMALLTEDRKksgLFlvlsv 348
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKS-TIANLL--TRFydiDEGEILLDGHD-LRDYTLASLRNQVALVSQNVH---LF----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 349 meNMSIVNMPEYIGKSGF-----VKHMKMAQdCMEQIRRLNIKTPTMdqIINN---LSGGNQQKVLIARWLLAQPKILIL 420
Cdd:PRK11176 430 --NDTIANNIAYARTEQYsreqiEEAARMAY-AMDFINKMDNGLDTV--IGENgvlLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 421 DEPTRGIDVGAKAEIYHLISEL-ANRGVAVImvSSELPEILGmSDRVMVMHEGRI 474
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELqKNRTSLVI--AHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-199 |
5.80e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGE----------PVQFQDTM-DALRAGISMI---- 85
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpPRNVEGTVyDFVAEGIEEQaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 86 ---HQELNLVPHMTVAENiwLGREPMKYGFVDHR---QLARQTQTLLNKLNirLSADRLVGELSIAAQQMVEIAKAVSWN 159
Cdd:PRK11147 99 kryHDISHLVETDPSEKN--LNELAKLQEQLDHHnlwQLENRINEVLAQLG--LDPDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490997255 160 ADIVIMDEPTSALTESEVAHLFTIIRDLreQGkAIIYISH 199
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISH 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-217 |
5.84e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 18 VKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPD---KGAIRVKG-EPVQFQDT-MDALRA-GISMIHQE--L 89
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGrEILNLPEKeLNKLRAeQISMIFQDpmT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 90 NLVPHMTVAENiwLGREPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLV---GELSIAAQQMVEIAKAVSWNADIVIMD 166
Cdd:PRK09473 109 SLNPYMRVGEQ--LMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490997255 167 EPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDG 217
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-199 |
6.84e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.81 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 2 NAFALEAEGISKFFPGVKAL-DNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRV-KGEPVQFqdtmdalr 79
Cdd:COG4178 359 EDGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLF-------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 80 agismIHQElnlvPHM---TVAENIWLGREPMKYgfvDHRQLAR-----QTQTLLNKLNIRLSADRlvgELSIAAQQMVE 151
Cdd:COG4178 431 -----LPQR----PYLplgTLREALLYPATAEAF---SDAELREaleavGLGHLAERLDEEADWDQ---VLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490997255 152 IAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDlREQGKAIIYISH 199
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
275-468 |
7.72e-08 |
|
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: 53.18 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 275 SVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDG-------QPVIIDSPSVAiekgMALLTEDRKKSGlflvls 347
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKADYEGTV----RDLLSSITKDFY------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 vmenmsivNMPEYigKSGFVKHMKMaqdcmEQIrrlniktptMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGI 427
Cdd:cd03237 91 --------THPYF--KTEIAKPLQI-----EQI---------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 428 DVGAKAEIYHLISELA-NRGVAVIMVSSELPEILGMSDRVMV 468
Cdd:cd03237 147 DVEQRLMASKVIRRFAeNNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
272-474 |
1.17e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.09 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSgevlIDGQPVIIDSPSVAIEKGMAL-LTEDRKKSG-------LF 343
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK----SAGSHIELLGRTVQREGRLARdIRKSRANTGyifqqfnLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 344 LVLSVMENMSIvnmpEYIGKSGFVK------HMKMAQDCMEQIRRLNIkTPTMDQIINNLSGGNQQKVLIARWLLAQPKI 417
Cdd:PRK09984 99 NRLSVLENVLI----GALGSTPFWRtcfswfTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 418 LILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
397-474 |
1.33e-07 |
|
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: 54.06 E-value: 1.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELPEILGmSDRVMVMHEGRI 474
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-199 |
1.44e-07 |
|
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: 51.00 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIrvkGEPVqfqdtmdalRAGISMIHQElnlvPHMTvaen 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPE---------GEDLLFLPQR----PYLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 101 iwLG--REpmkygfvdhrQLARQTQTllnklnirlsadrlvgELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVA 178
Cdd:cd03223 77 --LGtlRE----------QLIYPWDD----------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 490997255 179 HLFTIirdLREQGKAIIYISH 199
Cdd:cd03223 129 RLYQL---LKELGITVISVGH 146
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
270-472 |
2.14e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPViiDSPSVaiEKGMALLTEdrkksGLFLVLSVM 349
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--EGPGA--ERGVVFQNE-----GLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIVNMPEYIGKSgfvKHMKMAQDCMEQI-------RRlniktptmdqiINNLSGGNQQKVLIARWLLAQPKILILDE 422
Cdd:PRK11248 89 DNVAFGLQLAGVEKM---QRLEIAHQMLKKVglegaekRY-----------IWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 423 PTRGIDVGAKAEIYHLISELANR-GVAVIMVSSELPEILGMSDRVMVMHEG 472
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
397-492 |
2.47e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.05 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITG 476
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
90
....*....|....*.
gi 490997255 477 ILDKDEADQETILSLA 492
Cdd:PRK13647 219 EGDKSLLTDEDIVEQA 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-208 |
2.47e-07 |
|
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: 53.80 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQFQDTMDaLRAGISMIHQE---------LNL 91
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDpvlfsgslrMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 92 VPHMTVA-ENIWLGREPMK-YGFVdhrqlarqtQTLLNKLNIRLSADrlvGE-LSIAAQQMVEIAKAVSWNADIVIMDEP 168
Cdd:TIGR00957 1381 DPFSQYSdEEVWWALELAHlKTFV---------SALPDKLDHECAEG---GEnLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490997255 169 TSALtESEVAHLftIIRDLREQGK--AIIYISHKMDEIFAIT 208
Cdd:TIGR00957 1449 TAAV-DLETDNL--IQSTIRTQFEdcTVLTIAHRLNTIMDYT 1487
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-217 |
2.53e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPD--KGAIRVKGEPVQFQdTMDalRAGisMIHQELNLVPHMTVA 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ-ILK--RTG--FVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENI---WLGREPmkygfvdhRQLARQTQTLL-----NKLNIRLSADRLVGE-----LSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:PLN03211 159 ETLvfcSLLRLP--------KSLTKQEKILVaesviSELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490997255 166 DEPTSALTESEVAHLFTIIRDLREQGKAIIYISHK-MDEIFAITDEISVFRDG 217
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-217 |
2.56e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIG--IYRPDKGAIRVKGEPVQFQDTMDALRAGISMIHQELNLVPHMTVA 98
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQYPIEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENIWLG----REPMKYGFVDHRQLARQTQTLLNKLNIRLS-ADRLVGE-LSIAAQQMVEIAKAVSWNADIVIMDEPTSAL 172
Cdd:CHL00131 103 DFLRLAynskRKFQGLPELDPLEFLEIINEKLKLVGMDPSfLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 173 tesEVAHLFTI---IRDLREQGKAIIYISHK---MDEIfaITDEISVFRDG 217
Cdd:CHL00131 183 ---DIDALKIIaegINKLMTSENSIILITHYqrlLDYI--KPDYVHVMQNG 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
378-469 |
2.84e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 378 EQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELP 457
Cdd:PRK13409 195 EVVERLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLA 272
|
90
....*....|...
gi 490997255 458 eILGM-SDRVMVM 469
Cdd:PRK13409 273 -VLDYlADNVHIA 284
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
270-474 |
3.51e-07 |
|
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: 52.82 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPvIIDSPSVAIEKGMALLTEDRkksgLFLVLSVM 349
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDIDRHTLRQFINYLPQEP----YIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 350 ENMSIVNMPeyigksgfvkhmKMAQDCMEQIRRL-NIKtptmDQIIN--------------NLSGGNQQKVLIARWLLAQ 414
Cdd:TIGR01193 566 ENLLLGAKE------------NVSQDEIWAACEIaEIK----DDIENmplgyqtelseegsSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490997255 415 PKILILDEPTRGIDVGAKAEIyhlISELAN-RGVAVIMVSSELpEILGMSDRVMVMHEGRI 474
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKI---VNNLLNlQDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
387-474 |
4.50e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.54 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 387 TPTMDQIINnLSGGNQQKVLIARWLLAQPKILILDEPTRGIDvgAKAEiYHLISEL--ANRGVAVIMVSSELPEILGMsD 464
Cdd:PRK11174 477 TPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSE-QLVMQALnaASRRQTTLMVTHQLEDLAQW-D 551
|
90
....*....|
gi 490997255 465 RVMVMHEGRI 474
Cdd:PRK11174 552 QIWVMQDGQI 561
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
254-472 |
5.88e-07 |
|
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: 51.01 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNLSRKG--YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpvIIDSPSVA-IEKGm 330
Cdd:cd03291 36 DDNNLFFSNLCLVGapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQFSwIMPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 alltedrkksglflvlSVMENMSI-VNMPEYIGKSgFVKHMKMAQDCMeqirrlniKTPTMDQIIN-----NLSGGNQQK 404
Cdd:cd03291 113 ----------------TIKENIIFgVSYDEYRYKS-VVKACQLEEDIT--------KFPEKDNTVLgeggiTLSGGQRAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 405 VLIARWLLAQPKILILDEPTRGIDVGAKAEIYH--LISELANRgvAVIMVSSELpEILGMSDRVMVMHEG 472
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKLMANK--TRILVTSKM-EHLKKADKILILHEG 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
257-476 |
7.76e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 257 VLTVRNL----SRKGYFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFD--SGEVLIDGQPVIIDSPsvaiekgm 330
Cdd:CHL00131 7 ILEIKNLhasvNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEP-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 alltEDRKKSGLFLVLSVMENMSIVNMPEYIGKSGFVKHMKMAQDCMEQIRRLNIKTP-----TMDQIINN------LSG 399
Cdd:CHL00131 79 ----EERAHLGIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEklklvGMDPSFLSrnvnegFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 400 GNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVsSELPEILG--MSDRVMVMHEGRI--T 475
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLDyiKPDYVHVMQNGKIikT 233
|
.
gi 490997255 476 G 476
Cdd:CHL00131 234 G 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
378-470 |
8.22e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 378 EQIRRLNIKtPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELp 457
Cdd:cd03236 122 ELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL- 199
|
90
....*....|....
gi 490997255 458 EILGM-SDRVMVMH 470
Cdd:cd03236 200 AVLDYlSDYIHCLY 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-227 |
9.02e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 16 PGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRV-----KGEPVQFQD----------------- 73
Cdd:PTZ00265 1179 PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehTNDMTNEQDyqgdeeqnvgmknvnef 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 74 -------------------------------TMDALRAGISMIHQELNLVpHMTVAENIWLGREPM---------KYGFV 113
Cdd:PTZ00265 1259 sltkeggsgedstvfknsgkilldgvdicdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDAtredvkracKFAAI 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 114 DHRqlarqTQTLLNKLnirlsaDRLVG----ELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDLRE 189
Cdd:PTZ00265 1338 DEF-----IESLPNKY------DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490997255 190 QG-KAIIYISHKMDEIfAITDEISVF----RDGTWVGSRQTGE 227
Cdd:PTZ00265 1407 KAdKTIITIAHRIASI-KRSDKIVVFnnpdRTGSFVQAHGTHE 1448
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-204 |
1.34e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 20 ALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpvqfqdtmdalragISMIHQELNLVPHMTVAE 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 100 NIWLGREPMKYgfvDHRQLARQTQTLLNKLNIRLSADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAH 179
Cdd:PRK13546 105 NIEFKMLCMGF---KRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180
....*....|....*....|....*
gi 490997255 180 LFTIIRDLREQGKAIIYISHKMDEI 204
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVSHNLGQV 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
254-472 |
1.40e-06 |
|
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: 51.06 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 254 GEEVLTVRNLSRKG--YFEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQpvIIDSPSVA-IEKGm 330
Cdd:TIGR01271 425 GDDGLFFSNFSLYVtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTSwIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 331 alltedrkksglflvlSVMENMSI-VNMPEYIGKSgFVKHMKMAQDCMEQIRRlnIKTPTMDQIINnLSGGNQQKVLIAR 409
Cdd:TIGR01271 502 ----------------TIKDNIIFgLSYDEYRYTS-VIKACQLEEDIALFPEK--DKTVLGEGGIT-LSGGQRARISLAR 561
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 410 WLLAQPKILILDEPTRGIDVGAKAEIYH--LISELANRgvAVIMVSSELpEILGMSDRVMVMHEG 472
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-195 |
1.49e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 27 RVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVQfqdTMDALRAgISMIHQELNLVPHMTVAENIwlgre 106
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRF-MAYLGHLPGLKADLSTLENL----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 107 pmkyGFVDHRQLARQTQTLLNKLNI-RLS--ADRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTI 183
Cdd:PRK13543 104 ----HFLCGLHGRRAKQMPGSALAIvGLAgyEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|...
gi 490997255 184 IR-DLREQGKAII 195
Cdd:PRK13543 180 ISaHLRGGGAALV 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
272-493 |
1.94e-06 |
|
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: 50.71 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFG-MERFDsGEVLIDGqpviidspSVAIEKGMALLTEDrkksglflvlSVME 350
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVE-GHVHMKG--------SVAYVPQQAWIQND----------SLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMsivnmpeYIGKSGFVKHMKMAQDCMEQIRRLNIkTPTMDQI-IN----NLSGGNQQKVLIARWLLAQPKILILDEPTR 425
Cdd:TIGR00957 718 NI-------LFGKALNEKYYQQVLEACALLPDLEI-LPSGDRTeIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 426 GIDVGAKAEIY-HLISE---LANRG-VAVIMVSSELPEIlgmsDRVMVMHEGRIT------GILDKDEADQETILSLAS 493
Cdd:TIGR00957 790 AVDAHVGKHIFeHVIGPegvLKNKTrILVTHGISYLPQV----DVIIVMSGGKISemgsyqELLQRDGAFAEFLRTYAP 864
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
396-473 |
3.61e-06 |
|
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: 47.85 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 396 NLSGGNQQKVLIARWLLAQPKILILDEPTRGID--VGAKaeIY-HLISELANRGVAVIMVSSELpEILGMSDRVMVMHEG 472
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDahVGRH--IFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
.
gi 490997255 473 R 473
Cdd:cd03250 204 R 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-87 |
4.71e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 4.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGI--YRPDKGAIRVKGEPVQFQDTMDALRAGISMIHQ 87
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQ 85
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-309 |
5.73e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 133 LSADRLVGELSIAAQQMVEIAKAVSwnADIV----IMDEPTSALTESEVAHLFTIIRDLREQGKAIIYISH--KM----D 202
Cdd:PRK00635 468 LTPERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHdeQMislaD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 203 EIFAITDEISVFrDGTWVGSRQTGEF--TRQSLITQMVGRELTQLFP-KFNNTIGEEVL---TVRNLsrkgyfEEVNFSV 276
Cdd:PRK00635 546 RIIDIGPGAGIF-GGEVLFNGSPREFlaKSDSLTAKYLRQELTIPIPeKRTNSLGTLTLskaTKHNL------KDLTISL 618
|
170 180 190
....*....|....*....|....*....|....*
gi 490997255 277 RRGEILGVAGLVGAGRSEVMESLF--GMERFDSGE 309
Cdd:PRK00635 619 PLGRLTVVTGVSGSGKSSLINDTLvpAVEEFIEQG 653
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
398-482 |
7.42e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 398 SGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHEGRITGI 477
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
....*
gi 490997255 478 LDKDE 482
Cdd:NF000106 226 GKVDE 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
389-469 |
7.55e-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: 46.16 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 389 TMDQIINNLSGGNQQKVLIARWLLAQPK--ILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSElPEILGMSDRV 466
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
...
gi 490997255 467 MVM 469
Cdd:cd03238 159 IDF 161
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-177 |
7.71e-06 |
|
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: 48.75 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpvqfqdtmdalragISMIHQELNLVPHmT 96
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGREPMKYGF---VDHRQLARQTQTLLNKLNIRLSADRLVgeLSIAAQQMVEIAKAVSWNADIVIMDEPTSAL- 172
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYtsvIKACQLEEDIALFPEKDKTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFTHLd 580
|
....*..
gi 490997255 173 --TESEV 177
Cdd:TIGR01271 581 vvTEKEI 587
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
397-451 |
8.05e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 8.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIM 451
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
271-474 |
9.60e-06 |
|
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: 48.40 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGqpviIDSPSVAIEKGMALLTEDRKKSGLFlvlSVME 350
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----LNIAKIGLHDLRFKITIIPQDPVLF---SGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMSIVNMPEYIGKS-----------GFVKHM--KMAQDCMEQIRrlniktptmdqiinNLSGGNQQKVLIARWLLAQPKI 417
Cdd:TIGR00957 1377 RMNLDPFSQYSDEEvwwalelahlkTFVSALpdKLDHECAEGGE--------------NLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 418 LILDEPTRGIDVGAKAEIYHLISELANrGVAVIMVSSELPEILGMSdRVMVMHEGRI 474
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
258-474 |
1.30e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 258 LTVRNLsRKGY------FEEVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiEKGMA 331
Cdd:PRK11650 4 LKLQAV-RKSYdgktqvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 332 LLTEDrkkSGLFLVLSVMENMS----IVNMPEyigksgfvkhmkmaqdcmEQIRR--------LNIkTPTMDQIINNLSG 399
Cdd:PRK11650 80 MVFQN---YALYPHMSVRENMAyglkIRGMPK------------------AEIEErvaeaariLEL-EPLLDRKPRELSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 400 GNQQKVLIARWLLAQPKILILDEPTRGID----VGAKAEIYHLISELanrGVAVIMVSSELPEILGMSDRVMVMHEGRI 474
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
397-472 |
1.56e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.70 E-value: 1.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVI-MVSSELPEILGMSDRVMVMHEG 472
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
392-475 |
1.57e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 392 QIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAkaeIYHLISELANRGVAVIMVSSELPEILGMSDRVMVMHE 471
Cdd:PLN03073 623 QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
....
gi 490997255 472 GRIT 475
Cdd:PLN03073 700 GKVT 703
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-177 |
1.87e-05 |
|
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: 46.39 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEpvqfqdtmdalragISMIHQELNLVPHmT 96
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 97 VAENIWLGREPMKYGF---VDHRQLARQTQTLLNKLNIRLSADRLVgeLSIAAQQMVEIAKAVSWNADIVIMDEPTSAL- 172
Cdd:cd03291 114 IKENIIFGVSYDEYRYksvVKACQLEEDITKFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGYLd 191
|
....*..
gi 490997255 173 --TESEV 177
Cdd:cd03291 192 vfTEKEI 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-101 |
1.88e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 7 EAEGISKFFPGVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRV--KGEPVQFqdtmDALRAgism 84
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtKLEVAYF----DQHRA---- 392
|
90
....*....|....*..
gi 490997255 85 ihqelNLVPHMTVAENI 101
Cdd:PRK11147 393 -----ELDPEKTVMDNL 404
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-220 |
2.09e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.23 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 6 LEAEGISKFFPGVkALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPD----KGAIRVKGEPVQFQDtmdaLRA- 80
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCA----LRGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 81 GISMIHQE----LNlvPHMTVAENiwlGREPMkygfvdhRQLARQT--QTLLNKL------NIRLSADRLVGELSIAAQQ 148
Cdd:PRK10418 80 KIATIMQNprsaFN--PLHTMHTH---ARETC-------LALGKPAddATLTAALeavgleNAARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 149 MVEIAKAVSWNADIVIMDEPTSALTESEVAHLFTIIRDL-REQGKAIIYISHKMDEIFAITDEISVFRDGTWV 220
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
17-111 |
2.15e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGEPVqfqDTMDALRAGISMIHQELNLVPHMT 96
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPADRDIAMVFQNYALYPHMS 92
|
90
....*....|....*
gi 490997255 97 VAENiwlgrepMKYG 111
Cdd:PRK11650 93 VREN-------MAYG 100
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
391-474 |
2.48e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 391 DQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELAN--RGVAVIMVSSELPEILGMSDRVMV 468
Cdd:TIGR00956 204 NDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSQDAYELFDKVIV 283
|
....*.
gi 490997255 469 MHEGRI 474
Cdd:TIGR00956 284 LYEGYQ 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-172 |
2.87e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVkgepvqfqdtmdaLRAGISMIHQeLNLVPHMTVAEN 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-------------IRGTVAYVPQ-VSWIFNATVRDN 698
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490997255 101 IWLGR--EPMKYGFVDHRQLARQTQTLLNKLNIRLSADRLVgELSIAAQQMVEIAKAVSWNADIVIMDEPTSAL 172
Cdd:PLN03130 699 ILFGSpfDPERYERAIDVTALQHDLDLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
391-429 |
3.13e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 3.13e-05
10 20 30
....*....|....*....|....*....|....*....
gi 490997255 391 DQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDV 429
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
271-472 |
5.21e-05 |
|
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: 44.63 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 271 EVNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSVAIEKGMALLTEDRKKSGLfLVLSVME 350
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-LNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMSIvnmpeyigKSGFVKH-MKMAQDCMEQIRRLNIkTPTMDQI-IN----NLSGGNQQKVLIARWLLAQPKILILDEPT 424
Cdd:cd03290 98 NITF--------GSPFNKQrYKAVTDACSLQPDIDL-LPFGDQTeIGergiNLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 425 RGIDVgakaeiyHLISELANRGV---------AVIMVSSELpEILGMSDRVMVMHEG 472
Cdd:cd03290 169 SALDI-------HLSDHLMQEGIlkflqddkrTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-202 |
6.31e-05 |
|
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: 45.67 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 17 GVKALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDkGAIRVKGepVQFQD-TMDALRAGISMIHQEL------ 89
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG--VSWNSvTLQTWRKAFGVIPQKVfifsgt 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 90 ---NLVPHMTVA-ENIWlgrepmkyGFVDHRQLARQTQTLLNKLNIRLSADRLVgeLSIAAQQMVEIAKAVSWNADIVIM 165
Cdd:TIGR01271 1308 frkNLDPYEQWSdEEIW--------KVAEEVGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490997255 166 DEPTsaltesevAHL----FTIIRDLREQGKA---IIYISHKMD 202
Cdd:TIGR01271 1378 DEPS--------AHLdpvtLQIIRKTLKQSFSnctVILSEHRVE 1413
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-96 |
6.68e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 6.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 21 LDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRV-KGEPVQF--QDTMDALRAGISMIHQELNLVPHMT 96
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYfaQHQLEFLRADESPLQHLARLAPQEL 406
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
395-459 |
7.76e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 7.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997255 395 NNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGVAVIMVSSELPEI 459
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTI 643
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
121-199 |
7.88e-05 |
|
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: 43.47 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 121 QTQTLLnKLNIR-LSADRLVGELSIAAQQMVEIAK--AVSWNADIVIMDEPTSALTESEVAHLFTIIRDLREQGKAIIYI 197
Cdd:cd03238 67 QLQFLI-DVGLGyLTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
|
..
gi 490997255 198 SH 199
Cdd:cd03238 146 EH 147
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-199 |
9.60e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 19 KALDNVSLRVRPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIRVKGepvqfQDTMDALRAGISMIHQELNLVPHMTVA 98
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN-----CNINNIAKPYCTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 99 ENIWLGREpmKYGFVDHRQLARQTQTLLNKLnirlsaDRLVGELSIAAQQMVEIAKAVSWNADIVIMDEPTSALTESEVA 178
Cdd:PRK13541 89 ENLKFWSE--IYNSAETLYAAIHYFKLHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180
....*....|....*....|.
gi 490997255 179 HLFTIIRDLREQGKAIIYISH 199
Cdd:PRK13541 161 LLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
270-474 |
4.32e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 270 EEVNFSVRRGEILGVAGLVGAGRSEVMESLfgMERFD--SGEVLIDGQPViidsPSVAIEKGMALLTEDRKKSGLFlVLS 347
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDvsEGDIRFHDIPL----TKLQLDSWRSRLAVVSQTPFLF-SDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 348 VMENMSIvnmpeyiGKSGfvkhmkMAQDCMEQIRRL-NIKtptmDQIIN--------------NLSGGNQQKVLIARWLL 412
Cdd:PRK10789 405 VANNIAL-------GRPD------ATQQEIEHVARLaSVH----DDILRlpqgydtevgergvMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490997255 413 AQPKILILDEPTRGIDVGAKAEIYHLISELAnRGVAVIMVSSELpEILGMSDRVMVMHEGRI 474
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRL-SALTEASEILVMQHGHI 527
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
358-470 |
4.34e-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: 41.02 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 358 PEYIGKSGFVKHMKMAQDCMEQIRRLNIKTPTMDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYH 437
Cdd:cd03222 33 PNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR 112
|
90 100 110
....*....|....*....|....*....|....
gi 490997255 438 LISELANRGV-AVIMVSSELPEILGMSDRVMVMH 470
Cdd:cd03222 113 AIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
402-472 |
4.73e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 4.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490997255 402 QQKVL-IARWLLAQPKILI-LDEPTRGIDVGAKAEIYHLISELANRGVAvIMVSSELPEILGMS--DRVMVMHEG 472
Cdd:TIGR00956 906 QRKRLtIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQA-ILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
112-204 |
5.49e-04 |
|
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: 41.83 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 112 FVDHRQLARQTQTLLNklnIRLSADRL---VGELSIAAQQMVEIAKAVSWNAD---IVIMDEPTSALTESEVAHLFTIIR 185
Cdd:cd03271 140 FENIPKIARKLQTLCD---VGLGYIKLgqpATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQ 216
|
90
....*....|....*....
gi 490997255 186 DLREQGKAIIYISHKMDEI 204
Cdd:cd03271 217 RLVDKGNTVVVIEHNLDVI 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
396-474 |
6.30e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 6.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997255 396 NLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVSSELpEILGMSDRVMVMHEGRI 474
Cdd:PLN03232 740 NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-208 |
8.86e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 38 GENGAGKSTLMKCL-------------IGIYRPD---KGAIR---------VKGEPVQFQDTMDALRAGIsMIHQElnlv 92
Cdd:cd03240 29 GQNGAGKTTIIEALkyaltgelppnskGGAHDPKlirEGEVRaqvklafenANGKKYTITRSLAILENVI-FCHQG---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 93 phmtvaENIWLgrepmkygFVDHRQlarqtqtllnklniRLSA-DRLVGELSIAaqqmVEIAKAVSWNADIVIMDEPTSA 171
Cdd:cd03240 104 ------ESNWP--------LLDMRG--------------RCSGgEKVLASLIIR----LALAETFGSNCGILALDEPTTN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490997255 172 LTESEVAH-LFTIIRDLREQG-KAIIYISH------KMDEIFAIT 208
Cdd:cd03240 152 LDEENIEEsLAEIIEERKSQKnFQLIVITHdeelvdAADHIYRVE 196
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
112-204 |
9.25e-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: 41.92 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 112 FVDHRQLARQTQTL----LNKLNIRLSADRLVGelsiAAQQMVEIAKAVSWNAD---IVIMDEPTSALTESEVAHLFTII 184
Cdd:TIGR00630 800 FEAVPSISRKLQTLcdvgLGYIRLGQPATTLSG----GEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVL 875
|
90 100
....*....|....*....|
gi 490997255 185 RDLREQGKAIIYISHKMDEI 204
Cdd:TIGR00630 876 QRLVDKGNTVVVIEHNLDVI 895
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
272-485 |
9.62e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 272 VNFSVRRGEILGVAGLVGAGRSEVMESLFGMERFDSGEVLIDGQPVIIDSPSvaiekgmalltEDRKK-SGLFLVLSVME 350
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-----------DYRKLfSAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 351 NMsivnmpeyIGKSGFVKHMKMAQDCMEQIrRLNIKTPTMDQIINN--LSGGNQQKV--LIArwLLAQPKILILDEPTRG 426
Cdd:PRK10522 411 QL--------LGPEGKPANPALVEKWLERL-KMAHKLELEDGRISNlkLSKGQKKRLalLLA--LAEERDILLLDEWAAD 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 427 IDVGAKAEIYH-LISELANRGVAVIMVSSElPEILGMSDRVMVMHEGRITGiLDKDEADQ 485
Cdd:PRK10522 480 QDPHFRREFYQvLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE-LTGEERDA 537
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
18-63 |
3.09e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.92 E-value: 3.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490997255 18 VKALDNVSLRV-----RPGTVHALMGENGAGKSTLMKCLIGIYRPDKGAIR 63
Cdd:PRK01889 177 VSALDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
396-474 |
3.30e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 396 NLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYH--LISELanRGVAVIMVSSELpEILGMSDRVMVMHEGR 473
Cdd:PLN03130 740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDEL--RGKTRVLVTNQL-HFLSQVDRIILVHEGM 816
|
.
gi 490997255 474 I 474
Cdd:PLN03130 817 I 817
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
394-453 |
5.22e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 5.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997255 394 INNLSGGNQQKVLIARWLLAQPK---ILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVS 453
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTT 296
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
390-457 |
5.74e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 5.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997255 390 MDQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGvAVIMVSSELP 457
Cdd:PRK13541 117 LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSG-GIVLLSSHLE 183
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
379-474 |
6.43e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 379 QIRRLNIKTPTM--DQIINNLSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISELANRGVAVIMVS--S 454
Cdd:PLN03140 317 KILGLDICKDTIvgDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllQ 396
|
90 100
....*....|....*....|
gi 490997255 455 ELPEILGMSDRVMVMHEGRI 474
Cdd:PLN03140 397 PAPETFDLFDDIILLSEGQI 416
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
397-476 |
6.76e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.34 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLISEL-ANRGvavimvsselpeilGMS------------ 463
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERP--------------GMSvlvataymeeae 202
|
90
....*....|....*..
gi 490997255 464 --DRVMVMHEGRI--TG 476
Cdd:NF033858 203 rfDWLVAMDAGRVlaTG 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
397-453 |
7.63e-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: 38.96 E-value: 7.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490997255 397 LSGGNQQKVLIARWLLAQPKILILDEPTRGIDVGAKAEIYHLiseLANRGVAVIMVS 453
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL---CREFGITLFSVS 636
|
|
| |
