|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-500 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 653.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvALVPGLSIAENIMLDRLAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFL 165
Cdd:COG1129 85 HQEL--NLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKMLGHELS 245
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRELE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 246 DIFPPKRPPhSDEVLLQVEGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGE--LNSQPWRPR 323
Cdd:COG1129 243 DLFPKRAAA-PGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD--PADSGEirLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 324 DPADSVARGLALVPEERRKEGIFIEEPVAMNLAVSADSSFSRWSLFGHRQAWRWAEEVIARVGIRTSGPAQTLRRLSGGN 403
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 404 QQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGA 483
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDRE 479
|
490
....*....|....*..
gi 503994372 484 EAREENILYYSTGGAAA 500
Cdd:COG1129 480 EATEEAIMAAATGGAAA 496
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-499 |
4.40e-149 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 435.90 E-value: 4.40e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAH--YEGEVVINNQSVSIRSPRDAK 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 79 QLGIHLVQQEVdvALVPGLSIAENIMLDRLAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARAL 158
Cdd:PRK13549 81 RAGIAIIHQEL--ALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEK 238
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 239 MLGHELSDIFPpkRPPHS-DEVLLQVEGL---HDEG----LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRL 310
Cdd:PRK13549 239 MVGRELTALYP--REPHTiGEVILEVRNLtawDPVNphikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 311 TrGE--LNSQPWRPRDPADSVARGLALVPEERRKEGIFIEEPVAMNLAVSADSSFSRWSLFGHRQAWRWAEEVIARVGIR 388
Cdd:PRK13549 317 E-GEifIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 389 TSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRI 468
Cdd:PRK13549 396 TASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRV 475
|
490 500 510
....*....|....*....|....*....|.
gi 503994372 469 CVLWDGRIVAEIPGAEAREENILYYSTGGAA 499
Cdd:PRK13549 476 LVMHEGKLKGDLINHNLTQEQVMEAALRSEH 506
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-490 |
1.34e-146 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 429.45 E-value: 1.34e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQEVdvALVPGLSIAENIMLDRLAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSH 160
Cdd:COG3845 81 GIGMVHQHF--MLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKML 240
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 241 GHELSDIfPPKRPPHSDEVLLQVEGLH---DEGL--LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE- 314
Cdd:COG3845 239 GREVLLR-VEKAPAEPGEVVLEVENLSvrdDRGVpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP--PASGSi 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 315 -LNSQPWRPRDPADSVARGLALVPEERRKEGIFIEEPVAMNLAVSA--DSSFSRWSLFGHRQAWRWAEEVIARVGIRTSG 391
Cdd:COG3845 316 rLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRyrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 392 PAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVL 471
Cdd:COG3845 396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVM 475
|
490
....*....|....*....
gi 503994372 472 WDGRIVAEIPGAEAREENI 490
Cdd:COG3845 476 YEGRIVGEVPAAEATREEI 494
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-491 |
3.78e-145 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 425.48 E-value: 3.78e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDvaLVPGLSIAENIMLDRLAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFL 165
Cdd:PRK11288 85 YQELH--LVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGP-MADLSGEQIVEKMLGHEL 244
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdMAQVDRDQLVQAMVGREI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 245 SDIFPpKRPPHSDEVLLQVEGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRD 324
Cdd:PRK11288 243 GDIYG-YRPRPLGEVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 325 PADSVARGLALVPEERRKEGIFIEEPVAMNLAVSADSSFSRWSLFGHRqawRW----AEEVIARVGIRTSGPAQTLRRLS 400
Cdd:PRK11288 322 PRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINN---RWeaenADRFIRSLNIKTPSREQLIMNLS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 401 GGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEI 480
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGEL 478
|
490
....*....|.
gi 503994372 481 PGAEAREENIL 491
Cdd:PRK11288 479 AREQATERQAL 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-493 |
4.61e-137 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 404.94 E-value: 4.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAH--YEGEVVINNQSVSIRSPRDAKQLGIH 83
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQEVdvALVPGLSIAENIML-DRLAEPGIaFRWGRLRQLAREALAQldVSLDvrrsIDSCTLAE-----KQQIL-LAR 156
Cdd:NF040905 82 IIHQEL--ALIPYLSIAENIFLgNERAKRGV-IDWNETNRRARELLAK--VGLD----ESPDTLVTdigvgKQQLVeIAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPM--ADLSGEQ 234
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCraDEVTEDR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 235 IVEKMLGHELSDIFPPkRPPHSDEVLLQVEG------LH-DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASK 307
Cdd:NF040905 233 IIRGMVGRDLEDRYPE-RTPKIGEVVFEVKNwtvyhpLHpERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 308 SRLTRGE--LNSQPWRPRDPADSVARGLALVPEERRKEGIFIEEPVAMNLAVSADSSFSRWSLFGHRQAWRWAEEVIARV 385
Cdd:NF040905 312 GRNISGTvfKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 386 GIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLC 465
Cdd:NF040905 392 NIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMC 471
|
490 500
....*....|....*....|....*...
gi 503994372 466 DRICVLWDGRIVAEIPGAEAREENILYY 493
Cdd:NF040905 472 DRIYVMNEGRITGELPREEASQERIMRL 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-491 |
1.18e-132 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 393.60 E-value: 1.18e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDvaLVPGLSIAENIMLDRlaEPGIAF---RWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHC 162
Cdd:PRK10762 85 HQELN--LIPQLTIAENIFLGR--EFVNRFgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 163 RFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKMLGH 242
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 243 ELSDIFPPKRPPHSdEVLLQVEGLHDEGlLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQPW 320
Cdd:PRK10762 241 KLEDQYPRLDKAPG-EVRLKVDNLSGPG-VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPR--TSGYvtLDGHEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 321 RPRDPADSVARGLALVPEERRKEGIFIEEPVAMNLAVSADSSFSRWSLFGHRQAWRWA-EEVIARVGIRTSGPAQTLRRL 399
Cdd:PRK10762 317 VTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAvSDFIRLFNIKTPSMEQAIGLL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 400 SGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
490
....*....|..
gi 503994372 480 IPGAEAREENIL 491
Cdd:PRK10762 477 FTREQATQEKLM 488
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-498 |
5.59e-132 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 392.23 E-value: 5.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQEVDValVPGLSIAENIMLDRLAEPGI----AFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLAR 156
Cdd:PRK09700 81 GIGIIYQELSV--IDELTVLENLYIGRHLTKKVcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIV 236
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 237 EKMLGHELSDIFPPKRPPHSD---EVLLQVEGL--HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLT 311
Cdd:PRK09700 239 RLMVGRELQNRFNAMKENVSNlahETVFEVRNVtsRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 312 RGELNSQPWRPRDPADSVARGLALVPEERRKEGIFIEEPVAMNLAVSADSSFSR----WSLFGHRQAWRWAEEVIARVGI 387
Cdd:PRK09700 319 EIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGykgaMGLFHEVDEQRTAENQRELLAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 388 RTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDR 467
Cdd:PRK09700 399 KCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDR 478
|
490 500 510
....*....|....*....|....*....|..
gi 503994372 468 ICVLWDGRIVAEIPG-AEAREENILYYSTGGA 498
Cdd:PRK09700 479 IAVFCEGRLTQILTNrDDMSEEEIMAWALPQE 510
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-500 |
8.93e-120 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 360.91 E-value: 8.93e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvALVPGLSIAENIMLdRLAEPGIAFRwgRLRQLareaLAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFL 165
Cdd:PRK15439 92 PQEP--LLFPNLSVKENILF-GLPKRQASMQ--KMKQL----LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKM----LG 241
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAItpaaRE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 242 HELSDI------FPPKRPPHS-DEVLLQVEGLHDEGlLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGE 314
Cdd:PRK15439 243 KSLSASqklwleLPGNRRQQAaGAPVLTVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 315 LNSQPWRPRDPADSVARGLALVPEERRKEGIFIEEPVAMNLAvsadssfsrwSLFGHRQAWrWA---------EEVIARV 385
Cdd:PRK15439 322 LNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC----------ALTHNRRGF-WIkparenavlERYRRAL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 386 GIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLC 465
Cdd:PRK15439 391 NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMA 470
|
490 500 510
....*....|....*....|....*....|....*
gi 503994372 466 DRICVLWDGRIVAEIPGAEAREENILYYSTGGAAA 500
Cdd:PRK15439 471 DRVLVMHQGEISGALTGAAINVDTIMRLAFGEHQA 505
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-491 |
6.62e-119 |
|
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: 358.37 E-value: 6.62e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAH--YEGEVVINNQSVSIRSPRDAKQLGIH 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQEVdvALVPGLSIAENIML-DRLAEPGIAFRWGRLRQLAREALAQLDVSLD-VRRSIDSCTLAEKQQILLARALSHH 161
Cdd:TIGR02633 82 IIHQEL--TLVPELSVAENIFLgNEITLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKMLG 241
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 242 HELSDIFPpkRPPHS-DEVLLQVEGL--HD-----EGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLtRG 313
Cdd:TIGR02633 240 REITSLYP--HEPHEiGDVILEARNLtcWDvinphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF-EG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 314 E--LNSQPWRPRDPADSVARGLALVPEERRKEGIFIEEPVAMNLAVSADSSFSRWSLFGHRQAWRWAEEVIARVGIRTSG 391
Cdd:TIGR02633 317 NvfINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTAS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 392 PAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVL 471
Cdd:TIGR02633 397 PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
490 500
....*....|....*....|
gi 503994372 472 WDGRIVAEIPGAEAREENIL 491
Cdd:TIGR02633 477 GEGKLKGDFVNHALTQEQVL 496
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-491 |
1.88e-118 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 357.12 E-value: 1.88e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 8 MQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLVQQ 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 88 EVDvaLVPGLSIAENIMLDRLAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLIL 167
Cdd:PRK10982 81 ELN--LVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 168 DEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKMLGHELSDI 247
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 248 FPPK--RPphsDEVLLQVEGLHD--EGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPR 323
Cdd:PRK10982 239 FPDKenKP---GEVILEVRNLTSlrQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 324 DPADSVARGLALVPEERRKEGIFIEEPVAMNLAVS-ADSSFSRWSLFGHRQAWRWAEEVIARVGIRTSGPAQTLRRLSGG 402
Cdd:PRK10982 316 NANEAINHGFALVTEERRSTGIYAYLDIGFNSLISnIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 403 NQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPG 482
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDT 475
|
....*....
gi 503994372 483 AEAREENIL 491
Cdd:PRK10982 476 KTTTQNEIL 484
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
258-476 |
4.43e-69 |
|
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: 218.84 E-value: 4.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 258 EVLLQVEGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE--LNSQPWRPRDPADSVARGLAL 335
Cdd:cd03215 2 EPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP--PASGEitLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 336 VPEERRKEGIFIEEPVAMNLAVSadssfsrwslfghrqawrwaeeviarvgirtsgpaqtlRRLSGGNQQKVAIGKWLRG 415
Cdd:cd03215 80 VPEDRKREGLVLDLSVAENIALS--------------------------------------SLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 416 NANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRI 476
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 |
3.82e-62 |
|
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: 199.96 E-value: 3.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevdvalvpgLSIAEnimldrlaepgiafrwgrlrqlarealaqldvsldvrrsidsctlaeKQQILLARALSHHCRFL 165
Cdd:cd03216 81 YQ---------LSVGE-----------------------------------------------RQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLI 222
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-484 |
1.05e-55 |
|
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: 193.97 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG--FRALSNVAFTLTGGSVHALTGANGAGKSTL-MAV--LCGTHAHYEGEVVINNQSVSIRSPRDAKQL 80
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLaLALmgLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 gIHLVQQEVDVALVPgLSIAENImldrlAEPGIAFRWGR--LRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARAL 158
Cdd:COG1123 85 -IGMVFQDPMTQLNP-VTVGDQI-----AEALENLGLSRaeARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVE 237
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 238 KMLGHELSDIFPPKRPPHSDEVLLQVEGLH-------DEGL--LQDISLRLRKGEILGIAGLAGAGKTELCKALFGAskS 308
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvrgKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL--L 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 309 RLTRGE--LNSQPWRPRDPAD--SVARGLALV---PE----ERRKEGIFIEEPVAMNLAVSAdssfsrwslfghRQAWRW 377
Cdd:COG1123 316 RPTSGSilFDGKDLTKLSRRSlrELRRRVQMVfqdPYsslnPRMTVGDIIAEPLRLHGLLSR------------AERRER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 378 AEEVIARVGIrtsgPAQTLRR----LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVI 452
Cdd:COG1123 384 VAELLERVGL----PPDLADRypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYL 459
|
490 500 510
....*....|....*....|....*....|..
gi 503994372 453 YASGEFAELVGLCDRICVLWDGRIVAEIPGAE 484
Cdd:COG1123 460 FISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-229 |
3.99e-42 |
|
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: 149.89 E-value: 3.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevDVALVPGLSIAENIML---DRLAEPGIAFRWGR----LRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARAL 158
Cdd:cd03219 81 FQ--IPRLFPELTVLENVMVaaqARTGSGLLLARARReereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMAD 229
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-244 |
5.12e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.13 E-value: 5.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIhLV 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY-VP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QqevDVALVPGLSIAENI-MLDRLAEpgiaFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRF 164
Cdd:COG1131 80 Q---EPALYPDLTVRENLrFFARLYG----LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 165 LILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSG---EQIVEKMLG 241
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKArllEDVFLELTG 232
|
...
gi 503994372 242 HEL 244
Cdd:COG1131 233 EEA 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-229 |
1.29e-38 |
|
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: 141.33 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEvdVALVPGLSIAENIMLDRLAEPGIAF---------RWGRLRQLAREALAQLD-VSLDVRRSIDSCTLAEKQQILL- 154
Cdd:COG0411 85 FQN--PRLFPELTVLENVLVAAHARLGRGLlaallrlprARREEREARERAEELLErVGLADRADEPAGNLSYGQQRRLe 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 155 -ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMAD 229
Cdd:COG0411 163 iARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-230 |
2.22e-38 |
|
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: 140.56 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGih 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARRIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQEVDVAlvPGLSIAENIMLDRLAEPGIAFRWGR-LRQLAREALAQLDVSLDVRRSIDscTLA--EKQQILLARALSH 160
Cdd:COG1120 79 YVPQEPPAP--FGLTVRELVALGRYPHLGLFGRPSAeDREAVEEALERTGLEHLADRPVD--ELSggERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-248 |
1.21e-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: 135.37 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIhlV 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvALVPGLSIAENIMLdrlaepgiafrWGRLRQLAREALA--------QLDVSLDVRRSIDSCTLAEKQQILLARA 157
Cdd:COG4555 80 PDER--GLYDRLTVRENIRY-----------FAELYGLFDEELKkrieelieLLGLEEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 158 LSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSgEQIVE 237
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR-EEIGE 225
|
250
....*....|.
gi 503994372 238 KmlghELSDIF 248
Cdd:COG4555 226 E----NLEDAF 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-247 |
4.93e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirspRDAKQL 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GiHLVQQEVDVALVPgLSIAENIMLDRLAEPGIAFRWGR-LRQLAREALAQLDVSLDVRRSIDscTLA--EKQQILLARA 157
Cdd:COG1121 78 G-YVPQRAEVDWDFP-ITVRDVVLMGRYGRRGLFRRPSRaDREAVDEALERVGLEDLADRPIG--ELSggQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 158 LSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLrDGRLIESGPMADLSGEQIVE 237
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLS 232
|
250
....*....|
gi 503994372 238 KMLGHELSDI 247
Cdd:COG1121 233 RAYGGPVALL 242
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-230 |
2.20e-35 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 131.69 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFS-GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGI- 82
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 ------HLVQQEV--DVALVP---GLSIAEnimldrlaepgiafrwgrLRQLAREALAQLDVS--LDvrRSIDSCTLAEK 149
Cdd:COG1122 81 fqnpddQLFAPTVeeDVAFGPenlGLPREE------------------IRERVEEALELVGLEhlAD--RPPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 150 QQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMAD 229
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
.
gi 503994372 230 L 230
Cdd:COG1122 221 V 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-230 |
3.98e-35 |
|
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: 137.34 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-----SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL 80
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 G--IHLVQQEVDVALVPGLSIAENImldrlAEPGIAFRWGR---LRQLAREALAQLDVSLDVR-RSIDSCTLAEKQQILL 154
Cdd:COG1123 341 RrrVQMVFQDPYSSLNPRMTVGDII-----AEPLRLHGLLSraeRRERVAELLERVGLPPDLAdRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-221 |
1.30e-33 |
|
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: 124.82 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIhLV 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY-LP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QqevDVALVPGLSIAENIMLdrlaepgiafrwgrlrqlarealaqldvsldvrrsidscTLAEKQQILLARALSHHCRFL 165
Cdd:cd03230 80 E---EPSLYENLTVRENLKL---------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-225 |
3.75e-33 |
|
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: 124.95 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRdakqlgIHLVQ 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 87 Q--EVDVALvPgLSIAENIMLDRLAEPGIAFRWGRL-RQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCR 163
Cdd:cd03235 75 QrrSIDRDF-P-ISVRDVVLMGLYGHKGLFRRLSKAdKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 164 FLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLrDGRLIESG 225
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-245 |
1.58e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.15 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGIhl 84
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQEVDVALvpGLSIAENIMLDRLAEPGIAfrwGRLRQLAREALAQLDVSLDVRRSIdsCTLA--EKQQILLARAL---- 158
Cdd:COG4559 80 LPQHSSLAF--PFTVEEVVALGRAPHGSSA---AQDRQIVREALALVGLAHLAGRSY--QTLSggEQQRVQLARVLaqlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 159 ---SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFIshrIHELK---AVCDTLTVLRDGRLIESGPMADLSG 232
Cdd:COG4559 153 epvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAV---LHDLNlaaQYADRILLLHQGRLVAQGTPEEVLT 229
|
250
....*....|...
gi 503994372 233 EQIVEKMLGHELS 245
Cdd:COG4559 230 DELLERVYGADLR 242
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-220 |
4.33e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 119.49 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSGFR--ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGih 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQ-----------EVDVALVPglsiaENIMLDRlaepgiafrwGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQI 152
Cdd:cd03225 79 LVFQnpddqffgptvEEEVAFGL-----ENLGLPE----------EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 153 LLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGR 220
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-221 |
7.24e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 7.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLgIHLV 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvALVPGlSIAENimldrLAEPGIAFRWGRLRQLAREALAQLDVSLDV-RRSIDSCTLAEKQQILLARALSHHCRF 164
Cdd:COG4619 80 PQEP--ALWGG-TVRDN-----LPFPFQLRERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 165 LILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-225 |
3.17e-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: 117.24 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRdakQLGIHLV 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevDVALVPGLSIAENIM--LDRLAEPGiafrwGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCR 163
Cdd:cd03259 78 FQ--DYALFPHLTVAENIAfgLKLRGVPK-----AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 164 FLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-230 |
1.07e-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: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFS----GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlG 81
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 IHLVQQEVDVALVPGLSIAenimlDRLAEPGIAFRWGRLRQLAREALAQLDVSLDVRR------SIdsctlAEKQQILLA 155
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVD-----RILAEPLRIHGLPDREERIAELLEQVGLPPSFLDryphqlSG-----GQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 156 RALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-230 |
1.16e-29 |
|
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: 115.61 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDValVPGLSIAENIMLDRLAEPGIAFRWGRLRQLAR-EALAQldvsldvRRSIDSCTLA--EKQQILLARALSHHC 162
Cdd:cd03224 81 PEGRRI--FPELTVEENLLLGAYARRRAKRKARLERVYELfPRLKE-------RRKQLAGTLSggEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 163 RFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-241 |
1.24e-29 |
|
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: 116.23 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDValVPGLSIAENIMLdrlaepgiAFRWGRLRQLAREALAQLdvsLDV------RRSIDSCTLA--EKQQILLARA 157
Cdd:COG0410 84 PEGRRI--FPSLTVEENLLL--------GAYARRDRAEVRADLERV---YELfprlkeRRRQRAGTLSggEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 158 LSHHCRFLILDEPT---APLDQnesERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSG-E 233
Cdd:COG0410 151 LMSRPKLLLLDEPSlglAPLIV---EEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAdP 227
|
....*...
gi 503994372 234 QIVEKMLG 241
Cdd:COG0410 228 EVREAYLG 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-234 |
1.47e-29 |
|
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: 121.79 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGih 83
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRRQIA-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQevDVALVPGlSIAENImldRLAEPGIAfrWGRLRQLAREA-----LAQLDVSLDVRrsidsctLAE---------K 149
Cdd:COG4988 415 WVPQ--NPYLFAG-TIRENL---RLGRPDAS--DEELEAALEAAgldefVAALPDGLDTP-------LGEggrglsggqA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 150 QQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLqRQGIGIVFISHRIHELKAvCDTLTVLRDGRLIESGPMAD 229
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
....*
gi 503994372 230 LSGEQ 234
Cdd:COG4988 558 LLAKN 562
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-230 |
2.79e-29 |
|
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: 121.86 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFR--ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLG 81
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 ihLVQQEVDvaLVPGlSIAENImldRLAEPGIAFRwgRLRQLAREA-----LAQLDVSLDVRrsidsctLAE-------- 148
Cdd:COG2274 553 --VVLQDVF--LFSG-TIRENI---TLGDPDATDE--EIIEAARLAglhdfIEALPMGYDTV-------VGEggsnlsgg 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 149 -KQQILLARALSHHCRFLILDEPTAPLDqNESERlfAVVRRLQR--QGIGIVFISHRiHELKAVCDTLTVLRDGRLIESG 225
Cdd:COG2274 616 qRQRLAIARALLRNPRILILDEATSALD-AETEA--IILENLRRllKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDG 691
|
....*
gi 503994372 226 PMADL 230
Cdd:COG2274 692 THEEL 696
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-230 |
4.36e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 118.41 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLgihlv 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 qqevdVALVP-GLSIAENIMLDRLAEPGIAFRWGRL-------RQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARA 157
Cdd:PRK09536 79 -----VASVPqDTSLSFEFDVRQVVEMGRTPHRSRFdtwtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 158 LSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-225 |
5.27e-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: 112.53 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQlgihlv 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElARK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 qqevdVALVPglsiaenimldrlaepgiafrwgrlrqlarEALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFL 165
Cdd:cd03214 75 -----IAYVP------------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
261-488 |
6.92e-29 |
|
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: 113.68 E-value: 6.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADSVARGLALV 336
Cdd:cd03224 1 LEVENLNagygKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 337 PEERRkegIFIEEPVAMNLAVSAdssfsrWSLFGHRQAWRWaEEVIA---RVGIRTSGPAQTlrrLSGGNQQKVAIGKWL 413
Cdd:cd03224 81 PEGRR---IFPELTVEENLLLGA------YARRRAKRKARL-ERVYElfpRLKERRKQLAGT---LSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 414 RGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAEAREE 488
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-220 |
1.06e-28 |
|
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: 111.18 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlgihlvq 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 87 qevDVALVPGLSiaenimldrlaePGiafrwgrlrqlarealaqldvsldvrrsidsctlaEKQQILLARALSHHCRFLI 166
Cdd:cd00267 74 ---RIGYVPQLS------------GG-----------------------------------QRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 167 LDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGR 220
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-221 |
1.77e-28 |
|
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: 111.37 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAfsgfRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHL 84
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQE-VDVALVPGLSIAENIMLDRLAEPGiafrwgrlrqlarealaqldvsldvrrsidsctlaeKQQ-ILLARALSHHC 162
Cdd:cd03215 80 VPEDrKREGLVLDLSVAENIALSSLLSGG------------------------------------NQQkVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 163 RFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-225 |
2.28e-28 |
|
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: 111.93 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPRDAKQLGIHLV 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevdvALVPGLSIAENIMLDRLAepgiafrWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFL 165
Cdd:cd03268 80 AP----GFYPNLTARENLRLLARL-------LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-242 |
4.65e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.05 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLA-FSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIH 83
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQE-VDVALVPGLSIAENIMLDRLAEPGIA----FRWGRLRQLAREALAQLDVSLdvrRSIDscTLAEK------QQI 152
Cdd:COG3845 337 YIPEDrLGRGLVPDMSVAENLILGRYRRPPFSrggfLDRKAIRAFAEELIEEFDVRT---PGPD--TPARSlsggnqQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 153 LLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSG 232
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491
|
250
....*....|
gi 503994372 233 EQIVEKMLGH 242
Cdd:COG3845 492 EEIGLLMAGV 501
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-225 |
9.51e-28 |
|
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: 110.67 E-value: 9.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLG 81
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 --IHLVQQEVDVALVPGLSIAENImldrlAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSI-----DSCTLAEKQQILL 154
Cdd:cd03257 82 keIQMVFQDPMSSLNPRMTIGEQI-----AEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlnrypHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 155 ARALSHHCRFLILDEPTAPLD---QNESERLFavvRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDvsvQAQILDLL---KKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
272-500 |
6.96e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.61 E-value: 6.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQPwrPRDPADSVARGLALVPEERrkeGIFIEE 349
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP--TSGEvrVLGED--VARDPAEVRRRIGYVPQEP---ALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 350 PVAMNLAVSADssfsrwsLFGH--RQAWRWAEEVIARVGIrTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTK 427
Cdd:COG1131 89 TVRENLRFFAR-------LYGLprKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 428 GVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAEARE---ENILYYSTGGAAA 500
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKArllEDVFLELTGEEAR 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
258-484 |
1.40e-26 |
|
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: 107.38 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 258 EVLLQVEGLH---DEGL-LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGE--LNSQPWRPRDPADSVAR 331
Cdd:COG0410 1 MPMLEVENLHagyGGIHvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL--PPRSGSirFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 332 GLALVPEERRkegIF----IEEpvamNLAVSAdssFSRwslfGHRQAWRWA-EEVIA---RVGIRTSGPAQTLrrlSGGN 403
Cdd:COG0410 79 GIGYVPEGRR---IFpsltVEE----NLLLGA---YAR----RDRAEVRADlERVYElfpRLKERRRQRAGTL---SGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 404 QQKVAIGKWLRGNANVLIFDEPTKG-----VDvkaktDLFNAIDGLAREGKGVIyasgefaeLV--------GLCDRICV 470
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTIL--------LVeqnarfalEIADRAYV 208
|
250
....*....|....
gi 503994372 471 LWDGRIVAEIPGAE 484
Cdd:COG0410 209 LERGRIVLEGTAAE 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-237 |
2.21e-26 |
|
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: 107.27 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL--GI 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQevDVALVPGLSIAENIMLDRLAE----PGIAFRWGRL-RQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARA 157
Cdd:cd03256 81 GMIFQ--QFNLIERLSVLENVLSGRLGRrstwRSLFGLFPKEeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 158 LSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIV 236
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
.
gi 503994372 237 E 237
Cdd:cd03256 239 E 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-479 |
3.56e-26 |
|
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: 104.05 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE--LNSQPWRPRDPADSVARGLALVPEerrkegifiee 349
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK--PDSGEilVDGKEVSFASPRDARRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 350 pvamnlavsadssfsrwslfghrqawrwaeeviarvgirtsgpaqtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGV 429
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503994372 430 DVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-221 |
4.12e-26 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 105.65 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD----- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 AKQLGIhlVQQevDVALVPGLSIAENIMLdrlaePGIAF--RWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILL 154
Cdd:cd03255 81 RRHIGF--VFQ--SFNLLPDLTALENVEL-----PLLLAgvPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRiHELKAVCDTLTVLRDGRL 221
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
272-478 |
4.96e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 105.31 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGELNSQPwrpRDPADSVARgLALVPEERRKEGIF---IE 348
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK--PTSGSIRVFG---KPLEKERKR-IGYVPQRRSIDRDFpisVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 EPVAMNLavsadssFSRWSLFGH--RQAWRWAEEVIARVGIrtSGPA-QTLRRLSGGNQQKVAIGKWLRGNANVLIFDEP 425
Cdd:cd03235 89 DVVLMGL-------YGHKGLFRRlsKADKAKVDEALERVGL--SELAdRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 426 TKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRIcVLWDGRIVA 478
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVA 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-477 |
5.14e-26 |
|
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: 111.31 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKS-TLMAV---LCGTHAHYEGEVVINNQSVSIR 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrlLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 73 SPRDAKQL---GIHLVQQEVDVALVP----GLSIAENIMLDRlaepgiAFRWGRLRQLAREALAQldVSL-DVRRSIDS- 143
Cdd:COG4172 82 SERELRRIrgnRIAMIFQEPMTSLNPlhtiGKQIAEVLRLHR------GLSGAAARARALELLER--VGIpDPERRLDAy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 144 ---CTLAEKQQILLARALSHHCRFLILDEPTAPLD---QNESERLfavVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVL 216
Cdd:COG4172 154 phqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvQAQILDL---LKDLQRElGMALLLITHDLGVVRRFADRVAVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 217 RDGRLIESGPMADL--SGEQIVEKMLgheLSDI--FPPKRPPHSDEVLLQVEGLH-----DEGLLQ----------DISL 277
Cdd:COG4172 231 RQGEIVEQGPTAELfaAPQHPYTRKL---LAAEprGDPRPVPPDAPPLLEARDLKvwfpiKRGLFRrtvghvkavdGVSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 278 RLRKGEILGIAGLAGAGKTELCKAL------------FGASKSRLTRGELnsQPWRPR------DP----------ADSV 329
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLGLALlrlipsegeirfDGQDLDGLSRRAL--RPLRRRmqvvfqDPfgslsprmtvGQII 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 330 ARGLALV-PEERRKEgifIEEPVAmnlavsadssfsrwslfghrqawrwaeEVIARVGIrtsgPAQTLRR----LSGGNQ 404
Cdd:COG4172 386 AEGLRVHgPGLSAAE---RRARVA---------------------------EALEEVGL----DPAARHRypheFSGGQR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 405 QKVAIGKWLRGNANVLIFDEPTKGVDV---KAKTDLFNAidgLAREGK----------GVIYAsgefaelvgLCDRICVL 471
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVsvqAQILDLLRD---LQREHGlaylfishdlAVVRA---------LAHRVMVM 499
|
....*.
gi 503994372 472 WDGRIV 477
Cdd:COG4172 500 KDGKVV 505
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-209 |
7.63e-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: 104.48 E-value: 7.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGI-- 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HlvqqevDVALVPGLSIAENIMLdrlaepgiafrWGRLRQL------AREALAQLDVS--LDVRrsIDSCTLAEKQQILL 154
Cdd:COG4133 82 H------ADGLKPELTVRENLRF-----------WAALYGLradreaIDEALEAVGLAglADLP--VRQLSAGQKRRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAV 209
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA 197
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-220 |
1.46e-25 |
|
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: 102.85 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGF--RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLgIH 83
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQevDVALVPGlSIAENIMldrlaePGiafrwGrlrqlarealaqldvsldvrrsidsctlaEKQQILLARALSHHCR 163
Cdd:cd03228 80 YVPQ--DPFLFSG-TIRENIL------SG-----G-----------------------------QRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 164 FLILDEPTAPLDqNESE-RLFAVVRRLqRQGIGIVFISHRIHELKAvCDTLTVLRDGR 220
Cdd:cd03228 117 ILILDEATSALD-PETEaLILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-223 |
2.45e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.97 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF----SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD----- 76
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 AKQLGIhlVQQevDVALVPGLSIAENIMLdrlaePGIAFRWGR--LRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILL 154
Cdd:COG1136 85 RRHIGF--VFQ--FFNLLPELTALENVAL-----PLLLAGVSRkeRRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRiHELKAVCDTLTVLRDGRLIE 223
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-244 |
2.45e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGIhL 84
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAV-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQevdVALVPGLSIAENIMLDRLaePGiAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARAL------ 158
Cdd:PRK13548 82 PQH---SSLSFPFTVEEVVAMGRA--PH-GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVE 237
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLR 235
|
....*..
gi 503994372 238 KMLGHEL 244
Cdd:PRK13548 236 RVYGADV 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-477 |
3.27e-25 |
|
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: 108.74 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAH--YEGEVVINnqsVSI-----------R 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYH---VALcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 73 SPRDAKQLGIHLVQQEVDV-----------------------ALVPGLSIAENIMLdrlAEPGIAFRWGRLRQLAREALA 129
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFwnlsdklrrrirkriaimlqrtfALYGDDTVLDNVLE---ALEEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 130 QLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKA 208
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 209 VCDTLTVLRDGRLIESGpmadlSGEQIVEKMLghELSDIFPPKRPPHSDEVLLQVEGLH------DEGLLQ---DISLRL 279
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEG-----TPDEVVAVFM--EGVSEVEKECEVEVGEPIIKVRNVSkryisvDRGVVKavdNVSLEV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 280 RKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELN---SQPWrprdpADSVARGLALVPEERRKEGIFIEEpvamnla 356
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEP--TSGEVNvrvGDEW-----VDMTKPGPDGRGRAKRYIGILHQE------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 357 vsadssfsrWSLFGHRQ-----------------AWRWAEEVIARVGIRTSGPAQTLRR----LSGGNQQKVAIGKWLRG 415
Cdd:TIGR03269 374 ---------YDLYPHRTvldnlteaiglelpdelARMKAVITLKMVGFDEEKAEEILDKypdeLSEGERHRVALAQVLIK 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 416 NANVLIFDEPTKGVDVKAKTDLFNAIDGlARE--GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILK-AREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-225 |
3.33e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.33 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGIhL 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLAL-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQEvdvaLVP-GLSIAENIMLDRlaEPGIAFrWGRL----RQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALS 159
Cdd:PRK11231 82 PQHH----LTPeGITVRELVAYGR--SPWLSL-WGRLsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
272-476 |
7.80e-25 |
|
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: 100.94 E-value: 7.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE--LNSQPwrPRDPADSVARGLALVPEERrkegifiee 349
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK--PDSGEikVLGKD--IKKEPEEVKRRIGYLPEEP--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 350 pvamnlavsadssfsrwSLFGHRQAWrwaeEVIarvgirtsgpaqtlrRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGV 429
Cdd:cd03230 83 -----------------SLYENLTVR----ENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503994372 430 DVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRI 476
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
272-478 |
7.99e-25 |
|
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: 101.97 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSQpWRPRDPADSvaRGLALVPEERrkeGIFIEEPV 351
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP--DSGEVLFD-GKPLDIAAR--NRIGYLPEER---GLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 AMNLAVsadssFSRWSLFGHRQAWRWAEEVIARVGIRTSGpAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDV 431
Cdd:cd03269 88 IDQLVY-----LAQLKGLKKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503994372 432 kAKTDLF-NAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:cd03269 162 -VNVELLkDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
272-485 |
8.39e-25 |
|
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: 102.41 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQPWRPRDPADsVARGLALV---PEERrkegIF 346
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP--TSGEvlVDGKDITKKNLRE-LRRKVGLVfqnPDDQ----LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 ---IEEPVA---MNLAVSADssfsrwslfghrQAWRWAEEVIARVGIrtsgpaQTLR-----RLSGGNQQKVAIgkwlrg 415
Cdd:COG1122 90 aptVEEDVAfgpENLGLPRE------------EIRERVEEALELVGL------EHLAdrpphELSGGQKQRVAI------ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 416 nA-------NVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAEA 485
Cdd:COG1122 146 -AgvlamepEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-230 |
1.09e-24 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 102.27 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL- 80
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 -GIHLVQQEVDvaLVPGLSIAENIMLD-RLAEPGIAFRWGRLRQLareaLAQLDVSLDVRRSIDSCTLAEKQQILLARAL 158
Cdd:cd03258 82 rRIGMIFQHFN--LLSSRTVFENVALPlEIAGVPKAEIEERVLEL----LELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-245 |
2.41e-24 |
|
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: 101.70 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG-THAHYEGEVVINNQ---SVSIRSPRdaKQLG 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGErrgGEDVWELR--KRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 IhlVQQEVDVALVPGLSIAENIM------LDRLAEPGiafrwGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLA 155
Cdd:COG1119 82 L--VSPALQLRFPRDETVLDVVLsgffdsIGLYREPT-----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 156 RALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQG-IGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQ 234
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSE 234
|
250
....*....|.
gi 503994372 235 IVEKMLGHELS 245
Cdd:COG1119 235 NLSEAFGLPVE 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
256-490 |
4.59e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 100.55 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 256 SDEVLLQVEGL----HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGELNsqpwRPRDPADSVAR 331
Cdd:COG1121 2 MMMPAIELENLtvsyGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP--PTSGTVR----LFGKPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 332 GLALVPEERRKEGIF---IEEPVAMNLavsadssFSRWSLFG--HRQAWRWAEEVIARVGIrtSGPA-QTLRRLSGGNQQ 405
Cdd:COG1121 76 RIGYVPQRAEVDWDFpitVRDVVLMGR-------YGRRGLFRrpSRADREAVDEALERVGL--EDLAdRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 406 KVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLwDGRIVAEIPGAEA 485
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEV 225
|
....*.
gi 503994372 486 -REENI 490
Cdd:COG1121 226 lTPENL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-225 |
9.21e-24 |
|
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: 98.80 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGsVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPRDAKQLgIHLV 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDValVPGLSIAEniMLDRLAE-PGIAFRwgRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRF 164
Cdd:cd03264 78 PQEFGV--YPNFTVRE--FLDYIAWlKGIPSK--EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 165 LILDEPTAPLDQNESERlfavVRR-LQRQGIGIVFI--SHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03264 152 LIVDEPTAGLDPEERIR----FRNlLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-225 |
1.08e-23 |
|
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: 98.89 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIrsprDAKQLGIHLV 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEvdvALVPGLSIAENIM-LDRLAepGIAFRWGRLRqlAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRF 164
Cdd:cd03269 77 EER---GLYPKMKVIDQLVyLAQLK--GLKKEEARRR--IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 165 LILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-219 |
1.76e-23 |
|
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: 98.10 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 10 NISLAFS-GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAkqlgIHLVQQE 88
Cdd:cd03226 4 NISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS----IGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 89 VDVALVpGLSIAENIML--DRLAEPGiafrwgrlrQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLI 166
Cdd:cd03226 80 VDYQLF-TDSVREELLLglKELDAGN---------EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 167 LDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDG 219
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-230 |
1.77e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 103.69 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 2 TGNRLEMQNISLAFSG--FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQ 79
Cdd:COG4987 330 GGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 80 LgIHLVQQEVDV--AlvpglSIAENImldRLAEPGIAFRwgRLRQLAREA-----LAQLDVSLDVRRSIDSCTLA--EKQ 150
Cdd:COG4987 410 R-IAVVPQRPHLfdT-----TLRENL---RLARPDATDE--ELWAALERVglgdwLAALPDGLDTWLGEGGRRLSggERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 151 QILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLqRQGIGIVFISHRIHELKAVcDTLTVLRDGRLIESGPMADL 230
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEEL 556
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-221 |
1.83e-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: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRA--LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirsPRDAKQLGIH 83
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS---QWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 L--VQQevDVALVPGlSIAENIMldrlaepgiafrwgrlrqlarealaqldvsldvrrsidscTLAEKQQILLARALSHH 161
Cdd:cd03246 78 VgyLPQ--DDELFSG-SIAENIL----------------------------------------SGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIhELKAVCDTLTVLRDGRL 221
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-225 |
2.96e-23 |
|
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: 97.82 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFS----GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPRDAKQ-L 80
Cdd:cd03266 2 ITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEARRrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHlvqqEVDVALVPGLSIAENIMLdrlaepgiafrWGRLRQLAR-EALAQLDV---SLDVRRSID----SCTLAEKQQI 152
Cdd:cd03266 81 GFV----SDSTGLYDRLTARENLEY-----------FAGLYGLKGdELTARLEEladRLGMEELLDrrvgGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 153 LLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-426 |
3.12e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 8 MQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVInnqsvsirsPRDAKqlgIHLVQQ 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR---IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 88 EVDvaLVPGLSIAENIM---------LDRLAEPGIAF--------RWGRLRQL------------AREALAQLDVS-LDV 137
Cdd:COG0488 69 EPP--LDDDLTVLDTVLdgdaelralEAELEELEAKLaepdedleRLAELQEEfealggweaearAEEILSGLGFPeEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 138 RRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDqneserLFAVV---RRLQRQGIGIVFISHRIHELKAVCDTLT 214
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIEwleEFLKNYPGTVLVVSHDRYFLDRVATRIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 215 VLRDGRLIE-SGPMAD------------LSGEQIVEKMLGHELSDI--FPPK--------------------RPPHSDEV 259
Cdd:COG0488 221 ELDRGKLTLyPGNYSAyleqraerleqeAAAYAKQQKKIAKEEEFIrrFRAKarkakqaqsrikaleklereEPPRRDKT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 --------------LLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKS---RLTRG----- 313
Cdd:COG0488 301 veirfppperlgkkVLELEGLSksygDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPdsgTVKLGetvki 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 314 --------ELNSQpwrpRDPADSVARGLalvPEERRKEgifieepvAMNLAvsadSSFsrwsLFGHRQAWRwaeeviaRV 385
Cdd:COG0488 381 gyfdqhqeELDPD----KTVLDELRDGA---PGGTEQE--------VRGYL----GRF----LFSGDDAFK-------PV 430
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 503994372 386 GirtsgpaqtlrRLSGGNQQKVAIGKWLRGNANVLIFDEPT 426
Cdd:COG0488 431 G-----------VLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
4.05e-23 |
|
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: 97.74 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 ----GIhLVQQEvdvALVPGLSIAENIML-----DRLAEPGIafrwgrlRQLAREALAQldVSLDvrrsiDSCTL--AE- 148
Cdd:COG1127 81 rrriGM-LFQGG---ALFDSLTVFENVAFplrehTDLSEAEI-------RELVLEKLEL--VGLP-----GAADKmpSEl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 149 ----KQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIE 223
Cdd:COG1127 143 sggmRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
....*..
gi 503994372 224 SGPMADL 230
Cdd:COG1127 223 EGTPEEL 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-172 |
4.83e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 95.02 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlGIHLVQQevDVALVPGLSIA 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQ--DPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 101 ENIMldrlaEPGIAFRWGRLRQLAR--EALAQLDVSLDVRRSIDS--CTLA--EKQQILLARALSHHCRFLILDEPTA 172
Cdd:pfam00005 78 ENLR-----LGLLLKGLSKREKDARaeEALEKLGLGDLADRPVGErpGTLSggQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
8-241 |
5.07e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 98.32 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 8 MQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV-SIRSPRDAKQLGiHLVQ 86
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKAFARKVA-YLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 87 QevdVALVPGLSIAENIMLDRLAEPGIAFRWGRL-RQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFL 165
Cdd:PRK10575 93 Q---LPAAEGMTVRELVAIGRYPWHGALGRFGAAdREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKMLG 241
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-225 |
5.74e-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: 96.98 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 23 NVAFTLTGGSVhALTGANGAGKSTLMAVLCGTHAHYEGEVVIN-------NQSVSIrSPRDAKqlgIHLVQQEVdvALVP 95
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsRKKINL-PPQQRK---IGLVFQQY--ALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 96 GLSIAENImldrlaEPGIAF-RWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPL 174
Cdd:cd03297 89 HLNVRENL------AFGLKRkRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503994372 175 DQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-241 |
1.78e-22 |
|
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: 100.59 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFRA--LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPRDakQLGI 82
Cdd:COG4618 330 RLSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS-QWDRE--ELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 H---LVQqevDVALVPGlSIAENImldrlaepgiafrwGRLRQLAREAL---AQL-DV-----SL----DVRRSIDSCTL 146
Cdd:COG4618 407 HigyLPQ---DVELFDG-TIAENI--------------ARFGDADPEKVvaaAKLaGVhemilRLpdgyDTRIGEGGARL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 147 --AEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELkAVCDTLTVLRDGRLIES 224
Cdd:COG4618 469 sgGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAF 547
|
250
....*....|....*..
gi 503994372 225 GPmadlsGEQIVEKMLG 241
Cdd:COG4618 548 GP-----RDEVLARLAR 559
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-247 |
2.10e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.69 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 2 TGNRLEMQNIS-LAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGtHAHYEGEVVINNQSVSIRSPRDAKQl 80
Cdd:PRK11174 346 DPVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRK- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 giHL--VQQEvdvALVPGLSIAENImldRLAEPGIAFrwGRLRQL-----AREALAQLDVSLDVRRSIDSCTLA--EKQQ 151
Cdd:PRK11174 424 --HLswVGQN---PQLPHGTLRDNV---LLGNPDASD--EQLQQAlenawVSEFLPLLPQGLDTPIGDQAAGLSvgQAQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 152 ILLARALSHHCRFLILDEPTAPLDQNeSERLfaVVRRLQR--QGIGIVFISHRIHELKAvCDTLTVLRDGRLIESGPMAD 229
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAH-SEQL--VMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
250
....*....|....*....
gi 503994372 230 LSGEQ-IVEKMLGHELSDI 247
Cdd:PRK11174 570 LSQAGgLFATLLAHRQEEI 588
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-238 |
4.28e-22 |
|
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: 95.00 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirsPRDAKQLGIHLV 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevDVALVPGLSIAENIMLD-RLAEPGIAfrwgRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRF 164
Cdd:cd03300 78 FQ--NYALFPHLTVFENIAFGlRLKKLPKA----EIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 165 LILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGpmadlSGEQIVEK 238
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG-----TPEEIYEE 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-225 |
4.66e-22 |
|
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: 94.36 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVsIRSPRDAKQlGIHLV 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRR-RIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevDVALVPGLSIAENI-MLDRLAepgiAFRWGRLRQLAREALAQLDVsLDVR-RSIDSCTLAEKQQILLARALSHHCR 163
Cdd:cd03265 79 FQ--DLSVDDELTGWENLyIHARLY----GVPGAERRERIDELLDFVGL-LEAAdRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 164 FLILDEPTAPLDQNESERLFAVVRRLQR-QGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
258-484 |
4.87e-22 |
|
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: 99.21 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 258 EVLLQVEGLH------DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLT-RGELNsqpWRPRDPadsva 330
Cdd:COG1123 2 TPLLEVRDLSvrypggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRiSGEVL---LDGRDL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 331 rgLALVPEERRKE--GIFIEEPVAMN-LAVSADSSFS-RWSLFGHRQAWRWAEEVIARVGI---RTSGPAQtlrrLSGGN 403
Cdd:COG1123 74 --LELSEALRGRRigMVFQDPMTQLNpVTVGDQIAEAlENLGLSRAEARARVLELLEAVGLerrLDRYPHQ----LSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 404 QQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPG 482
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
..
gi 503994372 483 AE 484
Cdd:COG1123 228 EE 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-230 |
6.06e-22 |
|
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: 94.71 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDaKQLGihLV 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNVG--FV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEvdVALVPGLSIAENI-----MLDRLAEPGIAFRWGRLRQLAReaLAQLDVSLDvrRSIDSCTLAEKQQILLARALSH 160
Cdd:cd03296 80 FQH--YALFRHMTVFDNVafglrVKPRSERPPEAEIRAKVHELLK--LVQLDWLAD--RYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQ-RQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-477 |
8.43e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKS----TLMAVLCGTHAHY-EGEVVINNQSVSI 71
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 72 RSPRDAKQL---GIHLVQQEVDVALVPGLSI----AENIMLDRlaepgiafrwGRLRQLAR-EALAQLD---VSLDVRRS 140
Cdd:PRK15134 81 ASEQTLRGVrgnKIAMIFQEPMVSLNPLHTLekqlYEVLSLHR----------GMRREAARgEILNCLDrvgIRQAAKRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 141 ID---SCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVL 216
Cdd:PRK15134 151 TDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 217 RDGRLIESGPMADL-SGEQ--IVEKMLGHELSDIFPPKrpPHSDEVLLQVEGLH-----DEGLL----------QDISLR 278
Cdd:PRK15134 231 QNGRCVEQNRAATLfSAPThpYTQKLLNSEPSGDPVPL--PEPASPLLDVEQLQvafpiRKGILkrtvdhnvvvKNISFT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 279 LRKGEILGIAGLAGAGKTELCKALFgasksRL--TRGEL--NSQP---WRPRdpadsvarglALVPEERRKEGIFIEEPV 351
Cdd:PRK15134 309 LRPGETLGLVGESGSGKSTTGLALL-----RLinSQGEIwfDGQPlhnLNRR----------QLLPVRHRIQVVFQDPNS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 AMNLAVSADSSFSRwSLFGHRQAWRWAE------EVIARVGI----RTSGPAQtlrrLSGGNQQKVAIGKWLRGNANVLI 421
Cdd:PRK15134 374 SLNPRLNVLQIIEE-GLRVHQPTLSAAQreqqviAVMEEVGLdpetRHRYPAE----FSGGQRQRIAIARALILKPSLII 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 422 FDEPTKGVDVKAKTDLFNAIDGL-AREGKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-230 |
1.15e-21 |
|
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: 93.72 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD----AKQLG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 IhLVQQEvdvALVPGLSIAENIMLdRLAEPGIAFRWgRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHH 161
Cdd:cd03261 81 M-LFQSG---ALFDSLTVFENVAF-PLREHTRLSEE-EIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-230 |
1.98e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.56 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSprdAKQL 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQEVdvALVPGLSIAENI-----MLDRLAEpgiafrwgRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLA 155
Cdd:PRK11432 79 DICMVFQSY--ALFPHMSLGENVgyglkMLGVPKE--------ERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 156 RALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
3.36e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVsirSPRDAKQLGihlv 85
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 qqevdvaLVP---GL----SIAENImldrlaepgIAFrwGRLRQL-AREALAQLDVSLD-------VRRSIDSCTLAEKQ 150
Cdd:COG4152 75 -------YLPeerGLypkmKVGEQL---------VYL--ARLKGLsKAEAKRRADEWLErlglgdrANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 151 QILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-216 |
4.02e-21 |
|
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: 96.20 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFR-ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPrDAKQLGIH 83
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQEvdVALVPGlSIAENIMLDRLAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLA--EKQQILLARALSHH 161
Cdd:TIGR02857 400 WVPQH--PFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSggQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLqRQGIGIVFISHRIHeLKAVCDTLTVL 216
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-248 |
4.17e-21 |
|
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: 94.41 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 24 VAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNqsVSIRSPRDAKQLGIH-----LVQQEVdvALVPGLS 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--RTLFDSRKGIFLPPEkrrigYVFQEA--RLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 IAENImldrlaEPGIAFRWGRLRQLAREALAQ-LDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQN 177
Cdd:TIGR02142 92 VRGNL------RYGMKRARPSERRISFERVIElLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 178 ESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKMLGHELSDIF 248
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLI 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-225 |
4.69e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.90 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRdakQLGIHLV 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvALVPGLSIAENIML----DRLAEPGIAFRwgrlrqlAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHH 161
Cdd:PRK11607 97 FQSY--ALFPHMTVEQNIAFglkqDKLPKAEIASR-------VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 162 CRFLILDEPTAPLDQNESERL-FAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-226 |
4.70e-21 |
|
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: 91.86 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHY-----EGEVVINNQSV-SIRSPRDAKQ 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 80 LGIHLVQQEvdVALVPGlSIAENIML-DRLAepGIAFRwGRLRQLAREAL--AQLDVSLDVRRSIDSCTLAEKQQILLAR 156
Cdd:cd03260 81 RRVGMVFQK--PNPFPG-SIYDNVAYgLRLH--GIKLK-EELDERVEEALrkAALWDEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQgIGIVFISHRIHELKAVCDTLTVLRDGRLIESGP 226
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
271-475 |
4.80e-21 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 91.37 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKAL---FGASKSRLTRGELNSQPWRPRDpadsVARGLALV---PEERrkeg 344
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnglLGPTSGEVLVDGKDLTKLSLKE----LRRKVGLVfqnPDDQ---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 345 IF---IEEPVA---MNLAVSADssfsrwslfghrQAWRWAEEVIARVGIrtSGPAQT-LRRLSGGNQQKVAIGKWLRGNA 417
Cdd:cd03225 88 FFgptVEEEVAfglENLGLPEE------------EIEERVEEALELVGL--EGLRDRsPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 418 NVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGR 475
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-220 |
8.54e-21 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 89.55 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV-SIRSPRDAKQLGIHL 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQevDVALVPGLSIAENIMLdrlaepgiafrwgrlrqlareALAQldvsldvrrsidsctlAEKQQILLARALSHHCRF 164
Cdd:cd03229 81 VFQ--DFALFPHLTVLENIAL---------------------GLSG----------------GQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 165 LILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGR 220
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-230 |
2.25e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFR-ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNqsVSIRS-PRDA--KQL 80
Cdd:COG1132 339 EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG--VDIRDlTLESlrRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIhlVQQevDVALVPGlSIAENImldRLAEPGIAfrwgrlRQLAREALAQLDVSLDVRR---SIDS------CTL--AEK 149
Cdd:COG1132 417 GV--VPQ--DTFLFSG-TIRENI---RYGRPDAT------DEEVEEAAKAAQAHEFIEAlpdGYDTvvgergVNLsgGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 150 QQILLARALSHHCRFLILDEPTAPLDqNESERL-FAVVRRLqRQGIGIVFISHRIHELKAvCDTLTVLRDGRLIESGPMA 228
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALD-TETEALiQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHE 559
|
..
gi 503994372 229 DL 230
Cdd:COG1132 560 EL 561
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-226 |
2.84e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.34 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFS-GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPRDA-----KQ 79
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREipylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 80 LGIhlVQQevDVALVPGLSIAENIMLD-RLAEpgiaFRWGRLRQLAREALAQldVSLDVRRSIDSCTLA--EKQQILLAR 156
Cdd:COG2884 81 IGV--VFQ--DFRLLPDRTVYENVALPlRVTG----KSRKEIRRRVREVLDL--VGLSDKAKALPHELSggEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGP 226
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-225 |
4.18e-20 |
|
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: 89.21 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQ---SVSIRSPRdaKQL 80
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirDISRKSLR--SMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIhlVQQevDVALVPGlSIAENIMLDRLAEPgiafrwgrlRQLAREALAQLDVSLDVRRSID-----------SCTLAEK 149
Cdd:cd03254 80 GV--VLQ--DTFLFSG-TIMENIRLGRPNAT---------DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 150 QQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVfISHRIHELKAVcDTLTVLRDGRLIESG 225
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSII-IAHRLSTIKNA-DKILVLDDGKIIEEG 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-489 |
4.35e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.38 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKS----TLMAVLCGTHAHYEGEVVI----NNQSVSIRS 73
Cdd:PRK10261 13 LAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLlrrrSRQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 74 PRDAKQLGIH-----LVQQEVDVALVPGLSIAENImldrlAEpGIAFRWGRLRQlarEALAQLDVSLDVRRSIDSCTL-- 146
Cdd:PRK10261 93 QSAAQMRHVRgadmaMIFQEPMTSLNPVFTVGEQI-----AE-SIRLHQGASRE---EAMVEAKRMLDQVRIPEAQTIls 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 147 --------AEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLR 217
Cdd:PRK10261 164 ryphqlsgGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 218 DGRLIESGpmadlSGEQIVEK------------------MLGHELSDIFP-------PKRPPHSD-------EVLLQVEG 265
Cdd:PRK10261 244 QGEAVETG-----SVEQIFHApqhpytrallaavpqlgaMKGLDYPRRFPlislehpAKQEPPIEqdtvvdgEPILQVRN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 266 LHDE-----GLL----------QDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRltRGELNSQPWR----PRDPA 326
Cdd:PRK10261 319 LVTRfplrsGLLnrvtrevhavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ--GGEIIFNGQRidtlSPGKL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 327 DSVARGLALVPEE-------RRKEGIFIEEPVAMNLAVSADSSFSRwslfghrQAWrwaeeVIARVGIRTSGPAQTLRRL 399
Cdd:PRK10261 397 QALRRDIQFIFQDpyasldpRQTVGDSIMEPLRVHGLLPGKAAAAR-------VAW-----LLERVGLLPEHAWRYPHEF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 400 SGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVa 478
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV- 543
|
570
....*....|.
gi 503994372 479 EIPGAEAREEN 489
Cdd:PRK10261 544 EIGPRRAVFEN 554
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-225 |
5.32e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.42 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFR--ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlGI 82
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQevDVALVPGlSIAENIML-------DRLAEpgiAFRWGRLRQLAREALAQLDvsLDVRRSIDSCTLAEKQQILLA 155
Cdd:cd03245 81 GYVPQ--DVTLFYG-TLRDNITLgapladdERILR---AAELAGVTDFVNKHPNGLD--LQIGERGRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 156 RALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRqGIGIVFISHRIHELkAVCDTLTVLRDGRLIESG 225
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-223 |
6.80e-20 |
|
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: 88.30 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRdakqlg 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 IHLVQQevDVALVPGLSIAENIMLdrlaepGIAFRwGRLRQLAREAlaqldvsldVRRSIDSCTLAE------------- 148
Cdd:cd03293 75 RGYVFQ--QDALLPWLTVLDNVAL------GLELQ-GVPKAEARER---------AEELLELVGLSGfenayphqlsggm 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 149 KQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVL--RDGRLIE 223
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-244 |
7.44e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHL 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQEvdVALVPGLSIAENIMLDRLAEPGIAFRWGRLRqlAREALAQLDVSlDVRRSI-DSCTLAEKQQILLARALSHHCR 163
Cdd:PRK10895 83 LPQE--ASIFRRLSVYDNLMAVLQIRDDLSAEQREDR--ANELMEEFHIE-HLRDSMgQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 164 FLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG-PMADLSGEQIVEKMLGH 242
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGtPTEILQDEHVKRVYLGE 237
|
..
gi 503994372 243 EL 244
Cdd:PRK10895 238 DF 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-237 |
1.17e-19 |
|
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: 87.98 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPRDAK-QLGIHL 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRaRLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQEVDValVPGLSIAENIMLdrlaepgIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLA----EKQQILLARALSH 160
Cdd:cd03218 80 LPQEASI--FRKLTVEENILA-------VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSlsggERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGpmadlSGEQIVE 237
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEG-----TPEEIAA 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
272-426 |
1.22e-19 |
|
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: 85.39 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGasKSRLTRGE--LNSQPWRpRDPADSVARGLALVPEErrkEGIFIEE 349
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG--LLSPTEGTilLDGQDLT-DDERKSLRKEIGYVFQD---PQLFPRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 350 PVAMNLAVSADSSFsrwslFGHRQAWRWAEEVIARVGI---RTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPT 426
Cdd:pfam00005 75 TVRENLRLGLLLKG-----LSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-226 |
1.41e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.40 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 16 SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirspRDAKQLGIHLVQQEVDVALVP 95
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 96 GLSIAENIMLDRLAEPGIAFR-WGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPL 174
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRaKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503994372 175 DQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDtLTVLRDGRLIESGP 226
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGP 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-230 |
2.37e-19 |
|
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: 89.39 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 10 NISLAFSGFrALsNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQ-----SVSIRSPRDAKQLGihL 84
Cdd:COG4148 6 DFRLRRGGF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPHRRRIG--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQevDVALVPGLSIAENIMLdrlaepGIAFRWGRLRQLAREALAQLdvsLDV----RRSIDSCTLAEKQQILLARALSH 160
Cdd:COG4148 82 VFQ--EARLFPHLSVRGNLLY------GRKRAPRAERRISFDEVVEL---LGIghllDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
260-479 |
3.42e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 86.41 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGL-----HDEG---LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE--LNSQPWRPRDPADSV 329
Cdd:cd03257 1 LLEVKNLsvsfpTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK--PTSGSiiFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 330 ARG--LALVPEE-------RRKEGIFIEEPVamnlavsadssfsrWSLFGHRQAWRwAEEVIARVGIRTSGPAQTLRR-- 398
Cdd:cd03257 79 IRRkeIQMVFQDpmsslnpRMTIGEQIAEPL--------------RIHGKLSKKEA-RKEAVLLLLVGVGLPEEVLNRyp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 399 --LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGR 475
Cdd:cd03257 144 heLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
....
gi 503994372 476 IVAE 479
Cdd:cd03257 224 IVEE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-240 |
4.66e-19 |
|
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: 89.88 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 23 NVAFTLTGGSVHALTGANGAGKSTLMAVLCGTH-AHYEGEVVINNQSVSIRSPRDAKQLGIHLVQQEVDV-ALVPGLSIA 100
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRhGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 101 ENIMLDRLAEpgIAFRwGRLRQLA-----REALAQLDV---SLDVrrSIDSCTLAEKQQILLARALSHHCRFLILDEPTA 172
Cdd:TIGR02633 358 KNITLSVLKS--FCFK-MRIDAAAelqiiGSAIQRLKVktaSPFL--PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 173 PLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKML 240
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
4.97e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 86.68 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGN--RLEMQNISLAF----SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSP 74
Cdd:COG1116 1 MSAAapALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 75 RdakqlgIHLVQQEvDvALVPGLSIAENIMLdrlaepGIAFRW---GRLRQLAREALAQLDvsldvrrsidsctLAE--- 148
Cdd:COG1116 81 D------RGVVFQE-P-ALLPWLTVLDNVAL------GLELRGvpkAERRERARELLELVG-------------LAGfed 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 149 ----------KQQILLARALSHHCRFLILDEPTAPLD-------QNESERLfavvrrLQRQGIGIVFISHRIHElkAV-- 209
Cdd:COG1116 134 ayphqlsggmRQRVAIARALANDPEVLLMDEPFGALDaltrerlQDELLRL------WQETGKTVLFVTHDVDE--AVfl 205
|
250
....*....|....*.
gi 503994372 210 CDTLTVL--RDGRLIE 223
Cdd:COG1116 206 ADRVVVLsaRPGRIVE 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-230 |
5.39e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.11 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLA------FSGfRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVS-------IR 72
Cdd:PRK13649 3 INLQNVSYTyqagtpFEG-RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 73 SPRdaKQLGI-------HLVQQEV--DVALVP---GLSIAEnimldrlAEpgiafrwgrlrQLAREALAQLDVSLDVR-R 139
Cdd:PRK13649 82 QIR--KKVGLvfqfpesQLFEETVlkDVAFGPqnfGVSQEE-------AE-----------ALAREKLALVGISESLFeK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 140 SIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDG 219
Cdd:PRK13649 142 NPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
250
....*....|.
gi 503994372 220 RLIESGPMADL 230
Cdd:PRK13649 222 KLVLSGKPKDI 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
271-477 |
8.91e-19 |
|
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: 84.62 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADSVArglaLVPEERRKegIFIEEP 350
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIG----YVMQDVDY--QLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNLAVSADSSfsrwslfgHRQAWRwAEEVIARVGIrtSGPAQTL-RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGV 429
Cdd:cd03226 89 VREELLLGLKEL--------DAGNEQ-AETVLKDLDL--YALKERHpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503994372 430 DVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
261-486 |
1.21e-18 |
|
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: 84.80 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLHDE--GL--LQDISLRLRKGEILGIAGLAGAGKTELCKALFGAskSRLTRGE--LNSQPWRPRDPADSVARGLA 334
Cdd:cd03219 1 LEVRGLTKRfgGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPTSGSvlFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 335 lvpeerRK---EGIFIEEPVAMNLAVSA-----DSSFSRWSLFGHRQAWRWAEEVIARVGI--RTSGPAQTlrrLSGGNQ 404
Cdd:cd03219 79 ------RTfqiPRLFPELTVLENVMVAAqartgSGLLLARARREEREARERAEELLERVGLadLADRPAGE---LSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 405 QKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIyasgefaeLV--------GLCDRICVLWDGRI 476
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVL--------LVehdmdvvmSLADRVTVLDQGRV 221
|
250
....*....|
gi 503994372 477 VAEIPGAEAR 486
Cdd:cd03219 222 IAEGTPDEVR 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
272-479 |
1.37e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 84.34 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTRGELNSQpwrpRDPADsVARGLALVPEerrKEGIFIE 348
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllePDAGFATVDGFDVV----KEPAE-ARRRLGFVSD---STGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 EPVAMNLAVSADssfsRWSLFGHRQAWRwAEEVIARVGI------RTSGpaqtlrrLSGGNQQKVAIGKWLRGNANVLIF 422
Cdd:cd03266 93 LTARENLEYFAG----LYGLKGDELTAR-LEELADRLGMeelldrRVGG-------FSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 423 DEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
261-480 |
1.86e-18 |
|
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: 83.81 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGL----HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPAdsvarglalv 336
Cdd:cd03268 1 LKTNDLtktyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 337 peeRRKEGIFIEEPvAMNLAVSADSSFSRWSLfGHRQAWRWAEEVIARVGIRTSGPAQTlRRLSGGNQQKVAIGKWLRGN 416
Cdd:cd03268 71 ---LRRIGALIEAP-GFYPNLTARENLRLLAR-LLGIRKKRIDEVLDVVGLKDSAKKKV-KGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 417 ANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEI 480
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-230 |
4.25e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.81 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVL-----CGTHAHYEGEVVINNQSVSirsprdak 78
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIF-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 79 QLGIHLVQQEVDVAL-----VPGLSIAENIM----LDRLAEPGiafrwGRLRQLAREALAQLDVSLDVRRSID----SCT 145
Cdd:PRK14247 74 KMDVIELRRRVQMVFqipnpIPNLSIFENVAlglkLNRLVKSK-----KELQERVRWALEKAQLWDEVKDRLDapagKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 146 LAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQgIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
....*
gi 503994372 226 PMADL 230
Cdd:PRK14247 228 PTREV 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-227 |
8.17e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGtHAHYE---GEVVINNQSVSIRSPRDAKQLGI 82
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKYEvtsGSILLDGEDILELSPDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLV-QQEVDvalVPGLSIAE--NIMLDRLAEPGIAFRwgRLRQLAREALAQLDVSLD-VRRSIDScTLA--EKQQ--ILL 154
Cdd:COG0396 80 FLAfQYPVE---IPGVSVSNflRTALNARRGEELSAR--EFLKLLKEKMKELGLDEDfLDRYVNE-GFSggEKKRneILQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 155 ARALSHhcRFLILDEPTAPLD----QNESErlfaVVRRLQRQGIGIVFISH--RI-HELKAvcDTLTVLRDGRLIESGPM 227
Cdd:COG0396 154 MLLLEP--KLAILDETDSGLDidalRIVAE----GVNKLRSPDRGILIITHyqRIlDYIKP--DFVHVLVDGRIVKSGGK 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-225 |
1.90e-17 |
|
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: 81.58 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSP-RDAKQLGiH 83
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvELRRKIG-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQevdVALVPGLSIAENIMLdrlaEPGIaFRWG--RLRQLAREALAqlDVSLD----VRRSIDSCTLAEKQQILLARA 157
Cdd:cd03295 80 VIQQ---IGLFPHMTVEENIAL----VPKL-LKWPkeKIRERADELLA--LVGLDpaefADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 158 LSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-225 |
1.94e-17 |
|
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: 81.61 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRaLSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPrdaKQLGIHLV 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevDVALVPGLSIAENImldrlaEPGIAFRWGRLRQLAREAL---AQLDVSLDVRRSIDSCTLAEKQQILLARALSHHC 162
Cdd:cd03299 77 PQ--NYALFPHMTVYKNI------AYGLKKRKVDKKEIERKVLeiaEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 163 RFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-279 |
2.03e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSpRDAKQlGIHLV 85
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARA-RIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDvaLVPGLSIAENIMLdrlaepgiafrWGR-LRQLAREA---------LAQLDVSLDVRRSIDSCTLaeKQQILLA 155
Cdd:PRK13536 120 PQFDN--LDLEFTVRENLLV-----------FGRyFGMSTREIeavipslleFARLESKADARVSDLSGGM--KRRLTLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 156 RALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQI 235
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 236 ---VEKMLG---HELSDIFPPKR-------------PPHSDEVLLQVEGLHDEGLLQ------DISLRL 279
Cdd:PRK13536 265 gcqVIEIYGgdpHELSSLVKPYArrievsgetlfcyAPDPEQVRVQLRGRAGLRLLQrppnleDVFLRL 333
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-225 |
2.28e-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: 81.22 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLVQQEV---DVALVP 95
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQlwwDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 96 GLSIAENIMldRLaePGIAFRwGRLRQLAreALAQLDVSLD--VRRsidsCTLAEKQQILLARALSHHCRFLILDEPTAP 173
Cdd:cd03267 115 SFYLLAAIY--DL--PPARFK-KRLDELS--ELLDLEELLDtpVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 174 LDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-230 |
2.62e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 80.63 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFR--ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQsvSIRSPRDAKQLGIH 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQevDVALVPGLSIAENIMLdrlaepgiafrWGRLRQLAREalaqlDVSLDVRRSIDSCTLAEKQQiLLARALS--HH 161
Cdd:cd03263 79 YCPQ--FDALFDELTVREHLRF-----------YARLKGLPKS-----EIKEEVELLLRVLGLTDKAN-KRARTLSggMK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 162 CR------------FLILDEPTAPLDQNESERLFAVVRRLqRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMAD 229
Cdd:cd03263 140 RKlslaialiggpsVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
.
gi 503994372 230 L 230
Cdd:cd03263 219 L 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-241 |
2.75e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.80 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG--------THAHYEGEVVINNQSVS-IRSPRD 76
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAaIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 AKQLGIHLVQQEVDVALvpglSIAENIMLDRLAEpgiAFRWG----RLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQI 152
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAF----SAREIVLLGRYPH---ARRAGalthRDGEIAWQALALAGATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 153 LLARALSH---------HCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLI 222
Cdd:PRK13547 155 QFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
250
....*....|....*....
gi 503994372 223 ESGPMADLSGEQIVEKMLG 241
Cdd:PRK13547 235 AHGAPADVLTPAHIARCYG 253
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-203 |
3.19e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 79.77 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 17 GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV--SIRSPRDAKQlGIHLVQQEVDVALV 94
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQ-RVGLVFQDPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 95 PGlSIAENIMLDRLaepGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPL 174
Cdd:TIGR01166 83 AA-DVDQDVAFGPL---NLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180
....*....|....*....|....*....
gi 503994372 175 DQNESERLFAVVRRLQRQGIGIVFISHRI 203
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDV 187
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-223 |
4.49e-17 |
|
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: 80.17 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRA----LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSI----- 71
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 72 RSPRDAKQLGIhlVQQEVDvaLVPGLSIAENIMLdrlaePGIAFRWGRLRQLAREALAQldVSLDVRRSIDSCTL--AEK 149
Cdd:COG4181 84 RARLRARHVGF--VFQSFQ--LLPTLTALENVML-----PLELAGRRDARARARALLER--VGLGHRLDHYPAQLsgGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 150 QQILLARALSHHCRFLILDEPTAPLDQNESER----LFAVVRrlqRQGIGIVFISHRiHELKAVCDTLTVLRDGRLIE 223
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFELNR---ERGTTLVLVTHD-PALAARCDRVLRLRAGRLVE 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-230 |
4.52e-17 |
|
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: 80.35 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV---SIRSPRdaKQLGIhlVQQevDVALVPG 96
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLR--RQIGL--VSQ--DVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 97 lSIAENIMLDRLAEPGiafrwGRLRQLAREALAQ---------LDVSLDVRRSIDSCtlAEKQQILLARALSHHCRFLIL 167
Cdd:cd03251 91 -TVAENIAYGRPGATR-----EEVEEAARAANAHefimelpegYDTVIGERGVKLSG--GQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 168 DEPTAPLDqNESERLF-AVVRRLQRQGIGIVfISHRIHELKAVcDTLTVLRDGRLIESGPMADL 230
Cdd:cd03251 163 DEATSALD-TESERLVqAALERLMKNRTTFV-IAHRLSTIENA-DRIVVLEDGKIVERGTHEEL 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-225 |
5.05e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 79.84 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 27 TLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD--------AKQLGIHL-VQQEVDVALVPGL 97
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvsmlfqENNLFAHLtVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 SIAEnimLDRLAEPGIafrwgrlrqLAREALAQLDvsldvRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQN 177
Cdd:cd03298 100 KLTA---EDRQAIEVA---------LARVGLAGLE-----KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503994372 178 ESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03298 163 LRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-238 |
5.83e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.88 E-value: 5.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGthAHYEGEVV------INNQSVSIRSPRDAKQL---GIHLVQQE 88
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG--ITKDNWHVtadrfrWNGIDLLKLSPRERRKIigrEIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 89 VDVALVPGLSIAENIMLdrlAEPGIAFR---WGRLRQLAREALAQLD-VSL-DVRRSIDS----CTLAEKQQILLARALS 159
Cdd:COG4170 98 PSSCLDPSAKIGDQLIE---AIPSWTFKgkwWQRFKWRKKRAIELLHrVGIkDHKDIMNSypheLTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMadlsgEQIVEK 238
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT-----EQILKS 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-227 |
6.41e-17 |
|
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: 79.11 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGtHAHYE---GEVVINNQSVSIRSPRDAKQLGI 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEvteGEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQEvdVALVPGLSIAEnimldrlaepgiafrwgrlrqLAREalaqLDVSL---DVRRSidsctlaEKQQILLARAls 159
Cdd:cd03217 80 FLAFQY--PPEIPGVKNAD---------------------FLRY----VNEGFsggEKKRN-------EILQLLLLEP-- 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 160 hhcRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAV-CDTLTVLRDGRLIESGPM 227
Cdd:cd03217 124 ---DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
271-475 |
9.51e-17 |
|
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: 77.29 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELnsqpwrprdpadsvarglalvpeerrkegifieep 350
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP--TSGEI----------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 vamnlavsadssfsrwSLFGHRQAWRWAEEVIARVGIRTSgpaqtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVD 430
Cdd:cd00267 57 ----------------LIDGKDIAKLPLEELRRRIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503994372 431 VKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGR 475
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-226 |
9.66e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFR-----------ALSNVAFTLTGGSVHALTGANGAGKSTL-MAVLCGTHAhyEGEVVINNQSVSIRS 73
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLINS--QGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 74 PRdakQL-----GIHLVQQEVDVALVPGLSIAENImldrlaEPGIAFRWGRLRQLAREA---LAQLDVSLDV---RRSID 142
Cdd:PRK15134 354 RR---QLlpvrhRIQVVFQDPNSSLNPRLNVLQII------EEGLRVHQPTLSAAQREQqviAVMEEVGLDPetrHRYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 143 SCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQ-RQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
....*
gi 503994372 222 IESGP 226
Cdd:PRK15134 505 VEQGD 509
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-298 |
1.12e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 82.37 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSprdAKQLGiHLV 85
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS---FEQLQ-KLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQE-----VDVaLVP-----GLSIAEnIMLDRLAEPGiafrwgRLRQLArealAQLDVS-LDVRRSIDSCTlAEKQQILL 154
Cdd:PRK10938 80 SDEwqrnnTDM-LSPgeddtGRTTAE-IIQDEVKDPA------RCEQLA----QQFGITaLLDRRFKYLST-GETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQ 234
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 235 IV------EKMLGHELSDIFPPKR----PPHSDEVLLQ--VEGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTEL 298
Cdd:PRK10938 227 LVaqlahsEQLEGVQLPEPDEPSArhalPANEPRIVLNngVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTL 302
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-220 |
1.14e-16 |
|
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: 79.02 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIR----SPRDAKQL---GIHLVQQEVDVa 92
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDlaqaSPREILALrrrTIGYVSQFLRV- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 93 lVPGLSiaeniMLDRLAEPGIAFRWGRL--RQLAREALAQLDV--SLdvrrsidsCTLA-------EKQQILLARALSHH 161
Cdd:COG4778 105 -IPRVS-----ALDVVAEPLLERGVDREeaRARARELLARLNLpeRL--------WDLPpatfsggEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGR 220
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
272-478 |
1.20e-16 |
|
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: 78.70 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGE-------LNSQPwrprdpaDSVARGLALVPeerRKEG 344
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSGTayingysIRTDR-------KAARQSLGYCP---QFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 345 IFIEEPVAMNLAVsadssFSRWSLFGHRQAWRWAEEVIARVGIrtSGPAQTL-RRLSGGNQQKVAIGKWLRGNANVLIFD 423
Cdd:cd03263 86 LFDELTVREHLRF-----YARLKGLPKSEIKEEVELLLRVLGL--TDKANKRaRTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 424 EPTKGVDVKAKTDLFNAIDGLaREGKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-205 |
1.22e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.91 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFR----ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAkql 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 gihLVQQevDVALVPGLSIAENIMLD-RLAEPGIAFRwgrlRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALS 159
Cdd:COG4525 80 ---VVFQ--KDALLPWLNVLDNVAFGlRLRGVPKAER----RARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHE 205
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEE 197
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
261-478 |
1.59e-16 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 78.33 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGE--LNSQPWRPRDPADsvaRGLA 334
Cdd:cd03259 1 LELKGLSktygSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLI--AGLERPDSGEilIDGRDVTGVPPER---RNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 335 LVPEERRkegIF----IEEPVAMNLavsadssfsRWSLFGHRQAWRWAEEVIARVGIRTSG---PAQtlrrLSGGNQQKV 407
Cdd:cd03259 76 MVFQDYA---LFphltVAENIAFGL---------KLRGVPKAEIRARVRELLELVGLEGLLnryPHE----LSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 408 AIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-221 |
1.95e-16 |
|
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: 77.96 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRdakqlgIHLV 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN------INEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEV-----DVALVPGLSIAENIMLdrlaepGIAFRWGRLR----QLAREALAQldVSLDVRRSIDSCTLA--EKQQILL 154
Cdd:cd03262 75 RQKVgmvfqQFNLFPHLTVLENITL------APIKVKGMSKaeaeERALELLEK--VGLADKADAYPAQLSggQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
274-484 |
2.02e-16 |
|
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: 80.54 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 274 DISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWrprdpADSvARGLALVPEERRKEGIFIEEPVAM 353
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-----FDS-RKGIFLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 354 NLAVSADSSFSRWSLFGHRQAWRWaEEVIARVGIrtsGP--AQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDV 431
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISF-ERVIELLGI---GHllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 432 KAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAE 484
Cdd:TIGR02142 165 PRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-221 |
3.42e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDA-----KQLG-IHLVQQevdvaLV 94
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGfIYQFHH-----LL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 95 PGLSIAENIMLDRL---AEPGIAfrwgrlRQLAREALAQldVSLDVRRSIDSCTLA--EKQQILLARALSHHCRFLILDE 169
Cdd:PRK11629 100 PDFTALENVAMPLLigkKKPAEI------NSRALEMLAA--VGLEHRANHRPSELSggERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 170 PTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTvLRDGRL 221
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-229 |
3.45e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAhYEGEVVINNQSVSIRSPRDAKQLGIHLVQQEVDVALVPglsIA 100
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMP---VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 101 ENIMLDRLAEPGIAFRWGRLRQLAReaLAQLDVSLDvrRSIDSCTLAEKQQILLA-------RALSHHCRFLILDEPTAP 173
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASALNEVAE--ALGLDDKLG--RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 174 LDQNESERLFAVVRRLQRQGIGIVFISHRI-HELKAVcDTLTVLRDGRLIESGPMAD 229
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLnHTLRHA-DRVWLLKQGKLLASGRRDE 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-221 |
3.57e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 77.45 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPRDAKQL---G 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPYlrrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 IHLVQQevDVALVPGLSIAENIM--LDRLAEPGiafrwGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALS 159
Cdd:cd03292 80 IGVVFQ--DFRLLPDRNVYENVAfaLEVTGVPP-----REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-225 |
3.60e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 32 SVHALTG---ANGAGKSTLMAVLCGTHAHYEGEVVINNQsvsirsPRDAKQLGIHLVQQEVDVALV-PGLSIAENIMldr 107
Cdd:PRK13638 25 SLSPVTGlvgANGCGKSTLFMNLSGLLRPQKGAVLWQGK------PLDYSKRGLLALRQQVATVFQdPEQQIFYTDI--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 108 laEPGIAFRWGRL----RQLAR---EALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESE 180
Cdd:PRK13638 96 --DSDIAFSLRNLgvpeAEITRrvdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503994372 181 RLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-230 |
4.69e-16 |
|
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: 80.50 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSNVAFTLTGGSVHALTGANGAGKSTL-MAVLcGTHAHyEGEVVINNQSVSIRSPRDAKQL--GIHLVQQEVDVALV 94
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLIPS-EGEIRFDGQDLDGLSRRALRPLrrRMQVVFQDPFGSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 95 PGLSIAENImldrlAEP----GIAFRWGRLRQLAREALAqlDVSLDVrrsidscTLAEK----------QQILLARALSH 160
Cdd:COG4172 377 PRMTVGQII-----AEGlrvhGPGLSAAERRARVAEALE--EVGLDP-------AARHRyphefsggqrQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 161 HCRFLILDEPTAPLD---QNESERLFavvRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG4172 443 EPKLLVLDEPTSALDvsvQAQILDLL---RDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-216 |
6.15e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 8 MQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVinnqsvsiRSPrdakQLGIHLVQQ 87
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNG----KLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 88 EVDVALVPGLSIAENIMLdrlaEPGIAfRWGRLRQLAREALAQLdvsldVRRSIDSCTLAEKQQILLARALSHHCRFLIL 167
Cdd:PRK09544 75 KLYLDTTLPLTVNRFLRL----RPGTK-KEDILPALKRVQAGHL-----IDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503994372 168 DEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVL 216
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-248 |
7.16e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVS-IRSPRDAKQLGIhlV 85
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAtTPSRELAKRLAI--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDVALvpGLSIAEnimLdrlaepgIAF-RW----GRL----RQLAREALAQLDVSlDVR-RSIDSCTLAEKQQILLA 155
Cdd:COG4604 81 RQENHINS--RLTVRE---L-------VAFgRFpyskGRLtaedREIIDEAIAYLDLE-DLAdRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 156 RALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQR-QGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLsgeq 234
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI---- 223
|
250
....*....|....
gi 503994372 235 IVEKMlgheLSDIF 248
Cdd:COG4604 224 ITPEV----LSDIY 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
261-479 |
7.34e-16 |
|
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: 76.77 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADSVarglalv 336
Cdd:cd03261 1 IELRGLTksfgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 337 pEERRKEGI-F----------IEEPVAMNLavSADSSFSRWSLFghrqawRWAEEVIARVGIRTSG---PAQtlrrLSGG 402
Cdd:cd03261 74 -RLRRRMGMlFqsgalfdsltVFENVAFPL--REHTRLSEEEIR------EIVLEKLEAVGLRGAEdlyPAE----LSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 403 NQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-225 |
8.80e-16 |
|
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: 76.42 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIrsprdakqLGIHlvqqevdVALVPGL 97
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLG-------GGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 SIAENIMLdrlaepgIAFRWGRLRQLARE------ALAQLDVSLD--VRrsidscTLAEKQQILLARALSHHCRF--LIL 167
Cdd:cd03220 100 TGRENIYL-------NGRLLGLSRKEIDEkideiiEFSELGDFIDlpVK------TYSSGMKARLAFAIATALEPdiLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 168 DEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
272-483 |
1.09e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.46 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTRGELNSQPWRPrdpADSVARGLALVPEERRkegIFIE 348
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdprATSGRIVFDGKDITDWQT---AKIMREAVAIVPEGRR---VFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 EPVAMNLAVSAdssfsrwsLFGHRQAW----RWAEEVIARVGIRTSGPAQTLrrlSGGNQQKVAIGKWLRGNANVLIFDE 424
Cdd:PRK11614 95 MTVEENLAMGG--------FFAERDQFqeriKWVYELFPRLHERRIQRAGTM---SGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 425 PTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGA 483
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGD 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-230 |
1.23e-15 |
|
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: 77.79 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTH---AHYEGEVVINNQSVSIRSPRDAK 78
Cdd:COG0444 2 LEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 79 QL---GIHLVQQEVDVALVPGLSIAENImldrlAEPGIAFRWGR---LRQLAREALAQLDVSLDVRRsidsctLAE---- 148
Cdd:COG0444 82 KIrgrEIQMIFQDPMTSLNPVMTVGDQI-----AEPLRIHGGLSkaeARERAIELLERVGLPDPERR------LDRyphe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 149 -----KQQILLARALSHHCRFLILDEPTAPLD---QNESERLFavvRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDG 219
Cdd:COG0444 151 lsggmRQRVMIARALALEPKLLIADEPTTALDvtiQAQILNLL---KDLQRElGLAILFITHDLGVVAEIADRVAVMYAG 227
|
250
....*....|.
gi 503994372 220 RLIESGPMADL 230
Cdd:COG0444 228 RIVEEGPVEEL 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
272-476 |
1.63e-15 |
|
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: 75.60 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQpwrprDPADSVARGLAlvpEERRKE-G-IF- 346
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRP--TSGEvrVDGT-----DISKLSEKELA---AFRRRHiGfVFq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 ---------IEEPVAMNLAVSADSSfsrwslfghRQAWRWAEEVIARVGIR---TSGPAQtlrrLSGGNQQKVAIGKWLR 414
Cdd:cd03255 90 sfnllpdltALENVELPLLLAGVPK---------KERRERAEELLERVGLGdrlNHYPSE----LSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFaELVGLCDRICVLWDGRI 476
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-229 |
1.96e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAfsgfRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAhYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:COG4138 1 LQLNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDVALVPGLsiaENIMLDRLAEPGIAFRWGRLRQLArEALaQLDVSLDvrRSIDSCTLAEKQQILLARAL------- 158
Cdd:COG4138 76 QQQSPPFAMPVF---QYLALHQPAGASSEAVEQLLAQLA-EAL-GLEDKLS--RPLTQLSGGEWQRVRLAAVLlqvwpti 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRI-HELKAvCDTLTVLRDGRLIESGPMAD 229
Cdd:COG4138 149 NPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLnHTLRH-ADRVWLLKQGKLVASGETAE 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-225 |
2.49e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHL 84
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQEVDVALVpGLSIAENIML--DRLAEPGIafrwgRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHC 162
Cdd:PRK13644 82 VFQNPETQFV-GRTVEEDLAFgpENLCLPPI-----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 163 RFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVcDTLTVLRDGRLIESG 225
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLEG 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
260-477 |
3.24e-15 |
|
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: 76.63 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLH-----DEGLLQ---DISLRLRKGEILGIAGLAGAGKTELCKALFG-ASKSRLTRGELNsqpWRPRDpadsva 330
Cdd:COG0444 1 LLEVRNLKvyfptRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGlLPPPGITSGEIL---FDGED------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 331 rgLALVPEERRKE-------GIF----------------IEEPVAMNLAVSAdssfsrwslfghRQAWRWAEEVIARVGI 387
Cdd:COG0444 72 --LLKLSEKELRKirgreiqMIFqdpmtslnpvmtvgdqIAEPLRIHGGLSK------------AEARERAIELLERVGL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 388 rtSGPAQTLRR----LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELV 462
Cdd:COG0444 138 --PDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVA 215
|
250
....*....|....*
gi 503994372 463 GLCDRICVLWDGRIV 477
Cdd:COG0444 216 EIADRVAVMYAGRIV 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-230 |
3.56e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.79 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRAlsNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPrdAKQLGIHLV 85
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QqevDVALVPGLSIAENImldrlaepGIAFRWG-RL----RQLAREALAQLDVS--LDVRRSIDSCtlAEKQQILLARAL 158
Cdd:COG3840 78 Q---ENNLFPHLTVAQNI--------GLGLRPGlKLtaeqRAQVEQALERVGLAglLDRLPGQLSG--GQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQR-QGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
271-477 |
4.33e-15 |
|
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: 73.74 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGE--LNSQPWRPRDPADSVArglaLVPEERrkegIFIE 348
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEvlINGRPLDKRSFRKIIG----YVPQDD----ILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 E-PVAMNLAVSADssfsrwslfghrqawrwaeeviarvgirtsgpaqtLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTK 427
Cdd:cd03213 96 TlTVRETLMFAAK-----------------------------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 428 GVDVKAKTDLFNAIDGLAREGKGV---IYASGefAELVGLCDRICVLWDGRIV 477
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADTGRTIicsIHQPS--SEIFELFDKLLLLSQGRVI 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-225 |
4.65e-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: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAkqlGIHLV 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQevDVALVPGLSIAENIM----LDRLAEPGIAfrwGRLRQLAReaLAQLDVSLDvrRSIDSCTLAEKQQILLARALSHH 161
Cdd:cd03301 78 FQ--NYALYPHMTVYDNIAfglkLRKVPKDEID---ERVREVAE--LLQIEHLLD--RKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-226 |
4.66e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 74.65 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVsirsprDAKQLGIHLV 85
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL------TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEV-----DVALVPGLSIAENIMLDrlaePGIAFRWGR--LRQLAREALAQldvsldVRrsidsctLAEK--------- 149
Cdd:COG1126 76 RRKVgmvfqQFNLFPHLTVLENVTLA----PIKVKKMSKaeAEERAMELLER------VG-------LADKadaypaqls 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 150 ---QQ---IllARALSHHCRFLILDEPTAPLD-QNESERLfAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLI 222
Cdd:COG1126 139 ggqQQrvaI--ARALAMEPKVMLFDEPTSALDpELVGEVL-DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
....
gi 503994372 223 ESGP 226
Cdd:COG1126 216 EEGP 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
272-475 |
4.83e-15 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 72.99 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPwrprdpadsVARGLALVPEERRKEGIFieepv 351
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED---------LTDLEDELPPLRRRIGMV----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 amnlavsadssFSRWSLFGHRqawrwaeEVIARVGIrtsgpaqtlrRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDV 431
Cdd:cd03229 82 -----------FQDFALFPHL-------TVLENIAL----------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503994372 432 KAKTDLFNAIDGL-AREGKGVIYASGEFAELVGLCDRICVLWDGR 475
Cdd:cd03229 134 ITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
272-488 |
5.54e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.53 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQPWRPRDpadsvARGLALVPEERrkeGIFIEE 349
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP--DSGEvlWDGEPLDPED-----RRRIGYLPEER---GLYPKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 350 PVAMNLAVsadssFSRwsLFG--HRQAWRWAEEVIARVGIrTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTK 427
Cdd:COG4152 87 KVGEQLVY-----LAR--LKGlsKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 428 GVDVKAKTDLFNAIDGLAREGKGVIYASG--EFAELvgLCDRICVLWDGRIVAEIPGAEAREE 488
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-261 |
6.64e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SGF----RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSP-RDAKQ 79
Cdd:COG1101 2 LELKNLSKTFnPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEyKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 80 LGIhlVQQEVDVALVPGLSIAENIMLDRLAEPGIAFRWG---RLRQLAREALAQLDVSLDVRRSIDSCTLA--EKQQILL 154
Cdd:COG1101 82 IGR--VFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRGltkKRRELFRELLATLGLGLENRLDTKVGLLSggQRQALSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIesgpmADLSGE 233
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII-----LDVSGE 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 503994372 234 QI----VEKML-------GHELSDifppkrpphsDEVLL 261
Cdd:COG1101 235 EKkkltVEDLLelfeeirGEELAD----------DRLLL 263
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-251 |
6.81e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 8 MQNISLAFSG-----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV--SIRSPRDAKQL 80
Cdd:PRK13645 9 LDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 gihlvqqEVDVALVpgLSIAENIMLDRLAEPGIAFRWGRLRQLAREALAQLDVSLD--------VRRSIDSCTLAEKQQI 152
Cdd:PRK13645 89 -------RKEIGLV--FQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKlvqlpedyVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 153 LLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQR-QGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG-PMADL 230
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGsPFEIF 239
|
250 260
....*....|....*....|.
gi 503994372 231 SGEQIVEKMlghelsDIFPPK 251
Cdd:PRK13645 240 SNQELLTKI------EIDPPK 254
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-230 |
7.08e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.61 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF----SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGthahyegeVVINNQSVSIR--------- 72
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKDNWRVTADrmrfddidl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 73 ---SPRDAKQL---GIHLVQQEVDVALVPGLSIAENIMLdrlAEPGIAFR---WGRLRQLAREALAQLD-VSLDVRRSID 142
Cdd:PRK15093 76 lrlSPRERRKLvghNVSMIFQEPQSCLDPSERVGRQLMQ---NIPGWTYKgrwWQRFGWRKRRAIELLHrVGIKDHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 143 SC-----TLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVL 216
Cdd:PRK15093 153 RSfpyelTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVL 232
|
250
....*....|....
gi 503994372 217 RDGRLIESGPMADL 230
Cdd:PRK15093 233 YCGQTVETAPSKEL 246
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
271-479 |
7.61e-15 |
|
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: 72.47 E-value: 7.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE--LNSQPWRPRDPADsVARGLALVPeerrkegifie 348
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK--PSSGEilLDGKDLASLSPKE-LARKIAYVP----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 epvamnlavsadssfsrwslfghrQAwrwaeevIARVGIrTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKG 428
Cdd:cd03214 80 ------------------------QA-------LELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503994372 429 VDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03214 128 LDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
258-478 |
9.49e-15 |
|
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: 73.10 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 258 EVLLQVEGLHDEGLLqDISLRLrKGEILGIAGLAGAGKTELCKALFGASKsrLTRG--ELNSQPWrprdpaDSVARGLAL 335
Cdd:cd03297 1 MLCVDIEKRLPDFTL-KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEK--PDGGtiVLNGTVL------FDSRKKINL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 336 VPEERRKEGIFIEEPVAMNLAVSADSSFSrwsLFGHRQAWR--WAEEVIARVGIRT---SGPAQtlrrLSGGNQQKVAIG 410
Cdd:cd03297 71 PPQQRKIGLVFQQYALFPHLNVRENLAFG---LKRKRNREDriSVDELLDLLGLDHllnRYPAQ----LSGGEKQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 411 KWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKG-VIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIpVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
268-484 |
1.25e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 268 DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDpADSVARGLALVPEERRKEGIF- 346
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVASVPQDTSLSFEFd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 IEEPVAMNlAVSADSSFSRWSLFGHRQAwrwaEEVIARVGIrTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPT 426
Cdd:PRK09536 94 VRQVVEMG-RTPHRSRFDTWTETDRAAV----ERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 427 KGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAE 484
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-226 |
1.29e-14 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 72.91 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDA-KQLGIhlVQQevDVALVPGlS 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrSRISI--IPQ--DPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 IAENimLDRLAEPGIAFRWGRLRQLA-REALAQLDVSLDVRRSIDSCTLA--EKQQILLARALSHHCRFLILDEPTAPLD 175
Cdd:cd03244 94 IRSN--LDPFGEYSDEELWQALERVGlKEFVESLPGGLDTVVEEGGENLSvgQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503994372 176 QnESERLFAVVRRLQRQGIGIVFISHRIHELKAvCDTLTVLRDGRLIESGP 226
Cdd:cd03244 172 P-ETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-225 |
1.39e-14 |
|
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: 73.29 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAK-QLGIhlVQQEvdvALVPGLS 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrQVGV--VLQE---NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 IAENIMLdrlAEPGIAFRwgRLRQLAREALAQlDVSLDVRRSID--------SCTLAEKQQILLARALSHHCRFLILDEP 170
Cdd:cd03252 92 IRDNIAL---ADPGMSME--RVIEAAKLAGAH-DFISELPEGYDtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 171 TAPLDQnESERlfAVVRRLQR--QGIGIVFISHRIHELKAVcDTLTVLRDGRLIESG 225
Cdd:cd03252 166 TSALDY-ESEH--AIMRNMHDicAGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQG 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-230 |
1.40e-14 |
|
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: 73.34 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQ---SVSIRSPRDakQLGIhlVQQEvdvalvPGL 97
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirDLNLRWLRS--QIGL--VSQE------PVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 ---SIAENIML---DRLAEPGIafrwgrlrQLAREALAQlDVSLDVRRSIDS------CTLA--EKQQILLARALSHHCR 163
Cdd:cd03249 89 fdgTIAENIRYgkpDATDEEVE--------EAAKKANIH-DFIMSLPDGYDTlvgergSQLSggQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 164 FLILDEPTAPLDqNESERLfaVVRRLQR--QGIGIVFISHRIHELKAvCDTLTVLRDGRLIESGPMADL 230
Cdd:cd03249 160 ILLLDEATSALD-AESEKL--VQEALDRamKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
261-484 |
1.54e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGL----HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKA---LFGASKSRLTRGELNSQPWRPRDPADSVARGL 333
Cdd:PRK11264 4 IEVKNLvkkfHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinlLEQPEAGTIRVGDITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 334 alvpeeRRKEGiFIeepvamnlavsadssFSRWSLFGHR-------------------QAWRWAEEVIARVGI---RTSG 391
Cdd:PRK11264 84 ------RQHVG-FV---------------FQNFNLFPHRtvleniiegpvivkgepkeEATARARELLAKVGLagkETSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 392 PaqtlRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVL 471
Cdd:PRK11264 142 P----RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFM 217
|
250
....*....|...
gi 503994372 472 WDGRIVAEIPGAE 484
Cdd:PRK11264 218 DQGRIVEQGPAKA 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-226 |
2.22e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSPrdAKQLGIHLV 85
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVP--AENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvALVPGLSIAENIM----LDRLAEPGI------AFRWGRLRQLAREALAQLdvsldvrrsidscTLAEKQQILLA 155
Cdd:PRK09452 92 FQSY--ALFPHMTVFENVAfglrMQKTPAAEItprvmeALRMVQLEEFAQRKPHQL-------------SGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 156 RALSHHCRFLILDEPTAPLD-------QNEserlfavVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGP 226
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDyklrkqmQNE-------LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-225 |
2.52e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSvsiRSPRDAKQLGI--- 82
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD---GQLRDLYALSEaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 -HL-------VQQEVDVALVPGLSIAENIMlDRLAEPGiAFRWGRLRQLAREALAQldVSLDVRRsID------SCTLAE 148
Cdd:PRK11701 84 rRLlrtewgfVHQHPRDGLRMQVSAGGNIG-ERLMAVG-ARHYGDIRATAGDWLER--VEIDAAR-IDdlpttfSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 149 KQQIllARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK11701 159 RLQI--ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-240 |
2.64e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.53 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGnRLEMQNISLAF---SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirsPRDA 77
Cdd:TIGR00958 475 LEG-LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV---QYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 KQLGIH--LVQQEvdvALVPGLSIAENIM--LDRLAEPGIafrwgrlRQLAREALAQlDVSLDVRRSIDS--------CT 145
Cdd:TIGR00958 551 HYLHRQvaLVGQE---PVLFSGSVRENIAygLTDTPDEEI-------MAAAKAANAH-DFIMEFPNGYDTevgekgsqLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 146 LAEKQQILLARALSHHCRFLILDEPTAPLDQnESERLFAVVRrlQRQGIGIVFISHRIHELKAvCDTLTVLRDGRLIESG 225
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDA-ECEQLLQESR--SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
250
....*....|....*
gi 503994372 226 PMADLSGEQIVEKML 240
Cdd:TIGR00958 696 THKQLMEDQGCYKHL 710
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-241 |
2.84e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirsprdakQLGIHLV 85
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--------DWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEvDVALVPG-------LSIAENIMLdrlaepGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLA--EKQQILLAR 156
Cdd:PRK11614 78 MRE-AVAIVPEgrrvfsrMTVEENLAM------GGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSggEQQMLAIGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLI-ESGPMADLSGEQI 235
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVlEDTGDALLANEAV 230
|
....*.
gi 503994372 236 VEKMLG 241
Cdd:PRK11614 231 RSAYLG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
261-487 |
3.48e-14 |
|
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: 71.02 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELnsqpwrprdpadsVARG---L 333
Cdd:cd03217 1 LEIKDLHvsvgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEI-------------LFKGediT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 334 ALVPEERRKEGIFIeepvamnlavsadssfsrwslfghrqAWRWAEEViarVGIRTsgpAQTLRRL----SGGNQQKVAI 409
Cdd:cd03217 68 DLPPEERARLGIFL--------------------------AFQYPPEI---PGVKN---ADFLRYVnegfSGGEKKRNEI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 410 GKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYAS--GEFAELVgLCDRICVLWDGRIVAEIPGAEARE 487
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYI-KPDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-225 |
3.55e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.04 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 16 SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG--THAHYEGEVVINNQSVSIRSPRdaKQLGihLVQQEvDVAL 93
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR--KIIG--YVPQD-DILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 94 vPGLSIAENIMLDrlaepgiafrwgrlrqlarealAQLdvsldvrRSIDSctlAEKQQILLARALSHHCRFLILDEPTAP 173
Cdd:cd03213 95 -PTLTVRETLMFA----------------------AKL-------RGLSG---GERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 174 LDQNESERLFAVVRRLQRQGIGIVFISHRI-HELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-241 |
3.83e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGIh 83
Cdd:PRK10253 7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvARRIGL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQevdvALVPG-LSIAENIMLDRLAEPGIAFRWGRLRQLA-REALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHH 161
Cdd:PRK10253 86 LAQN----ATTPGdITVQELVARGRYPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQR-QGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVEKML 240
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
.
gi 503994372 241 G 241
Cdd:PRK10253 242 G 242
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-235 |
5.03e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.94 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIhlVQQEVDVALVPGLSIAENIML--DRLAEPGI---AFRWGRLRQLAREALAQLDVSLDVRRSID-----SCTLAEKQ 150
Cdd:PRK11300 81 GV--VRTFQHVRLFREMTVIENLLVaqHQQLKTGLfsgLLKTPAFRRAESEALDRAATWLERVGLLEhanrqAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 151 QILL--ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRliesgPM 227
Cdd:PRK11300 159 QRRLeiARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT-----PL 233
|
....*...
gi 503994372 228 ADLSGEQI 235
Cdd:PRK11300 234 ANGTPEEI 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-225 |
5.67e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQ 79
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 80 lGIHLVQQEvdvALVPGLSIAENIMLDR-LAEPGIafrWGRLR--QLArEALAQLDVSLDVRRSIDSCTLA--EKQQILL 154
Cdd:PRK10790 416 -GVAMVQQD---PVVLADTFLANVTLGRdISEEQV---WQALEtvQLA-ELARSLPDGLYTPLGEQGNNLSvgQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNeSERLFAVVRRLQRQGIGIVFISHRIHELkAVCDTLTVLRDGRLIESG 225
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTI-VEADTILVLHRGQAVEQG 556
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-225 |
6.44e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG---------THAHYEGEVVINNQSVSiRSPRD 76
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagSHIELLGRTVQREGRLA-RDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 AKQLGIHLVQQevdVALVPGLSIAENIMLDRLAEPGI---AFRW--GRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQ 151
Cdd:PRK09984 84 SRANTGYIFQQ---FNLVNRLSVLENVLIGALGSTPFwrtCFSWftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 152 ILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-229 |
6.46e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.27 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirsprdakqlgihLVqqEVDVALVPGL 97
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA-------------LL--ELGAGFHPEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 SIAENIMLDrlaepgiafrwGRLRQLAR----------EALAQLDVSLD-----------VRrsidsctlaekqqilLAR 156
Cdd:COG1134 104 TGRENIYLN-----------GRLLGLSRkeidekfdeiVEFAELGDFIDqpvktyssgmrAR---------------LAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 157 ALSHHCRF--LILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMAD 229
Cdd:COG1134 158 AVATAVDPdiLLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-237 |
7.25e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDA-KQLG 81
Cdd:PRK13647 3 NIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 ihLVQQ-----------EVDVALVP---GLSIAEniMLDRLAEpgiAFRWGRLRQLAREALAQLdvsldvrrsidscTLA 147
Cdd:PRK13647 83 --LVFQdpddqvfsstvWDDVAFGPvnmGLDKDE--VERRVEE---ALKAVRMWDFRDKPPYHL-------------SYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 148 EKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPM 227
Cdd:PRK13647 143 QKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
250
....*....|
gi 503994372 228 ADLSGEQIVE 237
Cdd:PRK13647 223 SLLTDEDIVE 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-247 |
9.64e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.58 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGF--RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDA- 77
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 KQLGIhlVQQ-----------EVDVALvpGLsiaENI------MLDRLaepgiafrwgrlrqlaREALAQLDVSLDVRRS 140
Cdd:PRK13635 81 RQVGM--VFQnpdnqfvgatvQDDVAF--GL---ENIgvpreeMVERV----------------DQALRQVGMEDFLNRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 141 IDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHElKAVCDTLTVLRDG 219
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDE-AAQADRVIVMNKG 216
|
250 260
....*....|....*....|....*...
gi 503994372 220 RLIESGPmadlsGEQIVEkmLGHELSDI 247
Cdd:PRK13635 217 EILEEGT-----PEEIFK--SGHMLQEI 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-230 |
1.06e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.51 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVsiRSPRdakqLGIHLV 85
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPK----VDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDVA-----LVPGLSIAENIMLDRLAEPGIAFRwgRLRQLAREALAQldVSLDVRRSIDSCTLAEKQQ--ILLARAL 158
Cdd:PRK09493 76 RQEAGMVfqqfyLFPHLTALENVMFGPLRVRGASKE--EAEKQARELLAK--VGLAERAHHYPSELSGGQQqrVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-243 |
1.08e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.44 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSiRSP--RDAkQLGI 82
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPmhKRA-RLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQEvdvalvP----GLSIAENIM--LdRLAEPGIAFRWGRLRQLareaLAQLDVSlDVRRSIDScTLA--EKQQILL 154
Cdd:COG1137 81 GYLPQE------AsifrKLTVEDNILavL-ELRKLSKKEREERLEEL----LEEFGIT-HLRKSKAY-SLSggERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 155 ARALSHHCRFLILDEPTAPLD-------QNeserlfaVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPM 227
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiavadiQK-------IIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTP 220
|
250
....*....|....*..
gi 503994372 228 ADLSGEQIVEKM-LGHE 243
Cdd:COG1137 221 EEILNNPLVRKVyLGED 237
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
271-471 |
1.11e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSQPwrprdpadsvARGLALVPEErrkegifIEEP 350
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP--TSGTVRRAG----------GARVAYVPQR-------SEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNLAVSADSSFSRWslfGHRQAWRW--------AEEVIARVGIRTSGPAQtLRRLSGGNQQKVAIGKWLRGNANVLIF 422
Cdd:NF040873 68 DSLPLTVRDLVAMGRW---ARRGLWRRltrddraaVDDALERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503994372 423 DEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASgEFAELVGLCDRICVL 471
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVT-HDLELVRRADPCVLL 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
248-493 |
1.12e-13 |
|
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: 73.26 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 248 FPPKRPPHSDEVLLQVEGLH------DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQP 319
Cdd:COG4987 321 EPAEPAPAPGGPSLELEDVSfrypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP--QSGSitLGGVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 320 WRPRDPADsVARGLALVPEERRkegIFiEEPVAMNLAVSADSSfsrwslfGHRQAWrwaeEVIARVGIRT--SGPAQTL- 396
Cdd:COG4987 399 LRDLDEDD-LRRRIAVVPQRPH---LF-DTTLRENLRLARPDA-------TDEELW----AALERVGLGDwlAALPDGLd 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 397 -------RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAReGKGVIYASGEFAELvGLCDRIC 469
Cdd:COG4987 463 twlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGL-ERMDRIL 540
|
250 260
....*....|....*....|....
gi 503994372 470 VLWDGRIVAEIPGAEAREENILYY 493
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
261-488 |
1.17e-13 |
|
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: 70.67 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGL-----HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGELNSqpwrprDPADSVARGLAL 335
Cdd:cd03256 1 IEVENLsktypNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV--EPTSGSVLI------DGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 336 VPEERRKEG-IF-----IEE-PVAMNLAVSADSSFSRW-SLFG--HRQAWRWAEEVIARVGIRTSGPAQTlRRLSGGNQQ 405
Cdd:cd03256 73 LRQLRRQIGmIFqqfnlIERlSVLENVLSGRLGRRSTWrSLFGlfPKEEKQRALAALERVGLLDKAYQRA-DQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 406 KVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIyASGEFAELV-GLCDRICVLWDGRIVAEIPGA 483
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVI-VSLHQVDLArEYADRIVGLKDGRIVFDGPPA 230
|
....*
gi 503994372 484 EAREE 488
Cdd:cd03256 231 ELTDE 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-225 |
1.21e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlgIHLV 85
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA--IREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDVA-----LVPGLSIAENimldrLAEPGIafrwgRLRQLAR-EALAQLDVSLDVRRsidsctLAEK---------- 149
Cdd:PRK11124 81 RRNVGMVfqqynLWPHLTVQQN-----LIEAPC-----RVLGLSKdQALARAEKLLERLR------LKPYadrfplhlsg 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 150 ---QQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK11124 145 gqqQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
261-476 |
1.40e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 69.87 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGELnsqpwrpRDPADSVARGLALV 336
Cdd:cd03262 1 IEIKNLHksfgDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE--PDSGTI-------IIDGLKLTDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 337 PEERRKegifieepVAMnlavsadsSFSRWSLFGHR-------------------QAWRWAEEVIARVGI---RTSGPAQ 394
Cdd:cd03262 72 NELRQK--------VGM--------VFQQFNLFPHLtvlenitlapikvkgmskaEAEERALELLEKVGLadkADAYPAQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 395 tlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGE--FAELVGlcDRICVLW 472
Cdd:cd03262 136 ----LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEmgFAREVA--DRVIFMD 209
|
....
gi 503994372 473 DGRI 476
Cdd:cd03262 210 DGRI 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-230 |
1.55e-13 |
|
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: 69.95 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFS-GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQ---SVSIRSPRdaKQLG 81
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirEVTLDSLR--RAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 82 IhlVQQevDVALVPGlSIAENImldrlaepgiafRWGRL-------RQLAREAlaqldvslDVRRSIDSCTLA------- 147
Cdd:cd03253 79 V--VPQ--DTVLFND-TIGYNI------------RYGRPdatdeevIEAAKAA--------QIHDKIMRFPDGydtivge 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 148 --------EKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLqRQGIGIVFISHRIHELKAvCDTLTVLRDG 219
Cdd:cd03253 134 rglklsggEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDG 211
|
250
....*....|.
gi 503994372 220 RLIESGPMADL 230
Cdd:cd03253 212 RIVERGTHEEL 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-230 |
1.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.99 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFR-ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLgIHL 84
Cdd:PRK13652 4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQ-----------EVDVALVPglsiaENIMLDrlaEPGIAFRwgrlrqlAREALAQLDVSLDVRRSIDSCTLAEKQQIL 153
Cdd:PRK13652 83 VFQnpddqifsptvEQDIAFGP-----INLGLD---EETVAHR-------VSSALHMLGLEELRDRVPHHLSGGEKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 154 LARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-230 |
1.64e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSI--RSPRDAKQLGIHLVQQEVDVALVPGLS 98
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 IAENI-----MLDRLAEpgiAFRWGRLRQLAReaLAQLDVSLDVRRSiDSCTLAEKQQILLARALSHHCRFLILDEPTAP 173
Cdd:PRK10419 108 VREIIreplrHLLSLDK---AERLARASEMLR--AVDLDDSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 174 LDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-230 |
1.78e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF---SG-FR-----ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV-----SI 71
Cdd:PRK15112 5 LEVRNLSKTFryrTGwFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 72 RSPRdakqlgIHLVQQEVDVALVPGLSIAEniMLD---RLAEpgiafrwgRLRQLARE-----ALAQLDVSLDvRRSIDS 143
Cdd:PRK15112 85 RSQR------IRMIFQDPSTSLNPRQRISQ--ILDfplRLNT--------DLEPEQREkqiieTLRQVGLLPD-HASYYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 144 CTLA--EKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQ-RQGIGIVFISHRIHELKAVCDTLTVLRDGR 220
Cdd:PRK15112 148 HMLApgQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
250
....*....|
gi 503994372 221 LIESGPMADL 230
Cdd:PRK15112 228 VVERGSTADV 237
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
35-223 |
2.45e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 35 ALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSI-----RSPRDAKQLGihLVQQEVdvALVPGLSIAENIMLDRLA 109
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeaRAKLRAKHVG--FVFQSF--MLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 110 EpGIAFRwgRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL 189
Cdd:PRK10584 116 R-GESSR--QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
|
170 180 190
....*....|....*....|....*....|....*
gi 503994372 190 QR-QGIGIVFISHRIhELKAVCDTLTVLRDGRLIE 223
Cdd:PRK10584 193 NReHGTTLILVTHDL-QLAARCDRRLRLVNGQLQE 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-263 |
2.47e-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: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG----ThahyEGEVVINNQSVSIRSPRD- 76
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlerpT----SGSVLVDGVDLTALSEREl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 -AKQLGIHLVQQevDVALVPGLSIAENIMLD-RLAepgiafRWGRLRQLAR-EALAQLdVSLDVRRSidsctlA------ 147
Cdd:COG1135 78 rAARRKIGMIFQ--HFNLLSSRTVAENVALPlEIA------GVPKAEIRKRvAELLEL-VGLSDKAD------Aypsqls 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 148 --EKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIES 224
Cdd:COG1135 143 ggQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 503994372 225 GPMADL---SGEQIVEKMLGHELSDIFPPK-----RPPHSDEVLLQV 263
Cdd:COG1135 223 GPVLDVfanPQSELTRRFLPTVLNDELPEEllarlREAAGGGRLVRL 269
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-238 |
2.84e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.11 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINN--------------QSVS 70
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkksllevrKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 71 I--RSPRDakQLGIHLVQQevDVALVP---GLSIAEnimldrlaepgiafrwgrLRQLAREALAQLDVSLDVRRSIDSCT 145
Cdd:PRK13639 82 IvfQNPDD--QLFAPTVEE--DVAFGPlnlGLSKEE------------------VEKRVKEALKAVGMEGFENKPPHHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 146 LAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK13639 140 GGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
250
....*....|....
gi 503994372 226 -PMADLSGEQIVEK 238
Cdd:PRK13639 220 tPKEVFSDIETIRK 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-202 |
3.03e-13 |
|
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: 72.01 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSG-FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLgIH 83
Cdd:TIGR02868 334 TLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQEvdvALVPGLSIAENIMLDRL----AEPGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCtlAEKQQILLARALS 159
Cdd:TIGR02868 413 VCAQD---AHLFDTTVRENLRLARPdatdEELWAALERVGLADWLRALPDGLDTVLGEGGARLSG--GERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVRRLQrQGIGIVFISHR 202
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-230 |
3.04e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG--FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV---SIRSPRDAkql 80
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLASLRNQ--- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 gIHLVQQEV----DvalvpglSIAENIMLDRLAEpgiaFRWGRLRQLAREALA-----QLDVSLDVRRSIDSCTLA--EK 149
Cdd:PRK11176 419 -VALVSQNVhlfnD-------TIANNIAYARTEQ----YSREQIEEAARMAYAmdfinKMDNGLDTVIGENGVLLSggQR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 150 QQILLARALSHHCRFLILDEPTAPLDqNESER-LFAVVRRLQRQGIGIVfISHRIHEL-KAvcDTLTVLRDGRLIESGPM 227
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALD-TESERaIQAALDELQKNRTSLV-IAHRLSTIeKA--DEILVVEDGEIVERGTH 562
|
...
gi 503994372 228 ADL 230
Cdd:PRK11176 563 AEL 565
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-225 |
3.09e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 69.98 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL---GIHLVQQevDVALVPG 96
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQ--SFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 97 LSIAENIMLDrLAEPGIAfRWGRLRQlAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLD- 175
Cdd:cd03294 117 RTVLENVAFG-LEVQGVP-RAEREER-AAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDp 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 176 ------QNEserLFAVVRRLQRQgigIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03294 194 lirremQDE---LLRLQAELQKT---IVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
251-479 |
3.79e-13 |
|
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: 71.71 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 251 KRPPHSDEVLLQVEGLH-----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGasKSRLTRGE--LNSQPWRPR 323
Cdd:COG4988 327 APLPAAGPPSIELEDVSfsypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG--FLPPYSGSilINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 324 DPaDSVARGLALVPEERRkegIFiEEPVAMNLavsadssfsrwsLFGHRQAWRWA-EEVIARVGIRT---SGPA--QTL- 396
Cdd:COG4988 405 DP-ASWRRQIAWVPQNPY---LF-AGTIRENL------------RLGRPDASDEElEAALEAAGLDEfvaALPDglDTPl 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 397 ----RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAReGKGVIYASGEfAELVGLCDRICVLW 472
Cdd:COG4988 468 geggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHR-LALLAQADRILVLD 545
|
....*..
gi 503994372 473 DGRIVAE 479
Cdd:COG4988 546 DGRIVEQ 552
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-221 |
4.16e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 3 GNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNqsvsirSPRDAKQLGI 82
Cdd:PRK11247 10 GTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT------APLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQevDVALVPGLSIAENIMLdrlaepGIAFRWgrlRQLAREALAQldVSLDVRRSIDSCTLA--EKQQILLARALSH 160
Cdd:PRK11247 84 RLMFQ--DARLLPWKKVIDNVGL------GLKGQW---RDAALQALAA--VGLADRANEWPAALSggQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 161 HCRFLILDEPTAPLD-------QNESERLFavvrrlQRQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:PRK11247 151 RPGLLLLDEPLGALDaltriemQDLIESLW------QQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
4.29e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.49 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFS-GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSV--SIRSPRDA 77
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 KQlGIHLVQQEVDVALVPGlSIAENIMLDRLaepGIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARA 157
Cdd:PRK13636 81 RE-SVGMVFQDPDNQLFSA-SVYQDVSFGAV---NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 158 LSHHCRFLILDEPTAPLD-QNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-230 |
5.65e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 10 NISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHA-----HYEGEVVINNQSvsIRSPRDA----KQL 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRS--IFNYRDVlefrRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIhLVQQEVDVALvpglSIAENIMLDRLAEPGIAFRwgRLRQLAREALAQLDVSLDVRRSIDSCTL----AEKQQILLAR 156
Cdd:PRK14271 104 GM-LFQRPNPFPM----SIMDNVLAGVRAHKLVPRK--EFRGVAQARLTEVGLWDAVKDRLSDSPFrlsgGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQgIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-231 |
6.50e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGFR-ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVI---NNQSVSIRSPRDAkql 80
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtDIRTVTRASLRRN--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 gIHLVQQEvdvalvPGL---SIAENIMLDR----LAEpgiafrwgrLRqLAREALAQLDVSLdvRRSIDSCTLA------ 147
Cdd:PRK13657 411 -IAVVFQD------AGLfnrSIEDNIRVGRpdatDEE---------MR-AAAERAQAHDFIE--RKPDGYDTVVgergrq 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 148 ----EKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLqRQGIGIVFISHRIHELKAVcDTLTVLRDGRLIE 223
Cdd:PRK13657 472 lsggERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNA-DRILVFDNGRVVE 549
|
....*...
gi 503994372 224 SGPMADLS 231
Cdd:PRK13657 550 SGSFDELV 557
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-229 |
6.87e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.83 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD--AKQL 80
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQEVDvaLVPGLSIAENIMLD-RLAepgiafRWGRLRQLAR-EALAQLdVSLDVRRSIDSCTLA--EKQQILLAR 156
Cdd:PRK11153 83 QIGMIFQHFN--LLSSRTVFDNVALPlELA------GTPKAEIKARvTELLEL-VGLSDKADRYPAQLSggQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMAD 229
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-233 |
8.66e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGtHAHY---EGEVVINNQSVSIRSPRDA 77
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYkilEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 KQLGIHLV-QQEVDvalVPGLSiaeNIMLDRLA-------------EPgIAFrwgrlRQLAREAL--AQLDVSLDVRRSI 141
Cdd:CHL00131 82 AHLGIFLAfQYPIE---IPGVS---NADFLRLAynskrkfqglpelDP-LEF-----LEIINEKLklVGMDPSFLSRNVN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 142 DSCTLAEK------QQILLARALShhcrflILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVC-DTLT 214
Cdd:CHL00131 150 EGFSGGEKkrneilQMALLDSELA------ILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVH 223
|
250
....*....|....*....
gi 503994372 215 VLRDGRLIESGPmADLSGE 233
Cdd:CHL00131 224 VMQNGKIIKTGD-AELAKE 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
272-476 |
9.21e-13 |
|
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: 67.43 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGasKSRLTRGELnsqpwRPRDPADSVARGLAlVPEERRKEG-IFIEEP 350
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYK--EELPTSGTI-----RVNGQDVSDLRGRA-IPYLRRKIGvVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNLAVSADSSFS-RWSLFGHRQAWRWAEEVIARVGIRT---SGPAQtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPT 426
Cdd:cd03292 89 LLPDRNVYENVAFAlEVTGVPPREIRKRVPAALELVGLSHkhrALPAE----LSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503994372 427 KGVDVKAKTDLFNAIDGLAREGKGVIYASGEfAELVG-LCDRICVLWDGRI 476
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATHA-KELVDtTRHRVIALERGKL 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
271-493 |
1.09e-12 |
|
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: 70.25 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGE--LNSQPWRPRDPAdSVARGLALVPEERRkegIF-- 346
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY--EPTSGRilIDGIDLRQIDPA-SLRRQIGVVLQDVF---LFsg 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 -IEEpvamNLAVSADS-SFSRWslfghRQAWRWA--EEVIAR--------VGIRTSGpaqtlrrLSGGNQQKVAIGKWLR 414
Cdd:COG2274 564 tIRE----NITLGDPDaTDEEI-----IEAARLAglHDFIEAlpmgydtvVGEGGSN-------LSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLAReGKGVIYASGEfAELVGLCDRICVLWDGRIVAEIPGAEAREENILYY 493
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-225 |
1.11e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIrsPRDAKQLGIHLVQQEVDVAL-----VP 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF--GKDIFQIDAIKLRKEVGMVFqqpnpFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 96 GLSIAENIMLDrLAEPGIAFRwGRLRQLAREALAQLDVSLDVRRSIDS----CTLAEKQQILLARALSHHCRFLILDEPT 171
Cdd:PRK14246 104 HLSIYDNIAYP-LKSHGIKEK-REIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 172 APLDQNESERLFAVVRRLQRQgIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-220 |
1.19e-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: 65.16 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVvinnqsvsirsprdakqlgihLV 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------TW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDVALVPGLSiaenimldrlaePGiafrwgrlrqlarealaqldvsldvrrsidsctlaEKQQILLARALSHHCRFL 165
Cdd:cd03221 60 GSTVKIGYFEQLS------------GG-----------------------------------EKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 166 ILDEPTAPLDQnesERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGR 220
Cdd:cd03221 93 LLDEPTNHLDL---ESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
261-479 |
1.22e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVeGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQP---WRPRdpadSVARGLALVP 337
Cdd:PRK11231 8 LTV-GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismLSSR----QLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 338 EER-RKEGIFIEEPVAMNLavsadssfSRW-SLFGhrqawRWAEEVIARVgirTSGPAQT---------LRRLSGGNQQK 406
Cdd:PRK11231 83 QHHlTPEGITVRELVAYGR--------SPWlSLWG-----RLSAEDNARV---NQAMEQTrinhladrrLTDLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 407 VAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
272-481 |
1.22e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 67.38 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGE--LNSQpwrprDPADSVARGLALVpeeRRKE-G-IF- 346
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL--GGLDRPTSGEvlIDGQ-----DISSLSERELARL---RRRHiGfVFq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 ---------IEEPVAMNLAVSADSsfsrwslfgHRQAWRWAEEVIARVGI---RTSGPAQtlrrLSGGNQQKVAIGKWLR 414
Cdd:COG1136 94 ffnllpeltALENVALPLLLAGVS---------RKERRERARELLERVGLgdrLDHRPSQ----LSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEfAELVGLCDRICVLWDGRIVAEIP 481
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRIVSDER 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-478 |
1.62e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 9 QNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLVQQE 88
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMPQG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 89 VDVALVPGLSIAENImldrlaepgiAFrWGRLRQLAREalaqldvslDVRRSIDSCTLAE-----------------KQQ 151
Cdd:NF033858 85 LGKNLYPTLSVFENL----------DF-FGRLFGQDAA---------ERRRRIDELLRATglapfadrpagklsggmKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 152 ILLARALSHHCRFLILDEPTA---PLdqneSERLF----AVVRRlQRQGIGiVFISHRIHELKAVCDTLTVLRDGRLIES 224
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTgvdPL----SRRQFweliDRIRA-ERPGMS-VLVATAYMEEAERFDWLVAMDAGRVLAT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 225 GPMADL---SGEQIVE----KML------GHELSDIfPPKRPPHSDEVLLQVEGLH---------DegllqDISLRLRKG 282
Cdd:NF033858 219 GTPAELlarTGADTLEaafiALLpeekrrGHQPVVI-PPRPADDDDEPAIEARGLTmrfgdftavD-----HVSFRIRRG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 283 EILGIAGLAGAGKTELCKALFG---AS--KSRL-----------TR-------------GELnsqpwrprdpadSVARGL 333
Cdd:NF033858 293 EIFGFLGSNGCGKSTTMKMLTGllpASegEAWLfgqpvdagdiaTRrrvgymsqafslyGEL------------TVRQNL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 334 AL------VPEERRKEGifIEEPVA-MNLAVSADSSFSRWSLfGHRQawrwaeeviarvgirtsgpaqtlrRLSggnqQK 406
Cdd:NF033858 361 ELharlfhLPAAEIAAR--VAEMLErFDLADVADALPDSLPL-GIRQ------------------------RLS----LA 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 407 VAIgkwLRGnANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEF---AElvgLCDRICVLWDGRIVA 478
Cdd:NF033858 410 VAV---IHK-PELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFmneAE---RCDRISLMHAGRVLA 477
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-230 |
1.74e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.47 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF--SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlGIH 83
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ-AIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 LVQQEVDV---ALVPGLSIA-ENIMLDRLAEPgiafrwgrLRQLAREALAQLDVSLDvrrsidsCTL---------AEKQ 150
Cdd:PRK11160 418 VVSQRVHLfsaTLRDNLLLAaPNASDEALIEV--------LQQVGLEKLLEDDKGLN-------AWLgeggrqlsgGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 151 QILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQrQGIGIVFISHRIHELKAVcDTLTVLRDGRLIESGPMADL 230
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-232 |
1.86e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDA--- 77
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 ----KQLG-----IHLVQQEVDvaLVPGLSIAENIMLDRLAEPGIAfrwgrlRQLARE-ALAQLD-VSLDVRRSID---S 143
Cdd:PRK10619 81 vadkNQLRllrtrLTMVFQHFN--LWSHMTVLENVMEAPIQVLGLS------KQEARErAVKYLAkVGIDERAQGKypvH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 144 CTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIE 223
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
....*....
gi 503994372 224 SGPMADLSG 232
Cdd:PRK10619 233 EGAPEQLFG 241
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
272-478 |
2.29e-12 |
|
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: 66.46 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADsVARGLALVPEERR------KEGI 345
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQDVTlfygtlRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 FIEEPVAMNLAVSADSSFSRWSLFGHRQAWRWAEEViarvGIRTSGpaqtlrrLSGGNQQKVAIGKWLRGNANVLIFDEP 425
Cdd:cd03245 99 TLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQI----GERGRG-------LSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 426 TKGVDVKAKTDLFNAIDGLAReGKGVIYASGEFAELVgLCDRICVLWDGRIVA 478
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLD-LVDRIIVMDSGRIVA 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-259 |
2.41e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIhlV 85
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDvaLVPGLSIAENIMLdrlaepgIAFRWGRLRQLAREAL------AQLDVSLDVRRSIDSCTLaeKQQILLARALS 159
Cdd:PRK13537 86 PQFDN--LDPDFTVRENLLV-------FGRYFGLSAAAARALVppllefAKLENKADAKVGELSGGM--KRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLsgeqiVEKM 239
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL-----IESE 229
|
250 260
....*....|....*....|
gi 503994372 240 LGHELSDIFPPKRPPHSDEV 259
Cdd:PRK13537 230 IGCDVIEIYGPDPVALRDEL 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-267 |
2.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.45 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSprdaKQLGIHLVQQEVDVAL-VPGL 97
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS----KQKEIKPVRKKVGVVFqFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 SIAENIMLDRLAEPGIAFRWGR--LRQLAREALAQLDVSLDV-RRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPL 174
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKekAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 175 DQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEqiVEKMLGHELSdifPPKRPP 254
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE--VDFLKAHELG---VPKATH 250
|
250
....*....|...
gi 503994372 255 HSDEvlLQVEGLH 267
Cdd:PRK13643 251 FADQ--LQKTGAV 261
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-219 |
3.27e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDaKQLGihLV 85
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-RKVG--FV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEvdVALVPGLSIAENI-----MLDRLAEPGIAFrwgrLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSH 160
Cdd:PRK10851 80 FQH--YALFRHMTVFDNIafgltVLPRRERPNAAA----IKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDG 219
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
259-490 |
4.33e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.33 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 259 VLLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQP---WRPRDpadsVAR 331
Cdd:PRK13548 1 AMLEARNLSvrlgGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladWSPAE----LAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 332 GLALVPEERRKEGIF-IEEPVAMNLAVsadssfsrWSLfGHRQAWRWAEEVIARVGIrtSGPAQTL-RRLSGGNQQKVAI 409
Cdd:PRK13548 77 RRAVLPQHSSLSFPFtVEEVVAMGRAP--------HGL-SRAEDDALVAAALAQVDL--AHLAGRDyPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 410 GKWL------RGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIyasgefAELVGL------CDRICVLWDGRI 476
Cdd:PRK13548 146 ARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVI------VVLHDLnlaaryADRIVLLHQGRL 219
|
250
....*....|....*
gi 503994372 477 VAEIPGAEA-REENI 490
Cdd:PRK13548 220 VADGTPAEVlTPETL 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
4.77e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 66.31 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNISLAFSGFRA--LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDA-KQL 80
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQE---------VDVALvpGLsiaENIMLDrlaepgiafrWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQ 151
Cdd:PRK13648 86 GIVFQNPDnqfvgsivkYDVAF--GL---ENHAVP----------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 152 ILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQR-QGIGIVFISHRIHElKAVCDTLTVLRDGRLIESG 225
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSE-AMEADHVIVMNKGTVYKEG 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
267-477 |
5.31e-12 |
|
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: 65.78 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 267 HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRL---TRGEL--NSQPWRPRDPAdsvarglalvpEERR 341
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-----NRLiepTSGEIfiDGEDIREQDPV-----------ELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 342 KEGIFIEE----P---VAMNLAVSAdsSFSRWSlfgHRQAWRWAEEVIARVGIrtsGPAQTLRR----LSGGNQQKVAIG 410
Cdd:cd03295 76 KIGYVIQQiglfPhmtVEENIALVP--KLLKWP---KEKIRERADELLALVGL---DPAEFADRypheLSGGQQQRVGVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 411 KWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
272-479 |
5.56e-12 |
|
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: 65.08 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGELNSQPWRPRDPADSVARGLALVPEERrkegifieepv 351
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKML--TTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDL----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 amnlavSADSSFSRWS---LFGHRQAWRWAE------EVIARVGIrTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIF 422
Cdd:cd03265 83 ------SVDDELTGWEnlyIHARLYGVPGAErreridELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 423 DEPTKGVDVKAKTDLFNAIDGL-AREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-214 |
5.92e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvalVPGLSIAENImldrlaepgiAFRWgRLRQLA------REALAQLDVSLDV-RRSIDSCTLAEKQQILLARAL 158
Cdd:PRK10247 88 QTPT----LFGDTVYDNL----------IFPW-QIRNQQpdpaifLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQR-QGIGIVFISHRIHELKAVCDTLT 214
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEINHADKVIT 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
272-477 |
7.01e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 64.58 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTRGELNSQPWRPRDpadsvaRGLALVPEERrkeGIFIE 348
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleePTSGRIYIGGRDVTDLPPKD------RDIAMVFQNY---ALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 EPVAMNLAvsadssfsrwslFGHRQAWRWAEEVIARVgirtSGPAQTL----------RRLSGGNQQKVAIGKWLRGNAN 418
Cdd:cd03301 87 MTVYDNIA------------FGLKLRKVPKDEIDERV----REVAELLqiehlldrkpKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 419 VLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-196 |
7.81e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 64.30 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirSPRDAKQLGIHLV 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA--EQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVdvALVPGLSIAENIMLdrlaepgiafrWGRLRQLAR----EALAQldVSLDVRRSIDSCTLAEKQQ--ILLARALS 159
Cdd:TIGR01189 79 GHLP--GLKPELSALENLHF-----------WAAIHGGAQrtieDALAA--VGLTGFEDLPAAQLSAGQQrrLALARLWL 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVR-RLQRQGIGI 196
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRaHLARGGIVL 181
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
272-491 |
7.91e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.78 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRltRGELNSQPWRPRDPADsvarglalVPEERRKEGIFIEEPV 351
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGIDTGDFSK--------LQGIRKLVGIVFQNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 A--MNLAVSADSSFSRWSL-FGHRQAWRWAEEVIARVGI---RTSGPaqtlRRLSGGNQQKVAIGKWLRGNANVLIFDEP 425
Cdd:PRK13644 88 TqfVGRTVEEDLAFGPENLcLPPIEIRKRVDRALAEIGLekyRHRSP----KTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 426 TKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELvGLCDRICVLWDGRIVaeipgAEAREENIL 491
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIV-----LEGEPENVL 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
271-477 |
8.05e-12 |
|
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: 64.98 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFG-ASKSRLTRGE--LNSQPWRPRDPADSVARGlalvpeerRKEGIFI 347
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTSGQilFNGQPRKPDQFQKCVAYV--------RQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 348 EE-PVAMNLAVSADSSFSRWSLFGHRQAwRWAEEVIARVGIRTSGpAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPT 426
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKK-RVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 427 KGVDVKAKTDLFNAIDGLAREGKGV---IYASGefAELVGLCDRICVLWDGRIV 477
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIViltIHQPR--SDLFRLFDRILLLSSGEIV 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
271-475 |
8.38e-12 |
|
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: 63.56 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQPWRPRDPaDSVARGLALVPEErrkegIFIe 348
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP--TSGEilIDGVDLRDLDL-ESLRKNIAYVPQD-----PFL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 epvamnlavsadssFSRwslfghrqawrwaeeviarvgirtsgpaqTLRR--LSGGNQQKVAIGKWLRGNANVLIFDEPT 426
Cdd:cd03228 88 --------------FSG-----------------------------TIREniLSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503994372 427 KGVDVKAKTDLFNAIDGLaREGKGVIYASGEFAeLVGLCDRICVLWDGR 475
Cdd:cd03228 125 SALDPETEALILEALRAL-AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-205 |
1.38e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirSPrdAKQLGIhLV 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GP--GAERGV-VF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEvdvALVPGLSIAENIMLD-RLAEPGIAFRwgrlRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRF 164
Cdd:PRK11248 77 QNE---GLLPWRNVQDNVAFGlQLAGVEKMQR----LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503994372 165 LILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHE 205
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEE 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-239 |
1.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.68 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINN-----QSVSIRSPRdaKQLGihLVQQEVDVAL 93
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIR--KKVG--LVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 94 vpglsIAENIMLDrlaepgIAFRWGRLrqlareALAQLDVSLDVRRSIDSCTL---------------AEKQQILLARAL 158
Cdd:PRK13637 97 -----FEETIEKD------IAFGPINL------GLSEEEIENRVKRAMNIVGLdyedykdkspfelsgGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 159 SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEqiVE 237
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE--VE 237
|
..
gi 503994372 238 KM 239
Cdd:PRK13637 238 TL 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-221 |
1.85e-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: 63.64 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAF---SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIrspRDAKQL- 80
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ---YEHKYLh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 -GIHLVQQEvdvALVPGLSIAENIMldrLAEPGIAFrwGRLRQLAREALA-------QLDVSLDVRRSIDSCTLAEKQQI 152
Cdd:cd03248 88 sKVSLVGQE---PVLFARSLQDNIA---YGLQSCSF--ECVKEAAQKAHAhsfiselASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 153 LLARALSHHCRFLILDEPTAPLDQNESERLFAVVRR-LQRQgiGIVFISHRIHELKAVcDTLTVLRDGRL 221
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDwPERR--TVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-284 |
1.86e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.82 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAF--SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGT---HAHYEGEVVINNQSVSIRSPR 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 76 DAKQ-LGIhlVQQEVDVALVpGLSIAENIM--LDRLAEPGiafrwGRLRQLAREALAQLDVsLDVRRSIDS-CTLAEKQQ 151
Cdd:PRK13640 81 DIREkVGI--VFQNPDNQFV-GATVGDDVAfgLENRAVPR-----PEMIKIVRDVLADVGM-LDYIDSEPAnLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 152 ILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHElKAVCDTLTVLRDGRLIESG-PMad 229
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGsPV-- 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 230 lsgeqivekmlghelsDIFPpkrpphsDEVLLQVEGLhDEGLLQDISLRLRKGEI 284
Cdd:PRK13640 229 ----------------EIFS-------KVEMLKEIGL-DIPFVYKLKNKLKEKGI 259
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
242-474 |
1.94e-11 |
|
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: 66.96 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 242 HELSDIFPPKRPPHSDEVLLQVeglhdegllqdislrlRKGEILGIAGLAGAGKTELCKALFG-----------ASKSRL 310
Cdd:TIGR01257 1941 NELTKVYSGTSSPAVDRLCVGV----------------RPGECFGLLGVNGAGKTTTFKMLTGdttvtsgdatvAGKSIL 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 311 TR-GELN-SQPWRPR-DPADSVARGLALVPEERRKEGIFIEEPvamnlavsadssfsrwslfghrqawrwaeEVIARVGI 387
Cdd:TIGR01257 2005 TNiSDVHqNMGYCPQfDAIDDLLTGREHLYLYARLRGVPAEEI-----------------------------EKVANWSI 2055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 388 RTSGPAQTLRRL----SGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVG 463
Cdd:TIGR01257 2056 QSLGLSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEA 2135
|
250
....*....|.
gi 503994372 464 LCDRICVLWDG 474
Cdd:TIGR01257 2136 LCTRLAIMVKG 2146
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
272-484 |
2.12e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.53 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGEL-----NSQPWRPRDpadsvarglalVPEERRKEGI- 345
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE--RPTSGQVlvngqDLSRLKRRE-----------IPYLRRRIGVv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 F----------IEEPVAMNLAVSAdssfsrwslFGHRQAWRWAEEVIARVGIRTSG---PAQtlrrLSGGNQQKVAIGKW 412
Cdd:COG2884 85 FqdfrllpdrtVYENVALPLRVTG---------KSRKEIRRRVREVLDLVGLSDKAkalPHE----LSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 413 LRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEfAELVGLCD-RICVLWDGRIVAEIPGAE 484
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD-LELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
260-479 |
2.13e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLHDEGLLQD-ISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPadsVARG-LALVP 337
Cdd:PRK13537 10 FRNVEKRYGDKLVVDgLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR---HARQrVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 338 EERRKEGIFieePVAMNLAVsadssFSRWSLFGHRQAWRWAEEVIARVGIRTSGPAQtLRRLSGGNQQKVAIGKWLRGNA 417
Cdd:PRK13537 87 QFDNLDPDF---TVRENLLV-----FGRYFGLSAAAARALVPPLLEFAKLENKADAK-VGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 418 NVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
271-493 |
2.24e-11 |
|
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: 63.66 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrltrgelnsqPWRPRDPADSVARGLALVPEERRKEGIFIEEP 350
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV-----------PENGRVLVDGHDLALADPAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNLAVSADSSFSRWSLFGHR--QAWRW--AEEVIAR--------VGIRTSGpaqtlrrLSGGNQQKVAIGKWLRGNAN 418
Cdd:cd03252 86 VLFNRSIRDNIALADPGMSMERviEAAKLagAHDFISElpegydtiVGEQGAG-------LSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 419 VLIFDEPTKGVDVKAKTDLF-NAIDGLAreGKGVIYASGEFAElVGLCDRICVLWDGRIVAEIPGAEAREENILYY 493
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMrNMHDICA--GRTVIIIAHRLST-VKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
261-478 |
2.27e-11 |
|
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: 63.89 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH---DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADsvaRGLALVP 337
Cdd:cd03299 1 LKVENLSkdwKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 338 EERrkeGIFIEEPVAMNLAvsadssfsrwslFGHRQAWRWAEEVIARVgIRTS---GPAQTL----RRLSGGNQQKVAIG 410
Cdd:cd03299 78 QNY---ALFPHMTVYKNIA------------YGLKKRKVDKKEIERKV-LEIAemlGIDHLLnrkpETLSGGEQQRVAIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 411 KWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-225 |
2.42e-11 |
|
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: 63.20 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSGF--RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlGI 82
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS-SL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQevDVALVPGlSIAENimLDRLAEpgiafrwgrlrqlarEALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHC 162
Cdd:cd03369 85 TIIPQ--DPTLFSG-TIRSN--LDPFDE---------------YSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 163 RFLILDEPTAPLDQnESERLFAVVRRLQRQGIGIVFISHRIHELkAVCDTLTVLRDGRLIESG 225
Cdd:cd03369 145 RVLVLDEATASIDY-ATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYD 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-225 |
2.47e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 63.44 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG---THAHYEGEVVINNQsvsirsprdakQLGIHLVQQEV-----D 90
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQ-----------PRKPDQFQKCVayvrqD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 91 VALVPGLSIAENI-------MLDRLAEPGIAFRW--GRLRQLAREALAQldvslDVRRSIDSctlAEKQQILLARALSHH 161
Cdd:cd03234 90 DILLPGLTVRETLtytailrLPRKSSDAIRKKRVedVLLRDLALTRIGG-----NLVKGISG---GERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQRQGiGIVFIShrIH----ELKAVCDTLTVLRDGRLIESG 225
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRN-RIVILT--IHqprsDLFRLFDRILLLSSGEIVYSG 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
272-484 |
2.75e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.57 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGELNSQPWRPRDPAdsvarglALVPEERRKEGIFieepv 351
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE--ITSGDLIVDGLKVNDPK-------VDERLIRQEAGMV----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 amnlavsadssFSRWSLFGH-------------------RQAWRWAEEVIARVGIRTSG---PAQtlrrLSGGNQQKVAI 409
Cdd:PRK09493 83 -----------FQQFYLFPHltalenvmfgplrvrgaskEEAEKQARELLAKVGLAERAhhyPSE----LSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 410 GKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGE--FAELVGlcDRICVLWDGRIVAEIPGAE 484
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEigFAEKVA--SRLIFIDKGRIAEDGDPQV 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
268-479 |
2.98e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.85 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 268 DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG-ASKSRLTRGELNSQ-PWRPRdpadSVARGLALVPEERRKEgi 345
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGmTSPDAGKITVLGVPvPARAR----LARARIGVVPQFDNLD-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 fIEEPVAMNLAVsadssFSRWslfgHRQAWRWAEEVI------ARVGIRTSGPaqtLRRLSGGNQQKVAIGKWLRGNANV 419
Cdd:PRK13536 127 -LEFTVRENLLV-----FGRY----FGMSTREIEAVIpsllefARLESKADAR---VSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 420 LIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-201 |
3.00e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 62.51 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirSPRDAKQLGIHLV 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDVALVpgLSIAENIMLdrlaepgiafrWGRL--RQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCR 163
Cdd:cd03231 79 GHAPGIKTT--LSVLENLRF-----------WHADhsDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRP 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 503994372 164 FLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISH 201
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
272-479 |
3.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.95 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCK---ALFGASKSRL------TRGELNSqpWRPRDPADSVARGlalvPEERRK 342
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnALLIPSEGKVyvdgldTSDEENL--WDIRNKAGMVFQN----PDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 343 EGIfIEEPVAM---NLAVSADSSFSRwslfghrqawrwAEEVIARVGI---RTSGPaqtlRRLSGGNQQKVAIGKWLRGN 416
Cdd:PRK13633 100 ATI-VEEDVAFgpeNLGIPPEEIRER------------VDESLKKVGMyeyRRHAP----HLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 417 ANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
272-477 |
3.16e-11 |
|
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: 63.82 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRL---TRGE--LNSQPwrprDPADSVARGLALvpeeRRKE--- 343
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCI-----NRLiepTSGKvlIDGQD----IAAMSRKELREL----RRKKism 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 344 -----GIF----IEEPVAMNLAVSADSSFSRwslfgHRQAwrwaEEVIARVGIRTSGpAQTLRRLSGGNQQKVAIGKWLR 414
Cdd:cd03294 107 vfqsfALLphrtVLENVAFGLEVQGVPRAER-----EERA----AEALELVGLEGWE-HKYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-239 |
3.61e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.86 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSGFR--ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDA-KQLGIh 83
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKKIGI- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 lVQQ-----------EVDVALvpGLsiaENIMLDRLAEPGI----AFRWGRLRQLAREALaqldvsldvrrsidSCTLAE 148
Cdd:PRK13632 88 -IFQnpdnqfigatvEDDIAF--GL---ENKKVPPKKMKDIiddlAKKVGMEDYLDKEPQ--------------NLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 149 KQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIG-IVFISHRIHE-LKAvcDTLTVLRDGRLIESG- 225
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKtLISITHDMDEaILA--DKVIVFSEGKLIAQGk 225
|
250
....*....|....
gi 503994372 226 PMADLSGEQIVEKM 239
Cdd:PRK13632 226 PKEILNNKEILEKA 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
272-478 |
3.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELnsqpwRPRDPADSVARGLALVPEERRKEGIFIEEPV 351
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP--TEGKV-----TVGDIVVSSTSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 A--MNLAVSADSSFSRWSL-FGHRQAWRWAEEVIARVGIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKG 428
Cdd:PRK13643 95 SqlFEETVLKDVAFGPQNFgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503994372 429 VDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-225 |
3.79e-11 |
|
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: 61.95 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF--SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIh 83
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 84 lVQQEVDVAlvpGLSIAENImldrlaepGIAFRWGrlrqlarealaqldvsldvrrsidsctlaEKQQILLARALSHHCR 163
Cdd:cd03247 80 -LNQRPYLF---DTTLRNNL--------GRRFSGG-----------------------------ERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 164 FLILDEPTAPLD---QNESERLFAVVRRlqrqGIGIVFISHRIHELKAVcDTLTVLRDGRLIESG 225
Cdd:cd03247 119 IVLLDEPTVGLDpitERQLLSLIFEVLK----DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
255-477 |
5.12e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.02 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 255 HSDEVLLQVEGL-HDEGL---LQDISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGELNsqpWRPRdpaDSVA 330
Cdd:PRK11701 1 MMDQPLLSVRGLtKLYGPrkgCRDVSFDLYPGEVLGIVGESGSGKTTLLNAL--SARLAPDAGEVH---YRMR---DGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 331 RGLALVPEERRK-----EGIFIEEPVAMNL--AVSADSSFS-RWSLFGHR-------QAWRWAEeviaRVGIRTSGPAQT 395
Cdd:PRK11701 73 RDLYALSEAERRrllrtEWGFVHQHPRDGLrmQVSAGGNIGeRLMAVGARhygdiraTAGDWLE----RVEIDAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 396 LRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDG 474
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
...
gi 503994372 475 RIV 477
Cdd:PRK11701 229 RVV 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
274-478 |
5.14e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 63.97 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 274 DISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGE--LNSQPWRprdpaDSvARGLALvPEERRKEGIFIEEP- 350
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAI--AGLERPDSGRirLGGEVLQ-----DS-ARGIFL-PPHRRRIGYVFQEAr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 ------VAMNLavsadssfsrwsLFGHRQAWRWA-----EEVIARVGIR---TSGPAQtlrrLSGGNQQKVAIGKWLRGN 416
Cdd:COG4148 88 lfphlsVRGNL------------LYGRKRAPRAErrisfDEVVELLGIGhllDRRPAT----LSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 417 ANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKG-VIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-223 |
6.23e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVInnqsvsirsprdAKQLGIHLV 85
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------------GETVKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEVDvALVPGLSIAENIMldRLAEpgiafrwGRLRQLAREALAQL----DvslDVRRSIDSCTLAEKQQILLARALSHH 161
Cdd:COG0488 384 DQHQE-ELDPDKTVLDELR--DGAP-------GGTEQEVRGYLGRFlfsgD---DAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 162 CRFLILDEPTAPLDqneSERLFAVVRRLQR-QGiGIVFISHRIHELKAVCDTLTVLRDGRLIE 223
Cdd:COG0488 451 PNVLLLDEPTNHLD---IETLEALEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
271-478 |
7.62e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.70 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNsqpwrprdpADSVARGLALVPEERRKEGIFIEEP 350
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP--QSGEIK---------IDGITISKENLKEIRKKIGIIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VA--MNLAVSADSSFS-RWSLFGHRQAWRWAEEVIARVGIRtsgpaQTLRR----LSGGNQQKVAIGKWLRGNANVLIFD 423
Cdd:PRK13632 93 DNqfIGATVEDDIAFGlENKKVPPKKMKDIIDDLAKKVGME-----DYLDKepqnLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 424 EPTKGVDVKAKTDLFNAIDGLAREG-KGVIYASGEFAELVgLCDRICVLWDGRIVA 478
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-230 |
8.84e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.21 E-value: 8.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL--GIHLVQQEVDVALVPG 96
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrRMQMVFQDPYASLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 97 LSIAenimlDRLAEP----GIAFRWGRlRQLAREALAQldVSLDvrrsidsctlAE-------------KQQILLARALS 159
Cdd:COG4608 112 MTVG-----DIIAEPlrihGLASKAER-RERVAELLEL--VGLR----------PEhadryphefsggqRQRIGIARALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 160 HHCRFLILDEPTAPLD-----QneserlfaVV---RRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG4608 174 LNPKLIVCDEPVSALDvsiqaQ--------VLnllEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-233 |
9.23e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.05 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGE--VVINNQSVSIRSPRD-----AKQLgIHLVQQEVDv 91
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPdgrgrAKRY-IGILHQEYD- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 92 aLVPGLSIAEN----IMLDrlaepgIAFRWGRLRqlAREALAQLDVSLDVRRSI-----DSCTLAEKQQILLARALSHHC 162
Cdd:TIGR03269 376 -LYPHRTVLDNlteaIGLE------LPDELARMK--AVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 163 RFLILDEPTAPLDQNESERLFAVVRRlQRQGIGIVFI--SHRIHELKAVCDTLTVLRDGRLIESGPMADLSGE 233
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILK-AREEMEQTFIivSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-230 |
1.15e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAFSgfRAL-SNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTH----AHYEGEVVINNQSVsirSPRDAKQ 79
Cdd:PRK10418 4 QIELRNIALQAA--QPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPV---APCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 80 LGIHLVQQEVDVALVPGLSiaeniMLDRLAEPGIAFrwGRLRQLAREALAQLDVSL-DVRRSIDSCTLAEK----QQILL 154
Cdd:PRK10418 79 RKIATIMQNPRSAFNPLHT-----MHTHARETCLAL--GKPADDATLTAALEAVGLeNAARVLKLYPFEMSggmlQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 155 ARALSHHCRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
256-479 |
1.19e-10 |
|
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: 61.53 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 256 SDEVLLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKAL-------------FGASKSRLTRGELNsq 318
Cdd:COG1127 1 MSEPMIEVRNLTksfgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIigllrpdsgeilvDGQDITGLSEKELY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 319 pwrprdpadsvarglalvpEERRKEGI-F----------IEEPVA----MNLAVSADSSFSRwslfghrqawrwAEEVIA 383
Cdd:COG1127 79 -------------------ELRRRIGMlFqggalfdsltVFENVAfplrEHTDLSEAEIREL------------VLEKLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 384 RVGIRTSG---PAQtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFA 459
Cdd:COG1127 128 LVGLPGAAdkmPSE----LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLD 203
|
250 260
....*....|....*....|
gi 503994372 460 ELVGLCDRICVLWDGRIVAE 479
Cdd:COG1127 204 SAFAIADRVAVLADGKIIAE 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-200 |
1.37e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQ-LGi 82
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLvqqevdVALVPGLSIAENIMLDRlaepgiAFRWGRLRQLArEALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHC 162
Cdd:PRK13539 80 HR------NAMKPALTVAENLEFWA------AFLGGEELDIA-AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 503994372 163 RFLILDEPTAPLDqNESERLFA-VVRRLQRQGiGIVFIS 200
Cdd:PRK13539 147 PIWILDEPTAALD-AAAVALFAeLIRAHLAQG-GIVIAA 183
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-202 |
1.64e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQsvSIRSPRDAKQLGIHLVQQEVDVAlvPGLSIA 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ--SIKKDLCTYQKQLCFVGHRSGIN--PYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 101 ENIMLDrlaepgIAFRWGRLRQLAREALAQLDVSLDVrrsidSCTL---AEKQQILLARALSHHCRFLILDEPTAPLDQN 177
Cdd:PRK13540 93 ENCLYD------IHFSPGAVGITELCRLFSLEHLIDY-----PCGLlssGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 503994372 178 ESERLFAVVRRLQRQGIGIVFISHR 202
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
260-484 |
1.93e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 61.16 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRL---TRGE--LNSQPwrprdpadsVA 330
Cdd:COG1126 1 MIEIENLHksfgDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-----NLLeepDSGTitVDGED---------LT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 331 RGLALVPEERRKegifieepVAMnlaVsadssFSRWSLFGHR-------------------QAWRWAEEVIARVGI---R 388
Cdd:COG1126 67 DSKKDINKLRRK--------VGM---V-----FQQFNLFPHLtvlenvtlapikvkkmskaEAEERAMELLERVGLadkA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 389 TSGPAQtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVD---VKaktDLFNAIDGLAREGKGVIYASGE--FAELVg 463
Cdd:COG1126 131 DAYPAQ----LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEmgFAREV- 202
|
250 260
....*....|....*....|.
gi 503994372 464 lCDRICVLWDGRIVAEIPGAE 484
Cdd:COG1126 203 -ADRVVFMDGGRIVEEGPPEE 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
272-479 |
2.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.40 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPwrprdpADSVARGLAlvpEERRKEGIFIEEP- 350
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP------IDYSRKGLM---KLRESVGMVFQDPd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 -VAMNLAVSADSSFSRWSL-FGHRQAWRWAEEVIARVGIRTSGPAQTlRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKG 428
Cdd:PRK13636 93 nQLFSASVYQDVSFGAVNLkLPEDEVRKRVDNALKRTGIEHLKDKPT-HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503994372 429 VDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-445 |
2.68e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 3 GNRLEMQNISLAFsgfralsnvaftLTGGSVHALtGANGAGKSTLMAVLCGTHAHYEGEVvinnqsvsirspRDAKQLGI 82
Cdd:TIGR03719 16 PKKEILKDISLSF------------FPGAKIGVL-GLNGAGKSTLLRIMAGVDKDFNGEA------------RPQPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQEVDvaLVPGLSIAENIM---------LDRL-------AEPGIAF-----RWGRLRQL-----AREALAQLDVSLD 136
Cdd:TIGR03719 71 GYLPQEPQ--LDPTKTVRENVEegvaeikdaLDRFneisakyAEPDADFdklaaEQAELQEIidaadAWDLDSQLEIAMD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 137 VRR------SIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDqneSERLFAVVRRLQRQGIGIVFISHRIHELKAVC 210
Cdd:TIGR03719 149 ALRcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTHDRYFLDNVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 211 DTLTVLRDGRLI-----------------------ESGPMADLSGE-------------------QIVEKMLGH------ 242
Cdd:TIGR03719 226 GWILELDRGRGIpwegnysswleqkqkrleqeekeESARQKTLKRElewvrqspkgrqakskarlARYEELLSQefqkrn 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 243 ELSDIFPPKRPPHSDEVlLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASK---SRLTRGEl 315
Cdd:TIGR03719 306 ETAEIYIPPGPRLGDKV-IEAENLTkafgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpdsGTIEIGE- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 316 nsqpwrprdpadSVArgLALVPEerrkegifieepvamnlavsadssfSRWSLFGHRQAWrwaEEV-----IARVGIRT- 389
Cdd:TIGR03719 384 ------------TVK--LAYVDQ-------------------------SRDALDPNKTVW---EEIsggldIIKLGKREi 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 390 -----------SGPAQTLR--RLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLA 445
Cdd:TIGR03719 422 psrayvgrfnfKGSDQQKKvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA 490
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
272-479 |
2.91e-10 |
|
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: 60.25 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRpRDPADSVAR-GLALVPEErrkEGIFIEEP 350
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRARlGIGYLPQE---ASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNL-AVSADSSFSRWslfghrQAWRWAEEVIARVGIrtsgpaQTLR-----RLSGGNQQKVAIGKWLRGNANVLIFDE 424
Cdd:cd03218 92 VEENIlAVLEIRGLSKK------EREEKLEELLEEFHI------THLRkskasSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 425 PTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
272-477 |
3.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSqpwrprDPADSVARGLALvPEERRKEGI------ 345
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP--TSGKIII------DGVDITDKKVKL-SDIRKKVGLvfqype 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 --FIEEPVAMNLAvsadssfsrwslFGHRQAWRWAEEVIARV--GIRTSG-PAQTLR-----RLSGGNQQKVAIGKWLRG 415
Cdd:PRK13637 94 yqLFEETIEKDIA------------FGPINLGLSEEEIENRVkrAMNIVGlDYEDYKdkspfELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 416 NANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGK-GVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
267-478 |
3.52e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 267 HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGasksrLTRGELNSQPWRPRdPADSVARGLALVpeeRRKEGIF 346
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSG-----LLRPQKGAVLWQGK-PLDYSKRGLLAL---RQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 IEEPVAMNLAVSADSSFSrwslFGHRQAWRWAEEVIARVG-IRTSGPAQTLRR-----LSGGNQQKVAIGKWLRGNANVL 420
Cdd:PRK13638 83 FQDPEQQIFYTDIDSDIA----FSLRNLGVPEAEITRRVDeALTLVDAQHFRHqpiqcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 421 IFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-226 |
3.98e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.05 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-SG---FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL- 80
Cdd:PRK10535 5 LELKDIRRSYpSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 --GIHLVQQEVDvaLVPGLSIAENIMLdrlaePGIAFRWGRLRQLAR--EALAQLDVSLDVRRSIDSCTLAEKQQILLAR 156
Cdd:PRK10535 85 reHFGFIFQRYH--LLSHLTAAQNVEV-----PAVYAGLERKQRLLRaqELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 157 ALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRiHELKAVCDTLTVLRDGRLIESGP 226
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPP 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-298 |
4.35e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 62.54 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 128 LAQLDVS-LDVRRSIDSCTLAEKQQILLARALSHHCRFL--ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRiH 204
Cdd:PRK00635 460 LIDLGLPyLTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-E 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 205 ELKAVCDtltvlrdgRLIESGPMADLSGEQIV----------------EKMLGHELSDIFPPKRPPHSDEVLLQVEGLHD 268
Cdd:PRK00635 539 QMISLAD--------RIIDIGPGAGIFGGEVLfngspreflaksdsltAKYLRQELTIPIPEKRTNSLGTLTLSKATKHN 610
|
170 180 190
....*....|....*....|....*....|
gi 503994372 269 eglLQDISLRLRKGEILGIAGLAGAGKTEL 298
Cdd:PRK00635 611 ---LKDLTISLPLGRLTVVTGVSGSGKSSL 637
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-230 |
4.61e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.13 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL--GIHLVQQEVDVALVPG 96
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQNPYGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 97 LSIAenimlDRLAEP-------GIAFRwgrlRQLAREALAQldVSLD---VRRSIDSCTLAEKQQILLARALSHHCRFLI 166
Cdd:PRK11308 109 KKVG-----QILEEPllintslSAAER----REKALAMMAK--VGLRpehYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 167 LDEPTAPLD---QNESERLFAvvrRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK11308 178 ADEPVSALDvsvQAQVLNLMM---DLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
272-477 |
4.79e-10 |
|
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: 59.56 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE--LNSQPWRP----RDPADSVARGLALVPEERrkegi 345
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET--PTSGEilLDGKDITNlpphKRPVNTVFQNYALFPHLT----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 fieepVAMNLAvsadssfsrwslFGHRQAWRWAEEVIARV----------GIRTSGPAQtlrrLSGGNQQKVAIGKWLRG 415
Cdd:cd03300 89 -----VFENIA------------FGLRLKKLPKAEIKERVaealdlvqleGYANRKPSQ----LSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 416 NANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
264-477 |
5.11e-10 |
|
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: 59.20 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 264 EGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRL-TRGELnSQPWRPRDPADSVARGlalvpeerrk 342
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDI-HYNGIPYKEFAEKYPG---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 343 EGIFI-EEPVAM-NLAVSADSSFSRwSLFGHrqawrwaeeviarvgirtsgpaQTLRRLSGGNQQKVAIGKWLRGNANVL 420
Cdd:cd03233 84 EIIYVsEEDVHFpTLTVRETLDFAL-RCKGN----------------------EFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 421 IFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFA--ELVGLCDRICVLWDGRIV 477
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-246 |
6.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.23 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIR-SPRDAKQLgihlvQQEVDVAL-VPG 96
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtGNKNLKKL-----RKKVSLVFqFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 97 LSIAENIML-DRLAEP-GIAFRWGRLRQLAREALAQLDVSLDV-RRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAP 173
Cdd:PRK13641 96 AQLFENTVLkDVEFGPkNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 174 LDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIE-SGPMADLSGEQIVEKmlgHELSD 246
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKhASPKEIFSDKEWLKK---HYLDE 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
272-477 |
9.89e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.64 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKalfgasksrLTRGELNSQPWRPRDPADSVARGLALVPEE---RRKEGIFIE 348
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQ---------LTNGLIISETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 EP--VAMNLAVSADSSFSRWSLFGHRQ-AWRWAEEVIARVGIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEP 425
Cdd:PRK13645 98 FPeyQLFQETIEKDIAFGPVNLGENKQeAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 426 TKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
271-491 |
1.05e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQP---WRPRdpadSVARGLALVPEE-RRKEGIF 346
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPlesWSSK----AFARKVAYLPQQlPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 IEEPVAMNlAVSADSSFSRWSLFGHRQAwrwaEEVIARVGIRTSgpAQTL-RRLSGGNQQKVAIGKWLRGNANVLIFDEP 425
Cdd:PRK10575 102 VRELVAIG-RYPWHGALGRFGAADREKV----EEAISLVGLKPL--AHRLvDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 426 TKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAEAREENIL 491
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-221 |
1.09e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.35 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFR-ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDakqlgIHL 84
Cdd:PRK10908 2 IRFEHVSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE-----VPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 VQQEVDVALVPGLSIAENIMLDRLAEPGIaFRWGRLRQLAREALAQLDVS--LDVRRSID-SCTLAEKQQILLARALSHH 161
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVglLDKAKNFPiQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
272-479 |
1.26e-09 |
|
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: 58.36 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSqpwrprDPADSVARGLALVPEERRKEG------- 344
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERP--TSGSVLV------DGTDLTLLSGKELRKARRRIGmifqhfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 345 IFIEEPVAMNLAVSADssfsrwsLFGHRQAWRW--AEEVIARVGI---RTSGPAQtlrrLSGGNQQKVAIGKWLRGNANV 419
Cdd:cd03258 93 LLSSRTVFENVALPLE-------IAGVPKAEIEerVLELLELVGLedkADAYPAQ----LSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 420 LIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
272-477 |
1.26e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALfgasksRL----TRGEL---NSQPWRPRDPADSVARGLalvpeeRRKEG 344
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVL------NLletpDSGQLniaGHQFDFSQKPSEKAIRLL------RQKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 345 I----------------FIEEPVAMnLAVSADssfsrwslfghrQAWRWAEEVIARVGIRTSGPAQTLRrLSGGNQQKVA 408
Cdd:COG4161 86 MvfqqynlwphltvmenLIEAPCKV-LGLSKE------------QAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 409 IGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREG--KGVIYASGEFAELVGlcDRICVLWDGRIV 477
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGitQVIVTHEVEFARKVA--SQVVYMEKGRII 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
272-479 |
1.33e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG----ASKSRLTRGElnsqpwrprdPADSVARGLALVpeeRRKEGIFI 347
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGilkpTSGEVLIKGE----------PIKYDKKSLLEV---RKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 348 EEPVAMNLA--VSADSSFSRWSL-FGHRQAWRWAEEVIARVGIrtSGPAQTL-RRLSGGNQQKVAIGKWLRGNANVLIFD 423
Cdd:PRK13639 85 QNPDDQLFAptVEEDVAFGPLNLgLSKEEVEKRVKEALKAVGM--EGFENKPpHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 424 EPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEfAELVGL-CDRICVLWDGRIVAE 479
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD-VDLVPVyADKVYVMSDGKIIKE 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
254-477 |
1.39e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 254 PHSDEV----LLQVEGL----HDEGL----LQDISLRLRKGEILGIAGLAGAGKTELCKALFgasksRL---TRGELNSQ 318
Cdd:PRK10261 2 PHSDELdardVLAVENLniafMQEQQkiaaVRNLSFSLQRGETLAIVGESGSGKSVTALALM-----RLleqAGGLVQCD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 319 P-WRPRDPADSVARGLALVPEERRKEG-----IFIEEPVAMN----LAVSADSSFSRWSLFGHRQAWRWAEEVIARVGIR 388
Cdd:PRK10261 77 KmLLRRRSRQVIELSEQSAAQMRHVRGadmamIFQEPMTSLNpvftVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 389 TSGP--AQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLC 465
Cdd:PRK10261 157 EAQTilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIA 236
|
250
....*....|..
gi 503994372 466 DRICVLWDGRIV 477
Cdd:PRK10261 237 DRVLVMYQGEAV 248
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
272-481 |
1.42e-09 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 58.35 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTRGELNsqpWRPRDPADSVARGLALvpeeRRKEGIFIE 348
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGAPDEGEVL---LDGKDIYDLDVDVLEL----RRRVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 EPVAMNLAVSADSSFSRWSlfgHRQAWRWAEEVIARVGIRTSG-PAQTLRR-----LSGGNQQKVAIGKWLRGNANVLIF 422
Cdd:cd03260 89 KPNPFPGSIYDNVAYGLRL---HGIKLKEELDERVEEALRKAAlWDEVKDRlhalgLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 423 DEPTKGVDVKAKTDLFNAIDGLAREgKGVIYASGEFAELVGLCDRICVLWDGRIVAEIP 481
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
272-479 |
1.65e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.11 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGELnsqpwrprdpadsvaRGLALVPEERRKEgifieepV 351
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL--QPTSGEV---------------RVAGLVPWKRRKK-------F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 AMNLAVsadssfsrwsLFGHRQAWRWAEEVI--------------ARVGIRTSGPA----------QTLRRLSGGNQQKV 407
Cdd:cd03267 93 LRRIGV----------VFGQKTQLWWDLPVIdsfyllaaiydlppARFKKRLDELSelldleelldTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 408 AIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-237 |
1.75e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.57 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF---SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQlGI 82
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR-KI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQEVDVALVpGLSIAENIMLDrLAEPGIAfrwgRLRQLAREALAQLDVS-LDVR-RSIDSCTLAEKQQILLARALSH 160
Cdd:PRK13642 84 GMVFQNPDNQFV-GATVEDDVAFG-MENQGIP----REEMIKRVDEALLAVNmLDFKtREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQ-RQGIGIVFISHRIHElKAVCDTLTVLRDGRLIESGPMADL--SGEQIVE 237
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDE-AASSDRILVMKAGEIIKEAAPSELfaTSEDMVE 236
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
275-484 |
2.04e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 275 ISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRltrgelnsqpWR---PRDPADSVARgLALVPEERRK------EGI 345
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN----------WRvtaDRMRFDDIDL-LRLSPRERRKlvghnvSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 FIEEPVAMNLAVSAD----SSFSRWSLFGH-RQAWRW----AEEVIARVGIR------TSGPAQtlrrLSGGNQQKVAIG 410
Cdd:PRK15093 95 FQEPQSCLDPSERVGrqlmQNIPGWTYKGRwWQRFGWrkrrAIELLHRVGIKdhkdamRSFPYE----LTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 411 KWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVI-YASGEFAELVGLCDRICVLWDGRIVAEIPGAE 484
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-202 |
2.26e-09 |
|
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: 56.39 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVInnqsvsirsPRDAKQLgihLVQQEvdvALVPGLSIA 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLL---FLPQR---PYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 101 ENImldrlaepgiAFRWGRLrqlarealaqldVSLDvrrsidsctlaEKQQILLARALSHHCRFLILDEPTAPLDQNESE 180
Cdd:cd03223 82 EQL----------IYPWDDV------------LSGG-----------EQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 503994372 181 RLFAVvrrLQRQGIGIVFISHR 202
Cdd:cd03223 129 RLYQL---LKELGITVISVGHR 147
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-230 |
2.39e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.56 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG----ThahyEGEVVINNQSVSIRSPRDAKQLGihLV----QQevd 90
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilvpT----SGEVRVLGYVPFKRRKEFARRIG--VVfgqrSQ--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 91 vaLVPGLSIAENIMLdrLAE----PGIAFRwGRLRQLArealAQLDVS--LD--VRR-SidsctLAEKQQILLARALSHH 161
Cdd:COG4586 107 --LWWDLPAIDSFRL--LKAiyriPDAEYK-KRLDELV----ELLDLGelLDtpVRQlS-----LGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
268-479 |
2.56e-09 |
|
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: 56.55 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 268 DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPwrprdpadsvargLALVPEERRKEGIFI 347
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-------------VSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 348 EEpvamnlavsadssfsRWSLFghrqawrwAEEVIARVGirtsgpaqtlRRLSGGNQQKVAIGKWLRGNANVLIFDEPTK 427
Cdd:cd03247 81 NQ---------------RPYLF--------DTTLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 428 GVDVKAKTDLFNAIDGLAREgKGVIYASgefAELVGL--CDRICVLWDGRIVAE 479
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKD-KTLIWIT---HHLTGIehMDKILFLENGKIIMQ 177
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
236-485 |
2.76e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 236 VEKMLGHElsdifppkrPPHSDEVllqvEGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGEL 315
Cdd:PLN03211 61 IKRILGHK---------PKISDET----RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 316 NSQPwrpRDPADSVARGLALVPEER-RKEGIFIEEPVAMNLAVSADSSFSRwslfghRQAWRWAEEVIARVGIRTSGPA- 393
Cdd:PLN03211 128 LANN---RKPTKQILKRTGFVTQDDiLYPHLTVRETLVFCSLLRLPKSLTK------QEKILVAESVISELGLTKCENTi 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 394 ---QTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELV-GLCDRIC 469
Cdd:PLN03211 199 ignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyQMFDSVL 278
|
250
....*....|....*.
gi 503994372 470 VLWDGRIVAEIPGAEA 485
Cdd:PLN03211 279 VLSEGRCLFFGKGSDA 294
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
266-477 |
3.26e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 266 LHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRLTrgELNSQPWRPRDPADSVARGLALVP--EERRKE 343
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-----NRLI--EIYDSKIKVDGKVLYFGKDIFQIDaiKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 344 GIFIEEPVAM-NLAVSADSSFSRWS--LFGHRQAWRWAEEVIARVGI------RTSGPAQtlrRLSGGNQQKVAIGKWLR 414
Cdd:PRK14246 93 GMVFQQPNPFpHLSIYDNIAYPLKShgIKEKREIKKIVEECLRKVGLwkevydRLNSPAS---QLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREgKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
261-479 |
3.86e-09 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 56.82 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH----DEGLLQDISLRLRKGeILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPwrPRDPADSVARGLALV 336
Cdd:cd03264 1 LQLENLTkrygKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 337 PEERRkegifieepVAMNLAVSADSSFSRWsLFG--HRQAWRWAEEVIARVGI--RTSGPAQTLrrlSGGNQQKVAIGKW 412
Cdd:cd03264 78 PQEFG---------VYPNFTVREFLDYIAW-LKGipSKEVKARVDEVLELVNLgdRAKKKIGSL---SGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 413 LRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLArEGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
271-478 |
4.00e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFG-----ASKSRLTRGELNSQPWRPRdpadsVARGLALVPEErrkEGI 345
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivprdAGNIIIDDEDISLLPLHAR-----ARRGIGYLPQE---ASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 FIEEPVAMNLAVSADSsfsRWSLFGHRQAWRwAEEVIARVGIrtSGPAQTL-RRLSGGNQQKVAIGKWLRGNANVLIFDE 424
Cdd:PRK10895 90 FRRLSVYDNLMAVLQI---RDDLSAEQREDR-ANELMEEFHI--EHLRDSMgQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 425 PTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-219 |
4.73e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.57 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 16 SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLVQQEVDVALVP 95
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 96 GLSIAENIMLdrlaepGIAFRWGRLRQLAREALAQLDVSL----DV----RRSIDsCTLAEKQQILLARALSHHCRFLIL 167
Cdd:cd03290 92 NATVEENITF------GSPFNKQRYKAVTDACSLQPDIDLlpfgDQteigERGIN-LSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 168 DEPTAPLDQNESERLF--AVVRRLQRQGIGIVFISHRIHELKAVcDTLTVLRDG 219
Cdd:cd03290 165 DDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPHA-DWIIAMKDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-239 |
5.61e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 23 NVAFTLTGGSVHALTGANGAGKSTL-MAVLCGTHAHY-EGEVVINNQSVSIRSPRDA------------KQLGIHLVQqe 88
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEVDVSTVSDAidaglayvtedrKGYGLNLID-- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 89 vdvalvpglSIAENIMLDRLaePGIAfRWGRLRQlAREalaqLDVSLDVRRS--IDSCTLAEK---------QQILLARA 157
Cdd:NF040905 356 ---------DIKRNITLANL--GKVS-RRGVIDE-NEE----IKVAEEYRKKmnIKTPSVFQKvgnlsggnqQKVVLSKW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 158 LSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVE 237
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMR 498
|
..
gi 503994372 238 KM 239
Cdd:NF040905 499 LI 500
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-217 |
5.69e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSnvaFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQsvSIRSPRDAKQ-----LGiHLvqqevdVA 92
Cdd:PRK13538 17 FSGLS---FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE--PIRRQRDEYHqdllyLG-HQ------PG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 93 LVPGLSIAENI-MLDRLAEPGIAFRwgrlrqlAREALAQldVSLDVRRSIDSCTLAEKQQ--ILLARALSHHCRFLILDE 169
Cdd:PRK13538 85 IKTELTALENLrFYQRLHGPGDDEA-------LWEALAQ--VGLAGFEDVPVRQLSAGQQrrVALARLWLTRAPLWILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503994372 170 PTAPLDQN---ESERLFAvvRRLQRQGIgIVFISHriHELKAVCDTLTVLR 217
Cdd:PRK13538 156 PFTAIDKQgvaRLEALLA--QHAEQGGM-VILTTH--QDLPVASDKVRKLR 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-230 |
6.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSprdaKQLGIHLVQQEVDVALvpgl 97
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT----KDKYIRPVRKRIGMVF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 SIAENIMLDRLAEPGIAF-------RWGRLRQLAREALAQLDVSLDV-RRSIDSCTLAEKQQILLARALSHHCRFLILDE 169
Cdd:PRK13646 92 QFPESQLFEDTVEREIIFgpknfkmNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 170 PTAPLDQNESERLFAVVRRLQ-RQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
272-481 |
6.22e-09 |
|
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: 56.33 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGE--LNSQPWRPRDPAdsvargLALVPEErrkEGIF--- 346
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE--RPTSGEvlVDGEPVTGPGPD------RGYVFQQ---DALLpwl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 -IEEPVAMNLavsadsSFSRWSlfgHRQAWRWAEEVIARVGIrtSG-----PAQtlrrLSGGNQQKVAIGKWLRGNANVL 420
Cdd:cd03293 89 tVLDNVALGL------ELQGVP---KAEARERAEELLELVGL--SGfenayPHQ----LSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 421 IFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVL--WDGRIVAEIP 481
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
250-477 |
7.06e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 250 PKRPPHSDEVLlQVEGL---------HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRltRGEL----- 315
Cdd:PRK13631 12 VPNPLSDDIIL-RVKNLycvfdekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK--YGTIqvgdi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 316 --NSQPWRPRDPADSVARGLALVPEERRKEGIFIEEP--VAMNLAVSADSSFSRWSLFGHR-QAWRWAEEVIARVGIRTS 390
Cdd:PRK13631 89 yiGDKKNNHELITNPYSKKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKsEAKKLAKFYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 391 GPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICV 470
Cdd:PRK13631 169 YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIV 248
|
....*..
gi 503994372 471 LWDGRIV 477
Cdd:PRK13631 249 MDKGKIL 255
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
379-472 |
7.68e-09 |
|
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: 56.61 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 379 EEVIARVGIRtsgpaQTLRR----LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYA 454
Cdd:cd03236 121 DELVDQLELR-----HVLDRnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVV 195
|
90
....*....|....*...
gi 503994372 455 SGEFAELVGLCDRICVLW 472
Cdd:cd03236 196 EHDLAVLDYLSDYIHCLY 213
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
270-477 |
8.00e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 270 GLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGE---LNSqpwRPRDpADSVARGLALVpeerRKEGIF 346
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGsvlLNG---MPID-AKEMRAISAYV----QQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 IEepvamNLAVSADSSFS-------RWSLFGHRQAwrwAEEVIARVGIRTS-----GPAQTLRRLSGGNQQKVAIGKWLR 414
Cdd:TIGR00955 111 IP-----TLTVREHLMFQahlrmprRVTKKEKRER---VDEVLQALGLRKCantriGVPGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYA----SgefAELVGLCDRICVLWDGRIV 477
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpS---SELFELFDKIILMAEGRVA 246
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-240 |
8.18e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEgevvinNQSVSIRSprdakqlgihlvqqevDVALVPGLS-- 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE------TSSVVIRG----------------SVAYVPQVSwi 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 ----IAENIMLDRLAEPGiafRWGRlrqlAREALAqLDVSLDVRRSIDSCTLAE---------KQQILLARALSHHCRFL 165
Cdd:PLN03232 691 fnatVRENILFGSDFESE---RYWR----AIDVTA-LQHDLDLLPGRDLTEIGErgvnisggqKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 166 ILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVcDTLTVLRDGRLIESGPMADLSGEQIVEKML 240
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
234-477 |
1.28e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.25 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 234 QIVEKmlghELSDIFPPKRPPHsdevlLQVeglhdeglLQDISLRLRKGEILGIAGLAGAGKT---ELCKALF----GAS 306
Cdd:PRK13651 2 QIKVK----NIVKIFNKKLPTE-----LKA--------LDNVSVEINQGEFIAIIGQTGSGKTtfiEHLNALLlpdtGTI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 307 KSRLTRGELNSQPWRPRDPADSV------ARGLALVPEERRKEGIF------------IEEPV---AMNLAVSADSSFSR 365
Cdd:PRK13651 65 EWIFKDEKNKKKTKEKEKVLEKLviqktrFKKIKKIKEIRRRVGVVfqfaeyqlfeqtIEKDIifgPVSMGVSKEEAKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 366 wslfghrqawrwAEEVIARVGIrtsgPAQTLRR----LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAI 441
Cdd:PRK13651 145 ------------AAKYIELVGL----DESYLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF 208
|
250 260 270
....*....|....*....|....*....|....*.
gi 503994372 442 DGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK13651 209 DNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-242 |
1.29e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.91 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLV 85
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 86 QQEV-----DVALVPGLSIAENIMLDRLAEPGIAfrWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSH 160
Cdd:PRK11264 84 RQHVgfvfqNFNLFPHRTVLENIIEGPVIVKGEP--KEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGE------- 233
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADpqqprtr 241
|
....*....
gi 503994372 234 QIVEKMLGH 242
Cdd:PRK11264 242 QFLEKFLLQ 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-220 |
1.46e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 2 TGNRLEMQNISLAFSGFRAL-SNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVInnqsvsirsPRDAKQL 80
Cdd:COG4178 359 EDGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 gihLVQQEV--------DVALVPGLsiAENIMLDRLAEpgiAFRWGRLRQLArealAQLDVSLDVRRSIdscTLAEKQQI 152
Cdd:COG4178 430 ---FLPQRPylplgtlrEALLYPAT--AEAFSDAELRE---ALEAVGLGHLA----ERLDEEADWDQVL---SLGEQQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 153 LLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRlQRQGIGIVFISHRiHELKAVCD-TLTVLRDGR 220
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDrVLELTGDGS 561
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-225 |
1.65e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVL-----CGTHAHYEGEVVINNQSVSIRsprdakQL 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYER------RV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQEVDVALvPGLSIAENIMLDRLAEPGIAFRWG---RLRQLAREALAQLDVSLDVRRSIDSCTL----AEKQQIL 153
Cdd:PRK14258 82 NLNRLRRQVSMVH-PKPNLFPMSVYDNVAYGVKIVGWRpklEIDDIVESALKDADLWDEIKHKIHKSALdlsgGQQQRLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 154 LARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQ-RQGIGIVFISHRIHELKAVCDTLTVL-----RDGRLIESG 225
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFG 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-225 |
2.11e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.41 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSvsIRSPRDAKQLgiHLVQQEVDVALvpglS 98
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--ITAGKKNKKL--KPLRKKVGIVF----Q 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 IAENIMLDRLAEPGIAF---RWG----RLRQLAREALAQLDVSLDVR-RSIDSCTLAEKQQILLARALSHHCRFLILDEP 170
Cdd:PRK13634 93 FPEHQLFEETVEKDICFgpmNFGvseeDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 171 TAPLD---QNESERLFAVVRRlqRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK13634 173 TAGLDpkgRKEMMEMFYKLHK--EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
261-484 |
2.17e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPW---RPRDPADSVARGL 333
Cdd:PRK10619 6 LNVIDLHkrygEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 334 ALVPEERRKEGIFIEEPVAMNLAVSADSSFSRWSLFG--HRQAWRWAEEVIARVGIRTSGPAQTLRRLSGGNQQKVAIGK 411
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGlsKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 412 WLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAE 484
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-237 |
2.19e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLVQQEV-DVALVPGLS 98
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 IAENIMLDRLAEpgIAFRWGRLRQLAREALAQLDV-SLDV-----RRSIDSCTLAEKQQILLARALSHHCRFLILDEPTA 172
Cdd:PRK10982 343 IGFNSLISNIRN--YKNKVGLLDNSRMKSDTQWVIdSMRVktpghRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 173 PLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADLSGEQIVE 237
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILR 485
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-219 |
2.41e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 3 GNR---LEMQNISLAFSGFR--ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVsIRSPRDA 77
Cdd:TIGR01257 1932 GNKtdiLRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 KQlgihlvqqevDVALVPGLSIAENIMLDRLAepgiAFRWGRLR--------QLAREALAQLDVSLDVRRSIDSCTLAEK 149
Cdd:TIGR01257 2011 HQ----------NMGYCPQFDAIDDLLTGREH----LYLYARLRgvpaeeieKVANWSIQSLGLSLYADRLAGTYSGGNK 2076
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 150 QQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDG 219
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
272-477 |
2.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCK---ALFGASKSRLTRGELNSQPWRPRDPADSVARGLALV---PEERRKEGI 345
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQhfnALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVfqfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 FIEEPV--AMNLAVSADSSfsrwslfgHRQAWRWaeevIARVGIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFD 423
Cdd:PRK13641 103 VLKDVEfgPKNFGFSEDEA--------KEKALKW----LKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503994372 424 EPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
2.93e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVL-----CGTHAHYEGEVVINnqSVSIRSPR-DA 77
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLF--GRNIYSPDvDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 KQlgihlVQQEVDVAL-----VPGLSIAENIMLDrLAEPGIAFRWGRLRQLAREALAQLDVSLDVRRSID----SCTLAE 148
Cdd:PRK14267 81 IE-----VRREVGMVFqypnpFPHLTIYDNVAIG-VKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 149 KQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQgIGIVFISHRIHELKAVCDTLTVLRDGRLIESGP 226
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
272-471 |
2.94e-08 |
|
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: 56.14 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGE--LNSQPWRPRDPaDSVARGLALVPEerrKEGIFiEE 349
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV--DPTEGSiaVNGVPLADADA-DSWRDQIAWVPQ---HPFLF-AG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 350 PVAMNLAvsadssfsrwslFGHRQAWRWA-EEVIARVGIRTSGPA-----QTL-----RRLSGGNQQKVAIGKWLRGNAN 418
Cdd:TIGR02857 411 TIAENIR------------LARPDASDAEiREALERAGLDEFVAAlpqglDTPigeggAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 419 VLIFDEPTKGVDVKAKTDLFNAIDGLAReGKGVIYASGEFAeLVGLCDRICVL 471
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
3.52e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 1 MTGNRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVL-----CGTHAHYEGEVVINNQsvSIRSPR 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGH--NIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 76 -DAKQL--GIHLVQQEvdvalvPG---LSIAENIMLD-RLAepGIAFRwGRLRQLAREALAQLDVSLDVRRSIDSCTLA- 147
Cdd:PRK14239 79 tDTVDLrkEIGMVFQQ------PNpfpMSIYENVVYGlRLK--GIKDK-QVLDEAVEKSLKGASIWDEVKDRLHDSALGl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 148 ---EKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLqRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIES 224
Cdd:PRK14239 150 sggQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
..
gi 503994372 225 GP 226
Cdd:PRK14239 229 ND 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-202 |
3.65e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGthAHYEGEVVINNQSVSIRSPRDAkqlgihlvqqevdvalvpgl 97
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVAGCVDVPDNQFGREA-------------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 SIAENImlDRLAEPGIAfrwgrLRQLAREALAqlDVSLdVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQN 177
Cdd:COG2401 101 SLIDAI--GRKGDFKDA-----VELLNAVGLS--DAVL-WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 503994372 178 ESERLFAVVRRLQRQ-GIGIVFISHR 202
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATHH 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
261-479 |
3.68e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 54.74 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH-----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTR-----GELNSQPWRPR---- 323
Cdd:PRK13647 5 IEVEDLHfrykdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiylPQRGRVKVmgrevNAENEKWVRSKvglv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 324 --DPADSVARGLalvpeerrkegifIEEPVA---MNLAVSADSSFSRwslfghrqawrwAEEVIARVGI---RTSGPAQt 395
Cdd:PRK13647 85 fqDPDDQVFSST-------------VWDDVAfgpVNMGLDKDEVERR------------VEEALKAVRMwdfRDKPPYH- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 396 lrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGR 475
Cdd:PRK13647 139 ---LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
....
gi 503994372 476 IVAE 479
Cdd:PRK13647 216 VLAE 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
272-453 |
4.56e-08 |
|
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: 52.71 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELnsqPWRPRDPAdsvarglalvpeerrkegIFIeepv 351
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFL---PKFSRNKL------------------IFI---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 amnlavsadSSFSRwslfghrqawrwaeevIARVGIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNA--NVLIFDEPTKGV 429
Cdd:cd03238 66 ---------DQLQF----------------LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGL 120
|
170 180
....*....|....*....|....
gi 503994372 430 DVKAKTDLFNAIDGLAREGKGVIY 453
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVIL 144
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
268-479 |
4.60e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 55.56 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 268 DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRL---TRGE--LNSQPwrPRD-PADSVARGLALVPEErr 341
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLL-----LRFydpTSGRilIDGVD--IRDlTLESLRRQIGVVPQD-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 342 kegIFI-EEPVAMNLAvsadssfsrwslFGHRQA-----WRWAE-----EVIAR--------VGIRtsGpaqtlRRLSGG 402
Cdd:COG1132 423 ---TFLfSGTIRENIR------------YGRPDAtdeevEEAAKaaqahEFIEAlpdgydtvVGER--G-----VNLSGG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 403 NQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLaREGKGVIYASGEFAELVGlCDRICVLWDGRIVAE 479
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-206 |
4.99e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 2 TGNRLEMQNISLAFS--GFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGThAHYEGEVVINN---QSVSIRSPRd 76
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGvswNSVTLQTWR- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 aKQLGIhlVQQEVDValvpgLSIAENIMLDRLAEPGIAFRWGRLRQLA-REALAQLDVSLDVRRSIDSCTLA--EKQQIL 153
Cdd:TIGR01271 1292 -KAFGV--IPQKVFI-----FSGTFRKNLDPYEQWSDEEIWKVAEEVGlKSVIEQFPDKLDFVLVDGGYVLSngHKQLMC 1363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 154 LARALSHHCRFLILDEPTAPLDqnesERLFAVVRRLQRQGIG---IVFISHRIHEL 206
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLD----PVTLQIIRKTLKQSFSnctVILSEHRVEAL 1415
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
272-481 |
6.08e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGELN--SQPWRPRDPADSVArglaLVPEERRKEGIF--- 346
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV--RLASGKISilGQPTRQALQKNLVA----YVPQSEEVDWSFpvl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 IEEPVAMnlavsadssfsrwSLFGHRQAWRWA--------EEVIARVGIRTSGPAQtLRRLSGGNQQKVAIGKWLRGNAN 418
Cdd:PRK15056 97 VEDVVMM-------------GRYGHMGWLRRAkkrdrqivTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 419 VLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDrICVLWDGRIVAEIP 481
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGP 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-230 |
6.33e-08 |
|
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: 55.21 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 2 TGNRLEMQNISLAFSGFRA-LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGthaHYE---GEVVINNQ---SVSIRSP 74
Cdd:COG5265 354 GGGEVRFENVSFGYDPERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR---FYDvtsGRILIDGQdirDVTQASL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 75 RDAkqLGIhlVQQEV----DvalvpglSIAENImldrlaepgiafRWGR-------LRQLAReaLAQLDvsldvrRSIDS 143
Cdd:COG5265 431 RAA--IGI--VPQDTvlfnD-------TIAYNI------------AYGRpdaseeeVEAAAR--AAQIH------DFIES 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 144 C-----TL----------AEKQQILLARALSHHCRFLILDEPTAPLDqNESERlfAVVRRLQRQGIG---IVfISHRihe 205
Cdd:COG5265 480 LpdgydTRvgerglklsgGEKQRVAIARTLLKNPPILIFDEATSALD-SRTER--AIQAALREVARGrttLV-IAHR--- 552
|
250 260
....*....|....*....|....*..
gi 503994372 206 LKAV--CDTLTVLRDGRLIESGPMADL 230
Cdd:COG5265 553 LSTIvdADEILVLEAGRIVERGTHAEL 579
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
271-475 |
6.43e-08 |
|
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: 52.86 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGasKSRLTRGELnsqpwrprdpadSVARGLALVPEErrkegifieeP 350
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSV------------SVPGSIAYVSQE----------P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNLAVsadssfsRWS-LFGHRQAWRWAEEVI-----------------ARVGIRTSGpaqtlrrLSGGNQQKVAIGKW 412
Cdd:cd03250 76 WIQNGTI-------RENiLFGKPFDEERYEKVIkacalepdleilpdgdlTEIGEKGIN-------LSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 413 LRGNANVLIFDEPTKGVDVKAKTDLF-NAIDGLAREGKGVIYASGEFaELVGLCDRICVLWDGR 475
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-238 |
6.62e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.98 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAF--SGFrALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQL-- 80
Cdd:PRK10522 322 TLELRNVTFAYqdNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLfs 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 ----GIHLVQQ-------EVDVALVPG-LSIAEniMLDRLAEPGIAFRWGRLRQLAREALAQLdvsldvrrsidsCTLAE 148
Cdd:PRK10522 401 avftDFHLFDQllgpegkPANPALVEKwLERLK--MAHKLELEDGRISNLKLSKGQKKRLALL------------LALAE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 149 KQQILLaralshhcrfliLDEPTAplDQNESERLF---AVVRRLQRQGIGIVFISHRIHELKAVcDTLTVLRDGRLIE-S 224
Cdd:PRK10522 467 ERDILL------------LDEWAA--DQDPHFRREfyqVLLPLLQEMGKTIFAISHDDHYFIHA-DRLLEMRNGQLSElT 531
|
250
....*....|....
gi 503994372 225 GPMADLSGEQIVEK 238
Cdd:PRK10522 532 GEERDAASRDAVAR 545
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
254-485 |
7.19e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.21 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 254 PHSDEVLLQVEGLH-----DEG---LLQDISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGE--LNSQPWRPR 323
Cdd:COG4181 2 SSSSAPIIELRGLTktvgtGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLL--AGLDRPTSGTvrLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 324 DpADSVARGlalvpeerRKEGI-FI------------EEPVAMNLavsadssfsrwSLFGHRQAWRWAEEVIARVGI--R 388
Cdd:COG4181 80 D-EDARARL--------RARHVgFVfqsfqllptltaLENVMLPL-----------ELAGRRDARARARALLERVGLghR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 389 TSG-PAQtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDvkAKT-----DL-FnaidGLARE-GKGVIYASGEfAE 460
Cdd:COG4181 140 LDHyPAQ----LSGGEQQRVALARAFATEPAILFADEPTGNLD--AATgeqiiDLlF----ELNRErGTTLVLVTHD-PA 208
|
250 260
....*....|....*....|....*
gi 503994372 461 LVGLCDRICVLWDGRIVAEIPGAEA 485
Cdd:COG4181 209 LAARCDRVLRLRAGRLVEDTAATAA 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
7.64e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG-----FRALSNVAFTLTGGSVHALTGANGAGKSTLMA-----------------VLCGTHAHYEGEVV 63
Cdd:PRK13631 22 LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiqvgdIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 64 INNQsvsiRSPRDAKQLG--IHLVQQEVDVALVPGlSIAENIMLDRLAepgIAFRWGRLRQLAREALAQLDVSLD-VRRS 140
Cdd:PRK13631 102 NPYS----KKIKNFKELRrrVSMVFQFPEYQLFKD-TIEKDIMFGPVA---LGVKKSEAKKLAKFYLNKMGLDDSyLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 141 IDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGR 220
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
....*
gi 503994372 221 LIESG 225
Cdd:PRK13631 254 ILKTG 258
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
272-479 |
8.22e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.48 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGAsksrltrgelnsqpWRPRDPADSVArGLALVPEE----RRKEGIFI 347
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--------------LLPEAGTITVG-GMVLSEETvwdvRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 348 EEP------------VAM---NLAVSADSSFSRwslfghrqawrwAEEVIARVGIrTSGPAQTLRRLSGGNQQKVAIGKW 412
Cdd:PRK13635 88 QNPdnqfvgatvqddVAFgleNIGVPREEMVER------------VDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 413 LRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGK-GVIYASGEFAElVGLCDRICVLWDGRIVAE 479
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDE-AAQADRVIVMNKGEILEE 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
272-476 |
8.53e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.18 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGE--LNSQ-----PWRPRdPADSVARGLALVPEerrkeg 344
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFET--PDSGRimLDGQdithvPAENR-HVNTVFQSYALFPH------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 345 IFIEEPVAmnlavsadssfsrwslFGHRQAWRWAEEVIARVG-----IRTSGPAQtlRR---LSGGNQQKVAIGKWLRGN 416
Cdd:PRK09452 101 MTVFENVA----------------FGLRMQKTPAAEITPRVMealrmVQLEEFAQ--RKphqLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 417 ANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRI 476
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
272-477 |
9.09e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.92 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGasksrL---TRGEL-------NSQPwrPRDpadsvaRGLALVPEErr 341
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-----LedpTSGEIliggrdvTDLP--PKD------RNIAMVFQS-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 342 kegiFIEEP---VAMNLAvsadssfsrwslFGHRQAwRWAEEVIAR--------VGI-----RTsgPAQtlrrLSGGNQQ 405
Cdd:COG3839 84 ----YALYPhmtVYENIA------------FPLKLR-KVPKAEIDRrvreaaelLGLedlldRK--PKQ----LSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 406 KVAIGkwlRG---NANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:COG3839 141 RVALG---RAlvrEPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
398-494 |
9.13e-08 |
|
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: 53.00 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 398 RLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAReGKGVIYASGEFAELVGlCDRICVLWDGRIV 477
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
90
....*....|....*..
gi 503994372 478 AEIPGAEAREENILYYS 494
Cdd:cd03253 215 ERGTHEELLAKGGLYAE 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
274-479 |
9.86e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 52.50 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 274 DISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADsvaRGLALVPEErrkEGIFIEEPVAM 353
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQE---NNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 354 NLAVSADSSFSRWSLfgHRQAwrwAEEVIARVGIrtsgpAQTLRR----LSGGNQQKVAIGKWLRGNANVLIFDEPTKGV 429
Cdd:cd03298 90 NVGLGLSPGLKLTAE--DRQA---IEVALARVGL-----AGLEKRlpgeLSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503994372 430 DVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03298 160 DPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
257-477 |
1.12e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 53.56 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 257 DEVLLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGE--LNSQPWrprdpadsva 330
Cdd:COG3842 2 AMPALELENVSkrygDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE--TPDSGRilLDGRDV---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 331 rgLALVPEERrkegifieePVAMnlaVsadssFSRWSLFGH------------------RQAWRWAEEVIARVGIRTSG- 391
Cdd:COG3842 70 --TGLPPEKR---------NVGM---V-----FQDYALFPHltvaenvafglrmrgvpkAEIRARVAELLELVGLEGLAd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 392 --PAQtlrrLSGGNQQKVAIGKWLrgnAN---VLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLC 465
Cdd:COG3842 131 ryPHQ----LSGGQQQRVALARAL---APeprVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALA 203
|
250
....*....|..
gi 503994372 466 DRICVLWDGRIV 477
Cdd:COG3842 204 DRIAVMNDGRIE 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
272-479 |
1.15e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.27 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG----ASKSRLTRGELNSQpwrprdpadsvarglALVPEERRKEGIFI 347
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGilkpTSGSVLIRGEPITK---------------ENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 348 EEP--VAMNLAVSADSSFSRWSL------FGHRqawrwAEEVIARVGI---RTSGPaqtlRRLSGGNQQKVAIGKWLRGN 416
Cdd:PRK13652 85 QNPddQIFSPTVEQDIAFGPINLgldeetVAHR-----VSSALHMLGLeelRDRVP----HHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 417 ANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
265-481 |
1.22e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 265 GLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgasksrltrGELNSQPWRPRDPADSVARGLAL-----VPEE 339
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL----------NRMNDKVSGYRYSGDVLLGGRSIfnyrdVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 340 RRKEGIFIEEP--VAMNLAVSADSSFSRWSLFGHRQAWRWAEEVIARVGIRTSGP---AQTLRRLSGGNQQKVAIGKWLR 414
Cdd:PRK14271 100 RRRVGMLFQRPnpFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdrlSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLArEGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIP 481
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
256-480 |
1.24e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.51 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 256 SDEVLLQVEGL---HDEG-----LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSQPwRPRDPAD 327
Cdd:PRK11629 1 MNKILLQCDNLckrYQEGsvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNG-QPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 328 SVARGlalvpEERRKEGIFIE------------EPVAMNLavsadssfsrwsLFGHR---QAWRWAEEVIARVGIRTSGP 392
Cdd:PRK11629 78 SAAKA-----ELRNQKLGFIYqfhhllpdftalENVAMPL------------LIGKKkpaEINSRALEMLAAVGLEHRAN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 393 AQTlRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGL-AREGKGVIYASGEFaELVGLCDRICVL 471
Cdd:PRK11629 141 HRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEM 218
|
....*....
gi 503994372 472 WDGRIVAEI 480
Cdd:PRK11629 219 RDGRLTAEL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-225 |
1.40e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.17 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD--AKQLGIHLVQQEVDVALVPG 96
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDPLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 97 LSIAENImldrlAEPGIAFRWGRLRQLAREALAQ--LDVSL---DVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPT 171
Cdd:PRK15079 115 MTIGEII-----AEPLRTYHPKLSRQEVKDRVKAmmLKVGLlpnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 172 APLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
275-479 |
1.47e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 275 ISLRLRKGEILGIAGLAGAGKTElckalfGASKSRLTRGELNSQPWR-----PRDPADSVARGLALVPEERRKEGIFIEE 349
Cdd:NF000106 32 VDLDVREGTVLGVLGP*GAA**R------GALPAHV*GPDAGRRPWRf*twcANRRALRRTIG*HRPVR*GRRESFSGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 350 PVAMnlavsadssFSRWSLFGHRQAWRWAEEVIARVGIrTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGV 429
Cdd:NF000106 106 NLYM---------IGR*LDLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503994372 430 DVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-225 |
1.68e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 16 SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQsvSIRSPRDAKQLGIHLVQQEvdVALVP 95
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVRQSLGMCPQH--NILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 96 GLSIAENIMLdrlaEPGIAFRWGRLRQLAREALAQlDVSLDVRRSIDSCTLAEKQQILLARALSH--HCRFLILDEPTAP 173
Cdd:TIGR01257 1017 HLTVAEHILF----YAQLKGRSWEEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFvgDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503994372 174 LDQNESERLFAVVRRLqRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
258-475 |
1.68e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 258 EVLLQVEGLH--------DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG--ASKSR--------------LTRG 313
Cdd:PRK09473 10 DALLDVKDLRvtfstpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGRiggsatfngreilnLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 314 ELNsqpwRPR---------DPADSvarglaLVPEERRKEGIF--------------IEEPVAMNLAVSADSSFSRWSLFG 370
Cdd:PRK09473 90 ELN----KLRaeqismifqDPMTS------LNPYMRVGEQLMevlmlhkgmskaeaFEESVRMLDAVKMPEARKRMKMYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 371 HRqawrwaeeviarvgirtsgpaqtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GK 449
Cdd:PRK09473 160 HE--------------------------FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNT 213
|
250 260
....*....|....*....|....*.
gi 503994372 450 GVIYASGEFAELVGLCDRICVLWDGR 475
Cdd:PRK09473 214 AIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
261-475 |
1.97e-07 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 50.14 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGL----HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGAsksrltrgelnsqpwrprdpadsvarglaLV 336
Cdd:cd03221 1 IELENLsktyGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE-----------------------------LE 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 337 PEErrkegifieepvamnlavsadssfsrwslfghrqawrwaeeviarvGIRTSGPAQT---LRRLSGGNQQKVAIGKWL 413
Cdd:cd03221 52 PDE----------------------------------------------GIVTWGSTVKigyFEQLSGGEKMRLALAKLL 85
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 414 RGNANVLIFDEPTKGVDVKAKTDLfnaIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGR 475
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
256-477 |
1.99e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 256 SDEVLLQVEGLHDEglLQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRL---TRGELNSqpwrprDPADSVARG 332
Cdd:PRK10070 30 SKEQILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-----NRLiepTRGQVLI------DGVDIAKIS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 333 LALVPEERRKEGIFIEEPVAM--NLAVSADSSFSRwSLFGHRQAWRW--AEEVIARVGIRTSGPAQTlRRLSGGNQQKVA 408
Cdd:PRK10070 97 DAELREVRRKKIAMVFQSFALmpHMTVLDNTAFGM-ELAGINAEERRekALDALRQVGLENYAHSYP-DELSGGMRQRVG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 409 IGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGL-AREGKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-201 |
2.08e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIR----SPRDA---- 77
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdPPRNVegtv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 78 --------KQLGIHLV---QQEVDVALVPGLSiaeniMLDRLAEPGIAFRWGRLRQL---AREALAQLDVSLDVRRSIDS 143
Cdd:PRK11147 84 ydfvaegiEEQAEYLKryhDISHLVETDPSEK-----NLNELAKLQEQLDHHNLWQLenrINEVLAQLGLDPDAALSSLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 144 CTLAEKqqILLARALSHHCRFLILDEPTAPLDQNESERLFAVVrrLQRQGiGIVFISH 201
Cdd:PRK11147 159 GGWLRK--AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISH 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
118-321 |
2.15e-07 |
|
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: 53.86 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 118 GRLRQLAREALAQ--------LDVSLD---VRRSIDSCTLAEKQQILLARAL-SHHCRFL-ILDEPTAPLDQNESERLFA 184
Cdd:TIGR00630 452 PEEKKIAEEVLKEirerlgflIDVGLDylsLSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLIN 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 185 VVRRLQRQGIGIVFISHrihelkavcDTLTVLRDGRLIESGPMADLSGEQIV-----EKMLGHELS----------DIFP 249
Cdd:TIGR00630 532 TLKRLRDLGNTLIVVEH---------DEDTIRAADYVIDIGPGAGEHGGEVVasgtpEEILANPDSltgqylsgrkKIEV 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 250 PKRPPHSDEVLLQVEGLHdEGLLQDISLRLRKGEILGIAGLAGAGKTELC-KALFGASKSRLTRGELNSQPWR 321
Cdd:TIGR00630 603 PAERRPGNGKFLTLKGAR-ENNLKNITVSIPLGLFTCITGVSGSGKSTLInDTLYPALANRLNGAKTVPGRYT 674
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
272-479 |
2.29e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.47 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCK---ALFGASKSRLTRGELNSQpwrpRDPADSVARGLalvpeeRRKEGIFIE 348
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQninALLKPTTGTVTVDDITIT----HKTKDKYIRPV------RKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 EPVAMNLavsaDSSFSRWSLFGHRQAWRWAEEVIARV-----------GIRTSGPAQtlrrLSGGNQQKVAIGKWLRGNA 417
Cdd:PRK13646 93 FPESQLF----EDTVEREIIFGPKNFKMNLDEVKNYAhrllmdlgfsrDVMSQSPFQ----MSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 418 NVLIFDEPTKGVDVKAKTDLFNAIDGLA-REGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-230 |
3.08e-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: 53.41 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAF-SGFR-ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirsprdakQLGI 82
Cdd:TIGR00957 1284 RVEFRNYCLRYrEDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--------KIGL 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLVQQEV-----DVALVPGlSIAENimLDRLA-----EPGIAFRWGRLRQLAREALAQLDvsLDVRRSIDSCTLAEKQQI 152
Cdd:TIGR00957 1356 HDLRFKItiipqDPVLFSG-SLRMN--LDPFSqysdeEVWWALELAHLKTFVSALPDKLD--HECAEGGENLSVGQRQLV 1430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 153 LLARALSHHCRFLILDEPTAPLDQnESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLtVLRDGRLIESGPMADL 230
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI-VLDKGEVAEFGAPSNL 1506
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-224 |
3.34e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLgIHLVQQEVDVALVpGLSIA 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNPDNQFV-GATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 101 ENIMLDrLAEPGIAFRwgRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESE 180
Cdd:PRK13650 101 DDVAFG-LENKGIPHE--EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503994372 181 RLFAVVRRL-QRQGIGIVFISHRIHELkAVCDTLTVLRDGRlIES 224
Cdd:PRK13650 178 ELIKTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ-VES 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-225 |
3.35e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.34 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSP---RDAKQLGIHLVQQEVdvALVPG 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSF--ALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 97 LSIAENIMLD-RLAEPGIAFRwgrlRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLD 175
Cdd:PRK10070 121 MTVLDNTAFGmELAGINAEER----REKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503994372 176 Q-NESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK10070 197 PlIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
272-476 |
3.49e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTelckalfgaSKSRLTRGELNSqpwrprDPADSVARGLALVPEE----RRKEGIFI 347
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKS---------TTVRLIDGLLEA------ESGQIIIDGDLLTEENvwdiRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 348 EEPvamnlavsaDSSFSRWSL-----FG-------HRQAWRWAEEVIARVGI---RTSGPAqtlrRLSGGNQQKVAIGKW 412
Cdd:PRK13650 88 QNP---------DNQFVGATVeddvaFGlenkgipHEEMKERVNEALELVGMqdfKEREPA----RLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 413 LRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAElVGLCDRICVLWDGRI 476
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
257-447 |
3.61e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 257 DEVLLQVEGlhDEGL-LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADsVARGLAL 335
Cdd:PRK13648 11 KNVSFQYQS--DASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK-LRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 336 V---PEERrkegiFIEEPVAMNLAVSADSsfsrwSLFGHRQAWRWAEEVIARVGI---RTSGPaqtlRRLSGGNQQKVAI 409
Cdd:PRK13648 88 VfqnPDNQ-----FVGSIVKYDVAFGLEN-----HAVPYDEMHRRVSEALKQVDMlerADYEP----NALSGGQKQRVAI 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 503994372 410 GKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE 447
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSE 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-241 |
3.70e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.12 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 35 ALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPrdaKQLGIHLVQQEVDvaLVPGLSIAENIMLDrlAEPGIa 114
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRPVSMLFQENN--LFSHLTVAQNIGLG--LNPGL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 115 frwgRLRQLAREALAQL--DVSLD--VRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLD---QNESERLFAVVR 187
Cdd:PRK10771 101 ----KLNAAQREKLHAIarQMGIEdlLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQEMLTLVSQVC 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 188 RlQRQgIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL-SGEQIVEKMLG 241
Cdd:PRK10771 177 Q-ERQ-LTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELlSGKASASALLG 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-220 |
4.08e-07 |
|
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: 50.55 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF-----SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINN-----------QSV 69
Cdd:cd03250 1 ISVEDASFTWdsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayvsqepwiQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 70 SIR------SPRDAKQLgihlvQQEVDV-ALVPGLSIAENIMLDRLAEPGIafrwgrlrqlarealaqldvsldvrrsid 142
Cdd:cd03250 81 TIRenilfgKPFDEERY-----EKVIKAcALEPDLEILPDGDLTEIGEKGI----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 143 scTLA--EKQQILLARALSHHCRFLILDEPTAPLDQNESERLFA-VVRRLQRQGIGIVFISHRIHELKAvCDTLTVLRDG 219
Cdd:cd03250 127 --NLSggQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
.
gi 503994372 220 R 220
Cdd:cd03250 204 R 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-191 |
4.24e-07 |
|
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: 50.32 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 19 RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG--THAHYEGEVVINNQSVSIRSPRD---AKQLGIHLVQQEVDVAL 93
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRStgyVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 94 -----VPGLSIAEnimldrlaepgiafrwgRLRqlarealaqldVSLDVRrsidsctLAEKQQILLaralshhcrfliLD 168
Cdd:cd03232 101 rfsalLRGLSVEQ-----------------RKR-----------LTIGVE-------LAAKPSILF------------LD 133
|
170 180
....*....|....*....|...
gi 503994372 169 EPTAPLDqneSERLFAVVRRLQR 191
Cdd:cd03232 134 EPTSGLD---SQAAYNIVRFLKK 153
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
272-474 |
4.26e-07 |
|
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: 50.93 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQPWRPRDPADSVA-RGLALVPEERRKEgifieep 350
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVfQNYSLLPWLTVRE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 vamNLAVSADSSFSRWSLFGHRQAwrwAEEVIARVGIRTSG---PAQtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTK 427
Cdd:TIGR01184 74 ---NIALAVDRVLPDLSKSERRAI---VEEHIALVGLTEAAdkrPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503994372 428 GVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDG 474
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
272-448 |
5.11e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.78 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKA--LFGASKSrltrGELN--------SQPwrprdPADSVARGLalvpeeRR 341
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVlnLLEMPRS----GTLNiagnhfdfSKT-----PSDKAIREL------RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 342 KEGI----------------FIEEPVAMnLAVSADSSFSRwslfghrqawrwAEEVIARvgIRTSGPAQTL-RRLSGGNQ 404
Cdd:PRK11124 83 NVGMvfqqynlwphltvqqnLIEAPCRV-LGLSKDQALAR------------AEKLLER--LRLKPYADRFpLHLSGGQQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503994372 405 QKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREG 448
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
272-489 |
5.15e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSQPwrpRDPADSVARGLALVpeeRRKEGIFIeepv 351
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKP--TSGTYRVAG---QDVATLDADALAQL---RREHFGFI---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 amnlavsadssFSRWSLFGH------------------RQAWRWAEEVIARVGI--RTS-GPAQtlrrLSGGNQQKVAIG 410
Cdd:PRK10535 92 -----------FQRYHLLSHltaaqnvevpavyaglerKQRLLRAQELLQRLGLedRVEyQPSQ----LSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 411 KWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEfAELVGLCDRICVLWDGRIVAEIPGAEAREEN 489
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQEKVNVA 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
267-479 |
5.42e-07 |
|
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: 50.69 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 267 HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgasksrltrgelnsqpwrPR--DPA------DSVA-RGLALvP 337
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI-------------------PRfyDVDsgriliDGHDvRDYTL-A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 338 EERRKEGIFIEEP------VAMNLAVSADSSFSRWSLFGHRQAWrwAEEVIAR--------VGIRTSgpaqtlrRLSGGN 403
Cdd:cd03251 73 SLRRQIGLVSQDVflfndtVAENIAYGRPGATREEVEEAARAAN--AHEFIMElpegydtvIGERGV-------KLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 404 QQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYA----SGEFAelvglcDRICVLWDGRIVAE 479
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAhrlsTIENA------DRIVVLEDGKIVER 217
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-230 |
6.09e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQS--VSIRSPRDAKQLGIhlvqqevdvalvpgl 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQLTGI--------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 siaENIMLDRLAepgIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQN 177
Cdd:PRK13545 104 ---ENIELKGLM---MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 178 ESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK13545 178 FTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
258-476 |
7.04e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.78 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 258 EVLLQVEGL----HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTRGELNSqpwRPRDPADSVA 330
Cdd:PRK09984 2 QTIIRVEKLaktfNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLG---RTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 331 RGlalVPEERRKEGIFIEE-------PVAMNLAVSADSSFSRW----SLFGHRQAWRwAEEVIARVGIrTSGPAQTLRRL 399
Cdd:PRK09984 79 RD---IRKSRANTGYIFQQfnlvnrlSVLENVLIGALGSTPFWrtcfSWFTREQKQR-ALQALTRVGM-VHFAHQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 400 SGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAR-EGKGVIYASGEFAELVGLCDRICVLWDGRI 476
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
261-476 |
7.99e-07 |
|
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: 49.14 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGL------HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGA---SKSRLTRGELNSQPWRPRDPADSVAr 331
Cdd:cd03246 1 LEVENVsfrypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlrpTSGRVRLDGADISQWDPNELGDHVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 332 glaLVPEErrkegifieepvamnlavsaDSSFSRwSLfghrqawrwAEEViarvgirtsgpaqtlrrLSGGNQQKVAIGK 411
Cdd:cd03246 80 ---YLPQD--------------------DELFSG-SI---------AENI-----------------LSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 412 WLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEfAELVGLCDRICVLWDGRI 476
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
260-447 |
8.14e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLT------------RGELNSQ-- 318
Cdd:PRK11248 1 MLQISHLYadygGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfvpYQHGSITldgkpvegpgaeRGVVFQNeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 319 --PWrpRDPADSVARGLAL--VPEERRKEGifieepvamnlavsadssfsrwslfghrqawrwAEEVIARVGIRTSGpAQ 394
Cdd:PRK11248 81 llPW--RNVQDNVAFGLQLagVEKMQRLEI---------------------------------AHQMLKKVGLEGAE-KR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 395 TLRRLSGGNQQKVAIGKWLRGNANVLIFDEPtkgvdvkaktdlFNAIDGLARE 447
Cdd:PRK11248 125 YIWQLSGGQRQRVGIARALAANPQLLLLDEP------------FGALDAFTRE 165
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-230 |
8.97e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 18 FRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQsVSIRSprdakqlgihlvqqeVDVALVPGL 97
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIA---------------ISAGLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 98 SIAENIMLDRLAepgIAFRWGRLRQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQN 177
Cdd:PRK13546 101 TGIENIEFKMLC---MGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 178 ESERLFAVVRRLQRQGIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPMADL 230
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
261-477 |
9.60e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 261 LQVEGLH---DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKS--RLTRGELNSQPwRPRDPADSVARGLAL 335
Cdd:PRK10418 5 IELRNIAlqaAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvRQTAGRVLLDG-KPVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 336 VPEERRKegifieepvAMNlAVSADSSFSRWSLfghRQAWRWAEEVIARVGIRTSG---PAQTLRR----LSGGNQQKVA 408
Cdd:PRK10418 84 IMQNPRS---------AFN-PLHTMHTHARETC---LALGKPADDATLTAALEAVGlenAARVLKLypfeMSGGMLQRMM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 409 IGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
273-479 |
9.63e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 273 QDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRLTRgELNSQPWR-----PRDPADSVARGLALVPEERRKEG-IF 346
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTL-----SRLMT-PAHGHVWLdgehiQHYASKEVARRIGLLAQNATTPGdIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 347 IEEPVAMnlavsadSSFSRWSLFGHrqaWRWAEEVIARVGIRTSG----PAQTLRRLSGGNQQKVAIGKWLRGNANVLIF 422
Cdd:PRK10253 98 VQELVAR-------GRYPHQPLFTR---WRKEDEEAVTKAMQATGithlADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 423 DEPTKGVDVKAKTDLFNAIDGLAREgKGVIYAS--GEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNRE-KGYTLAAvlHDLNQACRYASHLIALREGKIVAQ 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
274-478 |
9.77e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.64 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 274 DISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSqpwrpRDPADSvARGLALVPEERRKEGIFIEE---P 350
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-----RVLFDA-EKGICLPPEKRRIGYVFQDArlfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 ---VAMNL----AVSADSSFSRwslfghrqawrwaeeVIARVGIRTsgpaqTLRR----LSGGNQQKVAIGKWLRGNANV 419
Cdd:PRK11144 90 hykVRGNLrygmAKSMVAQFDK---------------IVALLGIEP-----LLDRypgsLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 420 LIFDEPTKGVDVKAKTDLFNAIDGLAREGK-GVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
272-479 |
1.05e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.18 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELckalfgaskSRLTRGELnsqpwRPRDPADSV--ARGLAL----VPEERRKEGI 345
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTI---------SKLINGLL-----LPDDNPNSKitVDGITLtaktVWDIREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 FIEEP--VAMNLAVSADSSFSrwslFGHRQAWR-----WAEEVIARVGI---RTSGPAQtlrrLSGGNQQKVAIGKWLRG 415
Cdd:PRK13640 89 VFQNPdnQFVGATVGDDVAFG----LENRAVPRpemikIVRDVLADVGMldyIDSEPAN----LSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 416 NANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-225 |
1.06e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLM----AVLCGThahyEGEVVINNQSVS-------IRS--------PRDakQL 80
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmnALLIPS----EGKVYVDGLDTSdeenlwdIRNkagmvfqnPDN--QI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVqqEVDVALVPglsiaENImldrlaepGIAFRWGRLRqlAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSH 160
Cdd:PRK13633 99 VATIV--EEDVAFGP-----ENL--------GIPPEEIRER--VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 161 HCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELkAVCDTLTVLRDGRLIESG 225
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEG 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-236 |
1.08e-06 |
|
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: 49.92 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLM---------------AVLCGTHAHYEG-----EVVINNQSVSIRSPR----- 75
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkKEQPGNHDRIEGlehidKVIVIDQSPIGRTPRsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 76 ------DAKQL------GIHLVQQEVDVaLVPGLSIAEniMLDRLAEPGIAFrWGRLRQLAREALAQLDVSLD-VRRSID 142
Cdd:cd03271 91 ytgvfdEIRELfcevckGKRYNRETLEV-RYKGKSIAD--VLDMTVEEALEF-FENIPKIARKLQTLCDVGLGyIKLGQP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 143 SCTLA--EKQQILLARALSHHCR---FLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKaVCDtltvlr 217
Cdd:cd03271 167 ATTLSggEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CAD------ 239
|
250
....*....|....*....
gi 503994372 218 dgRLIESGPMADLSGEQIV 236
Cdd:cd03271 240 --WIIDLGPEGGDGGGQVV 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-230 |
1.19e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAF----SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGThAHYEGEVV-----INNQSVSIRSPRD 76
Cdd:PRK11022 4 LNVDKLSVHFgdesAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMaekleFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 AKQL---GIHLVQQEVDVALVPGLSIAENIMLDRLAEPGIAFRWgrLRQLAREALAQLDV-----SLDVRRSIDSCTLAe 148
Cdd:PRK11022 83 RRNLvgaEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKT--RRQRAIDLLNQVGIpdpasRLDVYPHQLSGGMS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 149 kQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRLIESGPM 227
Cdd:PRK11022 160 -QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
...
gi 503994372 228 ADL 230
Cdd:PRK11022 239 HDI 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
272-492 |
1.39e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGasksrltrgELNsqpwrPRDPADSVARG-LALVPEerrKEGIFiEEP 350
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELS-----HAETSSVVIRGsVAYVPQ---VSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNLAVSADSSFSRWslfghrqaWRwAEEVIARVGIRTSGPAQTLRRL-------SGGNQQKVAIGKWLRGNANVLIFD 423
Cdd:PLN03232 695 VRENILFGSDFESERY--------WR-AIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 424 EPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFaELVGLCDRICVLWDGRIVAEIPGAEAREENILY 492
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSGSLF 833
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
271-484 |
1.76e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFG------ASKSRLTRGE--LNSQPWRpRDPADSVARGLALVPEERRK 342
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggAPRGARVTGDvtLNGEPLA-AIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 343 EgifieepvamnLAVSADS--SFSRWSLFGHRQAWRWAEEVIARVGIRTSGPAQTLRR----LSGGNQQKVAIGKWL--- 413
Cdd:PRK13547 95 A-----------FAFSAREivLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRdvttLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 414 ------RGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGK-GVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAE 484
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
378-452 |
2.00e-06 |
|
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: 50.17 E-value: 2.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 378 AEEVIARVGIRTSgPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVI 452
Cdd:COG1245 193 LDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
397-476 |
2.27e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 397 RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLaREGKGVIYASGEFAELVGLCDRICVLWDGRI 476
Cdd:TIGR01257 1060 QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
256-445 |
2.44e-06 |
|
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: 50.05 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 256 SDEVLLQVEGLH-----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGAsksrltrgelnsqpWRPRDPA---D 327
Cdd:TIGR02868 330 LGKPTLELRDLSagypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL--------------LDPLQGEvtlD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 328 SVARGLALVPEERRKEGIFIEEP------VAMNLAVSA-DSSFSRwslfghrqawrwAEEVIARVGI-----RTSGPAQT 395
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAhlfdttVRENLRLARpDATDEE------------LWAALERVGLadwlrALPDGLDT 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 396 L-----RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAK----TDLFNAIDGLA 445
Cdd:TIGR02868 464 VlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAdellEDLLAALSGRT 522
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
2.62e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.31 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 5 RLEMQNISLAF-----SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEV--VINNQ---------- 67
Cdd:PRK13651 2 QIKVKNIVKIFnkklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEknkkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 68 ----SVSIRSPRDAKQLGIHLVQQEVDVALvpglSIAENIMLDRLAEPGIAF---RWGRLRQLARE------ALAQLDVS 134
Cdd:PRK13651 82 kvleKLVIQKTRFKKIKKIKEIRRRVGVVF----QFAEYQLFEQTIEKDIIFgpvSMGVSKEEAKKraakyiELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 135 LdVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRI-HELKAVCDTL 213
Cdd:PRK13651 158 Y-LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTI 236
|
250
....*....|..
gi 503994372 214 tVLRDGRLIESG 225
Cdd:PRK13651 237 -FFKDGKIIKDG 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
271-447 |
3.18e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.57 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSQPwrprdpadsvARGLALVPEErrkegifieep 350
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAP--DEGVIKRNG----------KLRIGYVPQK----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 vaMNLAVSADSSFSRWSLFghrqawrwaeeviaRVGIRTS--GPA-----------QTLRRLSGGNQQKVAIGKWLRGNA 417
Cdd:PRK09544 76 --LYLDTTLPLTVNRFLRL--------------RPGTKKEdiLPAlkrvqaghlidAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190
....*....|....*....|....*....|
gi 503994372 418 NVLIFDEPTKGVDVKAKTDLFNAIDGLARE 447
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
373-477 |
3.46e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 373 QAWRWAEEVIARVGIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVI 452
Cdd:PRK13649 120 EAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIV 199
|
90 100
....*....|....*....|....*
gi 503994372 453 YASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK13649 200 LVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
272-430 |
3.48e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.92 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTEL--CKAL-----------FGASKSRLTRGELNsqpwrprdpadsvarglalvpE 338
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLirCINLlerptsgsvlvDGVDLTALSERELR---------------------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 339 ERRKEG-IF----------IEEPVAMNLAVsadssfSRWSlfgHRQAWRWAEEVIARVGI---RTSGPAQtlrrLSGGNQ 404
Cdd:COG1135 80 ARRKIGmIFqhfnllssrtVAENVALPLEI------AGVP---KAEIRKRVAELLELVGLsdkADAYPSQ----LSGGQK 146
|
170 180
....*....|....*....|....*.
gi 503994372 405 QKVAIGKWLRGNANVLIFDEPTKGVD 430
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALD 172
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-230 |
4.15e-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: 49.56 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNqSVSirsprdakqlgiHLVQQevdvALVPGLSIA 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVA------------YVPQQ----AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 101 ENIMLDRLAEPgiafrwGRLRQLArEALAQLdVSLDVRRSIDSCTLAEK---------QQILLARALSHHCRFLILDEPT 171
Cdd:TIGR00957 717 ENILFGKALNE------KYYQQVL-EACALL-PDLEILPSGDRTEIGEKgvnlsggqkQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 172 APLDQNESERLFAVVrrLQRQGI----GIVFISHRIHELKAVcDTLTVLRDGRLIESGPMADL 230
Cdd:TIGR00957 789 SAVDAHVGKHIFEHV--IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
272-431 |
4.23e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.81 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSQPWRPRDPADSVARGL-------------ALVPe 338
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETP--TGGELYYQGQDLLKADPEAQKLLrqkiqivfqnpygSLNP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 339 eRRKEGIFIEEPVAMNLAVSADSSFSRwslfghrqawrwAEEVIARVGIRTSGPAQTLRRLSGGNQQKVAIGKWLRGNAN 418
Cdd:PRK11308 108 -RKKVGQILEEPLLINTSLSAAERREK------------ALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170
....*....|...
gi 503994372 419 VLIFDEPTKGVDV 431
Cdd:PRK11308 175 VVVADEPVSALDV 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
260-486 |
4.33e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLHDE--GLL--QDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGE--LNSQPWRPRdPADSVAR-G 332
Cdd:PRK11300 5 LLSVSGLMMRfgGLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKP--TGGTilLRGQHIEGL-PGHQIARmG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 333 LALVPEERRkegIFIEEPVAMNLAVsADSSFSRWSLF-------GHRQAWRWAEEVIA----RVGIR--TSGPAQTLrrl 399
Cdd:PRK11300 82 VVRTFQHVR---LFREMTVIENLLV-AQHQQLKTGLFsgllktpAFRRAESEALDRAAtwleRVGLLehANRQAGNL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 400 SGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIVA 478
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
....*...
gi 503994372 479 EIPGAEAR 486
Cdd:PRK11300 235 NGTPEEIR 242
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-226 |
5.05e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.28 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG---THAHYEGEVVINNQsvsirsPRDAKQlgIHL----VQQevDVAL 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrspKGVKGSGSVLLNGM------PIDAKE--MRAisayVQQ--DDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 94 VPGLSIAENIMLdrLAEpgiaFRWGRL------RQLAREALAQL------DVSLDVRRSIDSCTLAEKQQILLARALSHH 161
Cdd:TIGR00955 111 IPTLTVREHLMF--QAH----LRMPRRvtkkekRERVDEVLQALglrkcaNTRIGVPGRVKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 162 CRFLILDEPTAPLDQNESERLFAVVRRL-QRQGIGIVFI---SHRIHELkavCDTLTVLRDGRLIESGP 226
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIhqpSSELFEL---FDKIILMAEGRVAYLGS 250
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-233 |
5.15e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRDAKQLGIHLVQQEVdvaLVPGlSIA 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPV---LFSG-TVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 101 ENImlDRLAEPGIAFRWGRL-RQLAREALAQLDVSLD--VRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQn 177
Cdd:PLN03232 1328 FNI--DPFSEHNDADLWEALeRAHIKDVIDRNPFGLDaeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV- 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 178 eseRLFAVVRRLQRQ---GIGIVFISHRIHELKAvCDTLTVLRDGRLIE-SGPMADLSGE 233
Cdd:PLN03232 1405 ---RTDSLIQRTIREefkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEyDSPQELLSRD 1460
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
272-479 |
5.48e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 49.03 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGEL------------------NSQP-------------- 319
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyhvalcekcgyverpskVGEPcpvcggtlepeevd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 320 -WRPRDP---------ADSVARGLALVPEERRKEGIfIEepvAMN-LAVSADSSFSRwslfghrqawrwAEEVIARVGI- 387
Cdd:TIGR03269 96 fWNLSDKlrrrirkriAIMLQRTFALYGDDTVLDNV-LE---ALEeIGYEGKEAVGR------------AVDLIEMVQLs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 388 -RTSGPAqtlRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVG-LC 465
Cdd:TIGR03269 160 hRITHIA---RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLS 236
|
250
....*....|....
gi 503994372 466 DRICVLWDGRIVAE 479
Cdd:TIGR03269 237 DKAIWLENGEIKEE 250
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
272-447 |
7.75e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 47.55 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGE--LNSQ-------------------PWRprDPADSVA 330
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLI--AGFLAPSSGEitLDGVpvtgpgadrgvvfqkdallPWL--NVLDNVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 331 RGLAL--VPEERRKEGifieepvamnlavsadssfsrwslfghrqawrwAEEVIARVGIRTSGPAQtLRRLSGGNQQKVA 408
Cdd:COG4525 99 FGLRLrgVPKAERRAR---------------------------------AEELLALVGLADFARRR-IWQLSGGMRQRVG 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 503994372 409 IGKWLRGNANVLIFDEPtkgvdvkaktdlFNAIDGLARE 447
Cdd:COG4525 145 IARALAADPRFLLMDEP------------FGALDALTRE 171
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-229 |
8.10e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG-THAH-YEGEVVINNqsvsiRSPRDAKQLGIHLVQQevDVALVPGLS 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNnFTGTILANN-----RKPTKQILKRTGFVTQ--DDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 99 IAENIMLDRLAE-PGIAFRWGRLRqLAREALAQLDV-----SLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTA 172
Cdd:PLN03211 157 VRETLVFCSLLRlPKSLTKQEKIL-VAESVISELGLtkcenTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 173 PLDQNESERLFAVVRRLQRQGIGIVFISH----RIHELkavCDTLTVLRDGRLIESGPMAD 229
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQM---FDSVLVLSEGRCLFFGKGSD 293
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
249-432 |
8.90e-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: 48.79 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 249 PPKRPPHSDEVLLQVEGL-HDEGL---LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELnsqpwrpRD 324
Cdd:TIGR00957 1275 PPSGWPPRGRVEFRNYCLrYREDLdlvLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES--AEGEI-------II 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 325 PADSVAR-GLAlvpEERRKEGIFIEEPV------AMNLavsadSSFSRWSlfgHRQAWrWAEEVIARVGIRTSGP----- 392
Cdd:TIGR00957 1346 DGLNIAKiGLH---DLRFKITIIPQDPVlfsgslRMNL-----DPFSQYS---DEEVW-WALELAHLKTFVSALPdkldh 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503994372 393 --AQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVK 432
Cdd:TIGR00957 1414 ecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
139-237 |
9.00e-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: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 139 RSIDSCTLAEKQQILLARAL---SHHCRFlILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHrihelkavcdTLTV 215
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELfsePPGTLF-ILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH----------NLDV 151
|
90 100
....*....|....*....|...
gi 503994372 216 LRDG-RLIESGPMADLSGEQIVE 237
Cdd:cd03238 152 LSSAdWIIDFGPGSGKSGGKVVF 174
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
272-482 |
9.22e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTRGELNSQPWRPRDpadsvarglalVPEERRKEGIFIE 348
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGierPSAGKIWFSGHDITRLKNRE-----------VPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 E-----------PVAMNLAVSADSSfsrwslfghRQAWRWAEEVIARVGI---RTSGPAQtlrrLSGGNQQKVAIGKWLR 414
Cdd:PRK10908 87 DhhllmdrtvydNVAIPLIIAGASG---------DDIRRRVSAALDKVGLldkAKNFPIQ----LSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 415 GNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPG 482
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGG 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-442 |
1.03e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 10 NISLAFsGFRAL-SNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVIN----------------NQSV--- 69
Cdd:PRK15064 6 NITMQF-GAKPLfENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlgklrqdqfafeEFTVldt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 70 ---------SIRSPRDA--------KQLGIHLVQQEVDVALVPGLSiAENIMLDRLAEPGIA--FRWGRLRQLARealaq 130
Cdd:PRK15064 85 vimghtelwEVKQERDRiyalpemsEEDGMKVADLEVKFAEMDGYT-AEARAGELLLGVGIPeeQHYGLMSEVAP----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 131 ldvsldvrrsidsctlAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRrlQRQGIGIVfISHRIHELKAVC 210
Cdd:PRK15064 159 ----------------GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN--ERNSTMII-ISHDRHFLNSVC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 211 DTLTVLRDGRL-IESGPMAD--LSGEQIVEKMLGH--------------------------------------ELSDIFP 249
Cdd:PRK15064 220 THMADLDYGELrVYPGNYDEymTAATQARERLLADnakkkaqiaelqsfvsrfsanaskakqatsrakqidkiKLEEVKP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 250 PKRPPHS-----DEVL----LQVEGL----HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLTRGEL- 315
Cdd:PRK15064 300 SSRQNPFirfeqDKKLhrnaLEVENLtkgfDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE--PDSGTVk 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 316 ---NSQP-WRPRDPADSVARGLALVP--EERRKEGifieepvAMNLAVSadSSFSRWsLFGhrqawrwAEEVIARVgirt 389
Cdd:PRK15064 378 wseNANIgYYAQDHAYDFENDLTLFDwmSQWRQEG-------DDEQAVR--GTLGRL-LFS-------QDDIKKSV---- 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 503994372 390 sgpaqtlRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAID 442
Cdd:PRK15064 437 -------KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE 482
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
272-448 |
1.14e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.32 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCK---ALFGASKSRLTRGELNSQPW-RPRDpadsvarglaLVPEeRRKEGI-- 345
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQhlnGLLQPTSGTVTIGERVITAGkKNKK----------LKPL-RKKVGIvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 ------FIEEPVA-------MNLAVSADssfsrwslfghrQAWRWAEEVIARVGIrtsgPAQTLRR----LSGGNQQKVA 408
Cdd:PRK13634 92 qfpehqLFEETVEkdicfgpMNFGVSEE------------DAKQKAREMIELVGL----PEELLARspfeLSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503994372 409 IGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREG 448
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEK 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
260-452 |
1.16e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQpwrprdpADSVargLAL 335
Cdd:CHL00131 7 ILEIKNLHasvnENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFK-------GESI---LDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 336 VPEERRKEGIFI--EEPVAMNLAVSADssFSRWSLFGHRQAWRWAE-------EVIAR----VGIRTSgpaqTLRR---- 398
Cdd:CHL00131 77 EPEERAHLGIFLafQYPIEIPGVSNAD--FLRLAYNSKRKFQGLPEldpleflEIINEklklVGMDPS----FLSRnvne 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 399 -LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVI 452
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSII 205
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-225 |
1.18e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHaHYE---GEVVINNQSVSIRSPRDAKQLGI 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE-DYEvtgGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 83 HLV-QQEVDvalVPGLS------IAENIMLD-RLAEPGIAFRWgrlRQLAREALAQLDVSLD-VRRSID---SCTLAEKQ 150
Cdd:PRK09580 81 FMAfQYPVE---IPGVSnqfflqTALNAVRSyRGQEPLDRFDF---QDLMEEKIALLKMPEDlLTRSVNvgfSGGEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 151 QILLARALSHHcrFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAV-CDTLTVLRDGRLIESG 225
Cdd:PRK09580 155 DILQMAVLEPE--LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
38-225 |
1.27e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 38 GANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPrdaKQLGIHLVQQEvdVALVPGLSIAENIMLD-RLAEPGIAFR 116
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQS--YALYPHLSVAENMSFGlKLAGAKKEEI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 117 WGRLRQLAReaLAQLDVSLDvrRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLD-----QNESE--RLFavvRRL 189
Cdd:PRK11000 111 NQRVNQVAE--VLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvQMRIEisRLH---KRL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 503994372 190 QRQGIgivFISHRIHELKAVCDTLTVLRDGRLIESG 225
Cdd:PRK11000 184 GRTMI---YVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
254-494 |
1.62e-05 |
|
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: 47.43 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 254 PHSDEVLLQVE---GLHDEgLLQDISLRLRKGEILGIAGLAGAGKTELCKALF-------------GASKSRLTRGEL-- 315
Cdd:TIGR01193 470 LNGDIVINDVSysyGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVgffqarsgeillnGFSLKDIDRHTLrq 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 316 --NSQPWRPRDPADSVARGLALvpeeRRKEGIFIEEPVAMNLAVSADSSFSRWSLfghrqawrwaeeviarvGIRTSgPA 393
Cdd:TIGR01193 549 fiNYLPQEPYIFSGSILENLLL----GAKENVSQDEIWAACEIAEIKDDIENMPL-----------------GYQTE-LS 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 394 QTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDV----KAKTDLFNAIDglaregKGVIYASGEFaELVGLCDRIC 469
Cdd:TIGR01193 607 EEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTitekKIVNNLLNLQD------KTIIFVAHRL-SVAKQSDKII 679
|
250 260
....*....|....*....|....*
gi 503994372 470 VLWDGRIVAEIPGAEAREENILYYS 494
Cdd:TIGR01193 680 VLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
399-476 |
1.62e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.95 E-value: 1.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 399 LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGL-AREGKGVIYASGEFAELVGLCDRICVLWDGRI 476
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
272-477 |
1.71e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.72 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRLTR---GEL--NSQpwrprDPADSVARGLALvpeERRKEG-I 345
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-----NLLERptsGRVlvDGQ-----DLTALSEKELRK---ARRQIGmI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 F----------IEEPVAMNL---AVSADSSFSRwslfghrqawrwAEEVIARVGI---RTSGPAQtlrrLSGGNQQKVAI 409
Cdd:PRK11153 88 FqhfnllssrtVFDNVALPLelaGTPKAEIKAR------------VTELLELVGLsdkADRYPAQ----LSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 410 GKWLRGNANVLIFDEPTKGVDvKAKTDlfnAIDGLARE-----GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALD-PATTR---SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
272-476 |
1.82e-05 |
|
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: 46.18 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLTRG--ELNSQPWRPRD---------------PADSVAR 331
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlerPDSGTILFGgeDATDVPVQERNvgfvfqhyalfrhmtVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 332 GLALVPEERRKEGIFIEEPVaMNLAvsadsSFSRWSLFGHRQawrwaeeviarvgirtsgPAQtlrrLSGGNQQKVAIGK 411
Cdd:cd03296 98 GLRVKPRSERPPEAEIRAKV-HELL-----KLVQLDWLADRY------------------PAQ----LSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994372 412 WLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRI 476
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
257-484 |
2.01e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 257 DEVLLQVEGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSQpwrpRDPADSVArglalv 336
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE----LLTAENVW------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 337 pEERRKEGIFIEEPVAMNLAVSADSSFSrwslFGHRQAWRWAEEVIARVG----------IRTSGPAqtlrRLSGGNQQK 406
Cdd:PRK13642 78 -NLRRKIGMVFQNPDNQFVGATVEDDVA----FGMENQGIPREEMIKRVDeallavnmldFKTREPA----RLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 407 VAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAE 484
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSE 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
260-477 |
2.15e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLH----DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNsqpWRPRDPadsvargLAL 335
Cdd:PRK09580 1 MLSIKDLHvsveDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVE---FKGKDL-------LEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 336 VPEERRKEGIFI--EEPVA---------MNLAVSADSSFSRWSLFGHRQAWRWAEEVIARVGIrtsgPAQTLRR-----L 399
Cdd:PRK09580 71 SPEDRAGEGIFMafQYPVEipgvsnqffLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKM----PEDLLTRsvnvgF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 400 SGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLaREGKGVIYASGEFAELVGLC--DRICVLWDGRIV 477
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIkpDYVHVLYQGRIV 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-241 |
2.90e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVV-------------INNQSVsiRS------PRDAKQL- 80
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWaersiayvpqqawIMNATV--RGnilffdEEDAARLa 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 -GIHLVQQEVDVALVPGLSIAEnimldrLAEPGIAFRWGrlrQLARealaqldVSldvrrsidsctlaekqqilLARALS 159
Cdd:PTZ00243 754 dAVRVSQLEADLAQLGGGLETE------IGEKGVNLSGG---QKAR-------VS-------------------LARAVY 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELkAVCDTLTVLRDGRLIESGPMADLSGEQIVEKM 239
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTSLYATL 877
|
..
gi 503994372 240 LG 241
Cdd:PTZ00243 878 AA 879
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-175 |
3.55e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLcGTHA-----------HYEGEVVINNQSV---SI 71
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM-AMHAidgipkncqilHVEQEVVGDDTTAlqcVL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 72 RSPRDAKQL---GIHLVQQEVDVALVPGL---------SIAENIMLDRLAEPgiafrWGRLRQL------AREA--LAQL 131
Cdd:PLN03073 257 NTDIERTQLleeEAQLVAQQRELEFETETgkgkgankdGVDKDAVSQRLEEI-----YKRLELIdaytaeARAAsiLAGL 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503994372 132 DVSLDV-RRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLD 175
Cdd:PLN03073 332 SFTPEMqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
272-479 |
3.59e-05 |
|
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: 45.22 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGAskSRLTRGELnsqpWRPRDPADSVARGLALVPEERRKEGIFIeepV 351
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPDSGTV----TVRGRVSSLLGLGGGFNPELTGRENIYL---N 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 352 AMNLAVSADSSFSRwslfghrqawrwAEEVIARVGIrtsGPAQTL--RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGV 429
Cdd:cd03220 109 GRLLGLSRKEIDEK------------IDEIIEFSEL---GDFIDLpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503994372 430 DVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVLWDGRIVAE 479
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-225 |
3.74e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSG----FRALSNVAFTLTGGSVHALTGANGAGKS----TLMAVLC-----GTHAHYEGEVVINNQSVSIR 72
Cdd:PRK09473 13 LDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriGGSATFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 73 SPRdAKQlgIHLVQQEVDVALVP----GLSIAENIMLDRLAEPGIAFRwgrlrqlarEALAQLD-VSL-DVRRSID---- 142
Cdd:PRK09473 93 KLR-AEQ--ISMIFQDPMTSLNPymrvGEQLMEVLMLHKGMSKAEAFE---------ESVRMLDaVKMpEARKRMKmyph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 143 SCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQ-GIGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
....
gi 503994372 222 IESG 225
Cdd:PRK09473 241 MEYG 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
244-302 |
5.36e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 5.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 244 LSDIFPPKRPPHSDEVLLqveglhdeglLQDISLRLRKGEILGIAGLAGAGKTELCKAL 302
Cdd:COG1134 24 LKELLLRRRRTRREEFWA----------LKDVSFEVERGESVGIIGRNGAGKSTLLKLI 72
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
121-271 |
5.50e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 121 RQLAREALAQLDVSLDVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFIS 200
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT 201
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 201 HRIHELKAVCDTLTVLRDGRLIESGPMADLSgeqivEKMLGHELSdifppKRPPHSDEVLLQVEGLHDEGL 271
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGRVIADGKVDELK-----TKVGGRTLQ-----IRPAHAAELDRMVGAIAQAGL 262
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-237 |
6.16e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 7 EMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCG--THAHYEGEVVIN----NQSVSIRSPRDAKQL 80
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISgfpkKQETFARISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQEVDVALV--------PGLSIAENIM-LDRLAEpgiafrwgrLRQLarEALAQLDVSLDvrrSIDSCTLAEKQQ 151
Cdd:PLN03140 962 DIHSPQVTVRESLIysaflrlpKEVSKEEKMMfVDEVME---------LVEL--DNLKDAIVGLP---GVTGLSTEQRKR 1027
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 152 ILLARALSHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHR--IHELKAVCDTLTVLRDGRLIESGPMAD 229
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGPLGR 1107
|
....*...
gi 503994372 230 LSgEQIVE 237
Cdd:PLN03140 1108 NS-HKIIE 1114
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
379-452 |
6.16e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 6.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 379 EEVIARVGIRTSgPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLArEGKGVI 452
Cdd:PRK13409 194 DEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVL 265
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
271-430 |
1.07e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.29 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFgasksRL--TRGEL-------NS---QPWRprdpadsvaRGLALVPE 338
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-----RLlsTEGEIqidgvswNSvtlQTWR---------KAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 339 ErrkegIFI-EEPVAMNLavsadSSFSRWSlfgHRQAWRWAEEVIARVGIRTSGPAQTLRR------LSGGNQQKVAIGK 411
Cdd:TIGR01271 1300 K-----VFIfSGTFRKNL-----DPYEQWS---DEEIWKVAEEVGLKSVIEQFPDKLDFVLvdggyvLSNGHKQLMCLAR 1366
|
170
....*....|....*....
gi 503994372 412 WLRGNANVLIFDEPTKGVD 430
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLD 1385
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
268-433 |
1.12e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 268 DEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALfgASKSRLTRGELNSQ-----------PwrPRDPADSV----ARG 332
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL--NGEVLLDDGRIIYEqdlivarlqqdP--PRNVEGTVydfvAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 333 LALVPEerrkegiFIEEPVAMNLAVSADSSFSRWS-------LFGHRQAWRW---AEEVIARVGIrtsGPAQTLRRLSGG 402
Cdd:PRK11147 91 IEEQAE-------YLKRYHDISHLVETDPSEKNLNelaklqeQLDHHNLWQLenrINEVLAQLGL---DPDAALSSLSGG 160
|
170 180 190
....*....|....*....|....*....|.
gi 503994372 403 NQQKVAIGKWLRGNANVLIFDEPTKGVDVKA 433
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-221 |
1.25e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 6 LEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVInnqsvsirsprdAKqlGIHL- 84
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------------AK--GIKLg 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 85 --VQQEVDValvpgLSIAENIM--LDRLAEPgiafrwgRLRQLAREALAQLDVSLD-VRRSIDSCTLAEKQQILLARALS 159
Cdd:PRK10636 379 yfAQHQLEF-----LRADESPLqhLARLAPQ-------ELEQKLRDYLGGFGFQGDkVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994372 160 HHCRFLILDEPTAPLDQNESERLFAVVrrLQRQGiGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-298 |
1.45e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 126 EALAQLDVS-LDVRRSIDSCTLAEKQQILLARAL---SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISH 201
Cdd:PRK00635 791 HALCSLGLDyLPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 202 RIHELKaVCDtltvlrdgRLIESGP---------MADLSGEQIVEK-----------MLGHE----LSDifPPKRPPHSD 257
Cdd:PRK00635 871 NMHVVK-VAD--------YVLELGPeggnlggylLASCSPEELIHLhtptakalrpyLSSPQelpyLPD--PSPKPPVPA 939
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503994372 258 EVLLQVEGLHDeglLQDISLRLRKGEILGIAGLAGAGKTEL 298
Cdd:PRK00635 940 DITIKNAYQHN---LKHIDLSLPRNALTAVTGPSASGKHSL 977
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-213 |
1.85e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 27 TLTGGSVHALTGANGAGKSTLM---AVLCGTHAHYEGevvinnqsvsirsPRDAKQLGIHLVQQEVDVA-LVPGLSIAEn 102
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILdaiGLALGGAQSATR-------------RRSGVKAGCIVAAVSAELIfTRLQLSGGE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 103 imldrlaepgiafrwgrlRQLAREALaqldvsldvrrsidsctlaekqqiLLARALSHHCRFLILDEPTAPLDQNESERL 182
Cdd:cd03227 83 ------------------KELSALAL------------------------ILALASLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....
gi 503994372 183 FAVVRRL---QRQGIgivFISHRiHELKAVCDTL 213
Cdd:cd03227 121 AEAILEHlvkGAQVI---VITHL-PELAELADKL 150
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-496 |
2.00e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 42.98 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALfgaskSRLTrgELNSQPwrpRDPADSVARG-----LALVPEERRKEGI 345
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-----NRLI--ELYPEA---RVSGEVYLDGqdifkMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 346 F----------IEEPVAMNLAVSADSSfSRWSLFghrQAWRWAEE---VIARVGIRTSGPAQtlrRLSGGNQQKVAIGKW 412
Cdd:PRK14247 88 FqipnpipnlsIFENVALGLKLNRLVK-SKKELQ---ERVRWALEkaqLWDEVKDRLDAPAG---KLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 413 LRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREgKGVIYASGEFAELVGLCDRICVLWDGRIVAEIPGAEA----REE 488
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVftnpRHE 239
|
....*...
gi 503994372 489 NILYYSTG 496
Cdd:PRK14247 240 LTEKYVTG 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
272-477 |
2.48e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.15 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 272 LQDISLRLRKGEILGIAGLAGAGKTELCKALFGasksrL---TRGElnsqpwrprdpadsvARGLALVPEERRKEgifie 348
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG-----IlvpTSGE---------------VRVLGYVPFKRRKE----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 349 epVAMNLAVsadssfsrwsLFGHRQAWRW----AE--EVIARV-GIRTSGPAQTLRRLSGG-------NQQ--KVAIGKW 412
Cdd:COG4586 93 --FARRIGV----------VFGQRSQLWWdlpaIDsfRLLKAIyRIPDAEYKKRLDELVELldlgellDTPvrQLSLGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 413 LRG--------NANVLIFDEPTKGVDVKAKTDLFNAIDGLARE-GKGVIYASGEFAELVGLCDRICVLWDGRIV 477
Cdd:COG4586 161 MRCelaaallhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-224 |
2.62e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 60 GEVVINNQSVSIRSPRDAKQLgIHLVQQEvdvALVPGLSIAENIMLDR----LAEPGIAFRWGRLRQLAREALAQLDVsl 135
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNL-FSIVSQE---PMLFNMSIYENIKFGKedatREDVKRACKFAAIDEFIESLPNKYDT-- 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 136 DVRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNeSERLF--AVVRRLQRQGIGIVFISHRIHELKAvCDTL 213
Cdd:PTZ00265 1351 NVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIekTIVDIKDKADKTIITIAHRIASIKR-SDKI 1428
|
170
....*....|....*
gi 503994372 214 TVL----RDGRLIES 224
Cdd:PTZ00265 1429 VVFnnpdRTGSFVQA 1443
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
399-471 |
2.92e-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: 41.79 E-value: 2.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 399 LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREG-KGVIYASGEFAELVGLCDRICVL 471
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
12-51 |
3.15e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 3.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503994372 12 SLAFSGFRALSNVAFTLtgGSVHALTGANGAGKSTLMAVL 51
Cdd:COG4637 4 RIRIKNFKSLRDLELPL--GPLTVLIGANGSGKSNLLDAL 41
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
397-478 |
3.46e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 43.28 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 397 RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAReGKGVIYASgefAELVGL--CDRICVLWDG 474
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMIT---HRLTGLeqFDRICVMDNG 549
|
....
gi 503994372 475 RIVA 478
Cdd:PRK11160 550 QIIE 553
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
268-476 |
4.22e-04 |
|
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: 41.69 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 268 DEGLLQDISLRLRKGEILGIAGLAGAGKTElCKALFgASKSRLTRGE--LNSQPWR---------------------PRD 324
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST-VVALL-ENFYQPQGGQvlLDGKPISqyehkylhskvslvgqepvlfARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 325 PADSVARGLALVPEERRKEgifieepvamnlAVSADSSFSRWSLFGHrqawrwaeeviarvGIRTsGPAQTLRRLSGGNQ 404
Cdd:cd03248 104 LQDNIAYGLQSCSFECVKE------------AAQKAHAHSFISELAS--------------GYDT-EVGEKGSQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 405 QKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAI-DGLAREGKGVIyasGEFAELVGLCDRICVLWDGRI 476
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALyDWPERRTVLVI---AHRLSTVERADQILVLDGGRI 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-62 |
4.26e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 4.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 4 NRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEV 62
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-231 |
4.36e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 20 ALSNVAFTLTGGSVHALTGANGAGKSTLMAVLcgtHAHY---EGEvvINNQSVSIRSPR-DAKQLGIHLVQQevdvalVP 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLI---QRHFdvsEGD--IRFHDIPLTKLQlDSWRSRLAVVSQ------TP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 96 GL---SIAENIMLDRlaePGIAFRwgRLRQLAREALAQLDVsLDVRRSIDS--------CTLAEKQQILLARALSHHCRF 164
Cdd:PRK10789 399 FLfsdTVANNIALGR---PDATQQ--EIEHVARLASVHDDI-LRLPQGYDTevgergvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 165 LILDEPTAPLD-QNESERLFAVvrRLQRQGIGIVFISHRIHELKAVCDTLtVLRDGRLIESGPMADLS 231
Cdd:PRK10789 473 LILDDALSAVDgRTEHQILHNL--RQWGEGRTVIISAHRLSALTEASEIL-VMQHGHIAQRGNHDQLA 537
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
154-201 |
4.81e-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: 41.44 E-value: 4.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 503994372 154 LARALSHHCRFLILDEPTAPLD-QNESERLFAVVRRLQRQGIG-IVFISH 201
Cdd:cd03240 132 LAETFGSNCGILALDEPTTNLDeENIEESLAEIIEERKSQKNFqLIVITH 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
396-487 |
4.82e-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: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 396 LRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGV----IYASGEfaELVGLCDRICVL 471
Cdd:TIGR00956 207 VRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTplvaIYQCSQ--DAYELFDKVIVL 284
|
90
....*....|....*.
gi 503994372 472 WDGRIVAEIPGAEARE 487
Cdd:TIGR00956 285 YEGYQIYFGPADKAKQ 300
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
260-484 |
5.47e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 260 LLQVEGLH----DEGL----LQDISLRLRKGEILGIAGLAGAGKTELCKALFGasksrltrgeLNSQPWRPRdpADSVAR 331
Cdd:PRK11022 3 LLNVDKLSvhfgDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG----------LIDYPGRVM--AEKLEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 332 G----LALVPEERRKegiFIEEPVAM---NLAVSADSSFS-----RWSLFGHR---QAWRW--AEEVIARVGIrtSGPAQ 394
Cdd:PRK11022 71 NgqdlQRISEKERRN---LVGAEVAMifqDPMTSLNPCYTvgfqiMEAIKVHQggnKKTRRqrAIDLLNQVGI--PDPAS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 395 TL----RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAR-EGKGVIYASGEFAELVGLCDRIC 469
Cdd:PRK11022 146 RLdvypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKII 225
|
250
....*....|....*
gi 503994372 470 VLWDGRIVAEIPGAE 484
Cdd:PRK11022 226 VMYAGQVVETGKAHD 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
370-476 |
5.99e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.59 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 370 GHRQAWR-WAEEVIARVGIR---TSGPAQtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLA 445
Cdd:PRK11247 105 GLKGQWRdAALQALAAVGLAdraNEWPAA----LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLW 180
|
90 100 110
....*....|....*....|....*....|..
gi 503994372 446 RE-GKGVIYASGEFAELVGLCDRICVLWDGRI 476
Cdd:PRK11247 181 QQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
266-304 |
6.08e-04 |
|
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: 41.77 E-value: 6.08e-04
10 20 30
....*....|....*....|....*....|....*....
gi 503994372 266 LHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG 304
Cdd:cd03291 47 LVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG 85
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
399-477 |
7.10e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.31 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 399 LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYA----SGEFAelvglcDRICVLWDG 474
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhrlsTIEKA------DEILVVEDG 554
|
...
gi 503994372 475 RIV 477
Cdd:PRK11176 555 EIV 557
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
271-430 |
7.88e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.10 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKSRLTRGELNSqpwrprdPADSVARGLALVpeerrkEGIFIEEP 350
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV-------PDNQFGREASLI------DAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VamNLAVsadssfsrwslfghrqawrwaeEVIARVGIrtsGPAQTLRR----LSGGNQQKVAIGKWLRGNANVLIFDEPT 426
Cdd:COG2401 112 F--KDAV----------------------ELLNAVGL---SDAVLWLRrfkeLSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
....
gi 503994372 427 KGVD 430
Cdd:COG2401 165 SHLD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-201 |
9.00e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNISLAFSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAH-YEGEVVI-NNQSVSIRSPRDAKQ-L 80
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgYSNDLTLfGRRRGSGETIWDIKKhI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 G-----IHL---VQQEVDVALVPGL--SIaenimldrlaepGIaFRW--GRLRQLAREALAQLDVSLDVRRS-IDSCTLA 147
Cdd:PRK10938 339 GyvsssLHLdyrVSTSVRNVILSGFfdSI------------GI-YQAvsDRQQKLAQQWLDILGIDKRTADApFHSLSWG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 148 EKQQILLARALSHHCRFLILDEPTAPLDqnESERLfaVVRRLQRQGIG-----IVFISH 201
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLD--PLNRQ--LVRRFVDVLISegetqLLFVSH 460
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
397-477 |
9.28e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.87 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 397 RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLaREGKGVIYASGEFAElVGLCDRICVLWDGRI 476
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLST-VRNADRILVFDNGRV 547
|
.
gi 503994372 477 V 477
Cdd:PRK13657 548 V 548
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
4-202 |
9.81e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 41.66 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNISLAF-SGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVI------------------ 64
Cdd:TIGR00954 450 NGIKFENIPLVTpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpakgklfyvpqrpymtlg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 65 --NNQSVSIRSPRDAKQLGIHlvqqevDVALVpglSIAENIMLDRLaepgiafrwgrlrqLAREalaqldVSLD-VRRSI 141
Cdd:TIGR00954 530 tlRDQIIYPDSSEDMKRRGLS------DKDLE---QILDNVQLTHI--------------LERE------GGWSaVQDWM 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994372 142 DSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESERLFavvRRLQRQGIGIVFISHR 202
Cdd:TIGR00954 581 DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY---RLCREFGITLFSVSHR 638
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
398-479 |
1.00e-03 |
|
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: 40.67 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 398 RLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLaREGKGVIYASGEFAELVGlCDRICVLWDGRIV 477
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
..
gi 503994372 478 AE 479
Cdd:cd03254 217 EE 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-223 |
1.16e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.66 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 3 GNRLEMQNISLAFSGF--RALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSirsprdakQL 80
Cdd:cd03288 17 GGEIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--------KL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 81 GIHLVQQEVDVALVPGLSIAENIML----------DRLAEpgiAFRWGRLRQLAREALAQLDVSldVRRSIDSCTLAEKQ 150
Cdd:cd03288 89 PLHTLRSRLSIILQDPILFSGSIRFnldpeckctdDRLWE---ALEIAQLKNMVKSLPGGLDAV--VTEGGENFSVGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 151 QILLARALSHHCRFLILDEPTAPLDQnESERLFAVVRRLQRQGIGIVFISHRIHELKAVcDTLTVLRDGRLIE 223
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVSTILDA-DLVLVLSRGILVE 234
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
119-236 |
1.19e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 119 RLRQLAREALAQLDVSldvrRSIDSCTLAEKQQILLARALSHHCRFL--ILDEPTAPLDQNESERLFAVVRRLQRQGIGI 196
Cdd:cd03270 117 RLGFLVDVGLGYLTLS----RSAPTLSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTV 192
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 503994372 197 VFISHrihelkavcDTLTVLRDGRLIESGPMADLSGEQIV 236
Cdd:cd03270 193 LVVEH---------DEDTIRAADHVIDIGPGAGVHGGEIV 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
392-479 |
1.35e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.15 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 392 PAQtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEFAELVGLCDRICVL 471
Cdd:PRK10584 144 PAQ----LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRL 219
|
....*...
gi 503994372 472 WDGRIVAE 479
Cdd:PRK10584 220 VNGQLQEE 227
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-203 |
1.38e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 4 NRLEMQNislaFSGFRALSNVAFTltgGSVHALTGANGAGKSTLM----AVLCGTHAHY-----------------EGEV 62
Cdd:COG0419 3 LRLRLEN----FRSYRDTETIDFD---DGLNLIVGPNGAGKSTILeairYALYGKARSRsklrsdlinvgseeasvELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 63 VINNQSVSIRSPRDAKQLGIHLVQQEVDVAL--VPGLSIAENIMlDRLAEpgiafrwgrLRQLAREALAQLDVSLDVRRS 140
Cdd:COG0419 76 EHGGKRYRIERRQGEFAEFLEAKPSERKEALkrLLGLEIYEELK-ERLKE---------LEEALESALEELAELQKLKQE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994372 141 I--------DSCTL--AEKQQILLARALShhcrfLILDepTAPLDQNESERLFAVVRRLQrqgigivFISHRI 203
Cdd:COG0419 146 IlaqlsgldPIETLsgGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-223 |
1.39e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 21 LSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVINNQSVSIRSPRD-AKQLGIhLVQQEVdvaLVPGlSI 99
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlRKVLGI-IPQAPV---LFSG-TV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 100 AENimLDRLAEPGIAFRWGRL-RQLAREALAQLDVSLD--VRRSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQ 176
Cdd:PLN03130 1330 RFN--LDPFNEHNDADLWESLeRAHLKDVIRRNSLGLDaeVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503994372 177 neseRLFAVVRRLQRQ---GIGIVFISHRIHELKAvCDTLTVLRDGRLIE 223
Cdd:PLN03130 1408 ----RTDALIQKTIREefkSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
266-464 |
1.45e-03 |
|
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: 41.43 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 266 LHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG---ASKSRLT---RGELNSQ-PW-RPRDPADSVARGLALvp 337
Cdd:TIGR01271 436 LYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGelePSEGKIKhsgRISFSPQtSWiMPGTIKDNIIFGLSY-- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 338 EERRKEGIF----IEEPVamnlavsadssfsrwSLFGHRQawrwaEEVIARVGIrtsgpaqtlrRLSGGNQQKVAIGKWL 413
Cdd:TIGR01271 514 DEYRYTSVIkacqLEEDI---------------ALFPEKD-----KTVLGEGGI----------TLSGGQRARISLARAV 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994372 414 RGNANVLIFDEPTKGVDVKAKTDLFNA-----------------IDGLAREGK------GVIYASGEFAELVGL 464
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLDVVTEKEIFESclcklmsnktrilvtskLEHLKKADKilllheGVCYFYGTFSELQAK 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-236 |
1.62e-03 |
|
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: 41.15 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 131 LDVSLD-VRRSIDSCTLA--EKQQILLARALSH---HCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIH 204
Cdd:TIGR00630 814 CDVGLGyIRLGQPATTLSggEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD 893
|
90 100 110
....*....|....*....|....*....|..
gi 503994372 205 ELKaVCDTltvlrdgrLIESGPMADLSGEQIV 236
Cdd:TIGR00630 894 VIK-TADY--------IIDLGPEGGDGGGTVV 916
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-221 |
1.74e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 23 NVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHYEGEVVinnqsvsirspRDAKQLGIHLVQQEVDvalvpGLSIAEN 102
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHHVD-----GLDLSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 103 IMLDRL-AEPGIafrwgrLRQLAREALAQLDVSLDVR-RSIDSCTLAEKQQILLARALSHHCRFLILDEPTAPLDQNESE 180
Cdd:PLN03073 591 PLLYMMrCFPGV------PEQKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE 664
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503994372 181 RLFAVVRRLQRqgiGIVFISHRIHELKAVCDTLTVLRDGRL 221
Cdd:PLN03073 665 ALIQGLVLFQG---GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-231 |
2.06e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 135 LDVRRSIDSCTLAEKQQILLARAL---SHHCRFLILDEPTAPLDQNESERLFAVVRRLQRQGIGIVFISHRIHELKAVcD 211
Cdd:PRK00635 1691 LPLGQNLSSLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQA-D 1769
|
90 100
....*....|....*....|....*.
gi 503994372 212 TLTVL------RDGRLIESGPMADLS 231
Cdd:PRK00635 1770 YLIEMgpgsgkTGGKILFSGPPKDIS 1795
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-230 |
2.37e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 12 SLAFSGFR---------ALSNVAFTLTGGSVHALTGANGAGKSTL------MAVLCGthahyeGEVVINNQSVSIRSPRD 76
Cdd:PTZ00243 1308 SLVFEGVQmryreglplVLRGVSFRIAPREKVGIVGRTGSGKSTLlltfmrMVEVCG------GEIRVNGREIGAYGLRE 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 77 AKQLGIHLVQqevDVALVPGlSIAENimLDRLAEPGIAFRWGRLRQLA-REALAQLDvsldvrRSIDSCTL--------A 147
Cdd:PTZ00243 1382 LRRQFSMIPQ---DPVLFDG-TVRQN--VDPFLEASSAEVWAALELVGlRERVASES------EGIDSRVLeggsnysvG 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 148 EKQQILLARA-LSHHCRFLILDEPTAPLDQNESERLFAVVRRlQRQGIGIVFISHRIHELkAVCDTLTVLRDGRLIESGP 226
Cdd:PTZ00243 1450 QRQLMCMARAlLKKGSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGS 1527
|
....
gi 503994372 227 MADL 230
Cdd:PTZ00243 1528 PREL 1531
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
240-477 |
2.87e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 240 LGHELSDIFPPKRPPHS--DEVLLQVEGLH---DEGL---LQDISLRLRKGEILGIAGLAGAGKTELCKALFGASKsrLT 311
Cdd:PLN03232 1212 LPSEATAIIENNRPVSGwpSRGSIKFEDVHlryRPGLppvLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE--LE 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 312 RGELNSqpwrprDPADSVARGLALVpeeRRKEGIFIEEPVAMNLAVSAD-SSFSRwslfgHRQAWRWaeEVIARVGIR-- 388
Cdd:PLN03232 1290 KGRIMI------DDCDVAKFGLTDL---RRVLSIIPQSPVLFSGTVRFNiDPFSE-----HNDADLW--EALERAHIKdv 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 389 -TSGP----AQTL---RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASgEFAE 460
Cdd:PLN03232 1354 iDRNPfgldAEVSeggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH-RLNT 1432
|
250
....*....|....*..
gi 503994372 461 LVGlCDRICVLWDGRIV 477
Cdd:PLN03232 1433 IID-CDKILVLSSGQVL 1448
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
117-199 |
2.94e-03 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 39.52 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 117 WGRLRQLAREALAQLDVSLDVRR-SIDSCTlaEKQQILLARALSHHCRFLILdeptAPLDqneSERLFAVVRRLQRQGIG 195
Cdd:cd20004 14 WKSVKAGAEKAAQELGVEIYWRGpSREDDV--EAQIQIIEYFIDQGVDGIVL----APLD---RKALVAPVERARAQGIP 84
|
....
gi 503994372 196 IVFI 199
Cdd:cd20004 85 VVII 88
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
392-468 |
3.05e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994372 392 PAQTLRRLSGGNQQKVAIGKWLRGNAN--VLIFDEPTKGVDVKAKTDLFNAIDGLAREGKGVIYASGEfAELVGLCDRI 468
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRI 547
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
271-454 |
3.28e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 39.09 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 271 LLQDISLRLRKGEILGIAGLAGAGKTELCKALFGASksRLTRGELNsqpWRPRDPADSVARGLAlvpeerrkegIFIEEP 350
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL--PPAAGTIK---LDGGDIDDPDVAEAC----------HYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 351 VAMNLAVSADSSFSRWSLFgHRQAWRWAEEVIARVGIrtsGPAQTL--RRLSGGNQQKVAIGKWLRGNANVLIFDEPTKG 428
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAF-LGGEELDIAAALEAVGL---APLAHLpfGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*.
gi 503994372 429 VDVKAKTDLFNAIDGLAREGKGVIYA 454
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
267-304 |
3.47e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.78 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|....*...
gi 503994372 267 HDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFG 304
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG 49
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-66 |
4.23e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 38.40 E-value: 4.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 503994372 15 FSGFRALSNVAFTLTGGSVHALTGANGAGKSTLMAVLCGTHAHY---EGEVVINN 66
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG 71
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
399-494 |
4.30e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 39.71 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 399 LSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAidgLAREGKGVIYASGEFAeLVGLCDRICVLWDGRIVA 478
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLS-TVERADQILVLKKGSVVE 693
|
90
....*....|....*.
gi 503994372 479 EIPGAEAREENILYYS 494
Cdd:TIGR00958 694 MGTHKQLMEDQGCYKH 709
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
233-477 |
4.33e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 39.83 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 233 EQIVEkMLGHELSDIFPPKRPPHSDEVL------LQVEGLHDEGLLQDISLRLRKGEILGIAGLAGAGKTELCKALFGAS 306
Cdd:PRK11174 322 ESLVT-FLETPLAHPQQGEKELASNDPVtieaedLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 307 K---SRLTRG----ELNSQPWRprdpadsvaRGLALVPEERRKEGIFIEEPVAMNLAVSADSSFsrWSLFghRQAWrwAE 379
Cdd:PRK11174 401 PyqgSLKINGielrELDPESWR---------KHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQL--QQAL--ENAW--VS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 380 EVIAR--------VGIRTSGpaqtlrrLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGLAReGKGV 451
Cdd:PRK11174 466 EFLPLlpqgldtpIGDQAAG-------LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTT 537
|
250 260
....*....|....*....|....*.
gi 503994372 452 IYASGEFAELVGlCDRICVLWDGRIV 477
Cdd:PRK11174 538 LMVTHQLEDLAQ-WDQIWVMQDGQIV 562
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
398-477 |
4.69e-03 |
|
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: 38.67 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 398 RLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDVKAKTDLFNAIDGlAREGKGVIYASGEFAELVGlCDRICVLWDGRIV 477
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
279-431 |
5.77e-03 |
|
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: 38.54 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994372 279 LRKGEILGIAGLAGAGKTELCKALFGASKSrlTRGELNSqpwrprdPADSVArglaLVPEErrkegifieepvamnlaVS 358
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKP--DEGDIEI-------ELDTVS----YKPQY-----------------IK 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994372 359 ADSSFSRWSLF-----GHRQAWRWAEEVIARVGIRtSGPAQTLRRLSGGNQQKVAIGKWLRGNANVLIFDEPTKGVDV 431
Cdd:cd03237 72 ADYEGTVRDLLssitkDFYTHPYFKTEIAKPLQIE-QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| |
