|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-506 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 1037.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTER 80
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMVG 240
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 241 RELTALYPNEPHTTGDEILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQWEGKIY 320
Cdd:PRK13549 242 RELTALYPREPHTIGEVILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 321 IDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFTGGiSQLDDAAEQKCILESIQQLKVKTSSPD 400
Cdd:PRK13549 322 IDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGG-SRIDDAAELKTILESIQRLKVKTASPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 401 LAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHE 480
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
490 500
....*....|....*....|....*.
gi 1014292979 481 GKLKANLINHNLTQEQVMEAALRSEH 506
Cdd:PRK13549 481 GKLKGDLINHNLTQEQVMEAALRSEH 506
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-502 |
0e+00 |
|
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: 926.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTERKGI 83
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHNG-IMDYDLMTLRCQKLLAQVSLSISPDTR-VGDLGLGQQQLVEIAKALNKQV 161
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGgRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 162 RLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMVGR 241
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 242 ELTALYPNEPHTTGDEILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQWEGKIYI 321
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 322 DGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFTgGISQLDDAAEQKCILESIQQLKVKTSSPDL 401
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFC-FKMRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 402 AIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
490 500
....*....|....*....|.
gi 1014292979 482 KLKANLINHNLTQEQVMEAAL 502
Cdd:TIGR02633 480 KLKGDFVNHALTQEQVLAAAL 500
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-508 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 759.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTER 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS--GEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMVG 240
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 241 RELTALYPNEPHTTGDEILRIEHLTAWhpvnrhiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIY 320
Cdd:COG1129 239 RELEDLFPKRAAAPGEVVLEVEGLSVG-------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-ADSGEIR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 321 IDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFT-GGIsqLDDAAEQKCILESIQQLKVKTSSP 399
Cdd:COG1129 311 LDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSrGGL--LDRRRERALAEEYIKRLRIKTPSP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 400 DLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMR 468
|
490 500
....*....|....*....|....*....
gi 1014292979 480 EGKLKANLINHNLTQEQVMEAALRSEHHV 508
Cdd:COG1129 469 EGRIVGELDREEATEEAIMAAATGGAAAA 497
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-500 |
0e+00 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 664.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTERKGI 83
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRD--AAGMSEDDIITMMVGR 241
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDcrADEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 242 ELTALYPNEPHTTGDEILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQWEGKIY 320
Cdd:NF040905 241 DLEDRYPERTPKIGEVVFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYGRNISGTVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 321 IDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFT-GGIsqLDDAAEQKCILESIQQLKVKTSSP 399
Cdd:NF040905 321 KDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSrRGV--IDENEEIKVAEEYRKKMNIKTPSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 400 DLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
490 500
....*....|....*....|.
gi 1014292979 480 EGKLKANLINHNLTQEQVMEA 500
Cdd:NF040905 479 EGRITGELPREEASQERIMRL 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-502 |
0e+00 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 544.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTER 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA--GSILYLGKEVTFNGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEITHN-GIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:PRK10762 79 AGIGIIHQELNLIPQLTIAENIFLGREFVNRfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMV 239
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 240 GRELTALYPNEPHTTGDEILRIEHLTAwhpvnrhiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKI 319
Cdd:PRK10762 239 GRKLEDQYPRLDKAPGEVRLKVDNLSG--------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT-SGYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 320 YIDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFTGGISQLDDAAEQKCILESIQQLKVKTSSP 399
Cdd:PRK10762 310 TLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 400 DLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMH 469
|
490 500
....*....|....*....|...
gi 1014292979 480 EGKLKANLINHNLTQEQVMEAAL 502
Cdd:PRK10762 470 EGRISGEFTREQATQEKLMAAAV 492
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-497 |
1.55e-177 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 508.80 E-value: 1.55e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGEEIQASHIRDTE 79
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPD---SGEILIDGKPVRIRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMV 239
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 240 GRELTALYPNEPHTTGDEILRIEHLTAwhPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKI 319
Cdd:COG3845 239 GREVLLRVEKAPAEPGEVVLEVENLSV--RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA-SGSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 320 YIDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKF---TGGI---SQLDDAAEQKcilesIQQLK 393
Cdd:COG3845 316 RLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPpfsRGGFldrKAIRAFAEEL-----IEEFD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 394 VKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSD 473
Cdd:COG3845 391 VRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSD 470
|
490 500
....*....|....*....|....
gi 1014292979 474 RVLVMHEGKLKANLINHNLTQEQV 497
Cdd:COG3845 471 RIAVMYEGRIVGEVPAAEATREEI 494
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-502 |
3.57e-175 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 502.52 E-value: 3.57e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTER 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA--GSILIDGQEMRFASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK11288 79 AGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGT-RDAAGMSEDDIITMMV 239
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQAMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 240 GRELTALYPNEPHTTGDEILRIEHLTAwhpvnrhIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKI 319
Cdd:PRK11288 239 GREIGDIYGYRPRPLGEVRLRLDGLKG-------PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRT-AGQV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 320 YIDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFTGGISQLDDAAEQKCILESIQQLKVKTSSP 399
Cdd:PRK11288 311 YLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 400 DLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:PRK11288 391 EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMR 470
|
490 500
....*....|....*....|...
gi 1014292979 480 EGKLKANLINHNLTQEQVMEAAL 502
Cdd:PRK11288 471 EGRIAGELAREQATERQALSLAL 493
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-505 |
5.54e-152 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 443.84 E-value: 5.54e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKGI 83
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK--GTITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHN----GIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMV 239
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 240 GRELTALYPNEPHTTG----DEILRIEHLTAwhpvnRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQw 315
Cdd:PRK09700 243 GRELQNRFNAMKENVSnlahETVFEVRNVTS-----RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 316 EGKIYIDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLA---ALNKFTGGISQLDDAAEQKCILESIQQL 392
Cdd:PRK09700 317 GGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYKGAMGLFHEVDEQRTAENQRELL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 393 KVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLS 472
Cdd:PRK09700 397 ALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVC 476
|
490 500 510
....*....|....*....|....*....|....
gi 1014292979 473 DRVLVMHEGKLKANLINHN-LTQEQVMEAALRSE 505
Cdd:PRK09700 477 DRIAVFCEGRLTQILTNRDdMSEEEIMAWALPQE 510
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-501 |
4.46e-151 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 440.71 E-value: 4.46e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 7 MKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGsyEGEIIFAGEEIQASHIRDTERKGIAII 86
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD--SGSILFQGKEIDFKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 87 HQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLIL 166
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 167 DEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMVGRELTAL 246
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 247 YPNEPHTTGDEILRIEHLTAWHPVNrhikrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQV 326
Cdd:PRK10982 239 FPDKENKPGEVILEVRNLTSLRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSAGTITLHGKKI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 327 DIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFTGGISQLDDAAEQKCILESIQQLKVKTSSPDLAIGRL 406
Cdd:PRK10982 313 NNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKAN 486
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
490
....*....|....*
gi 1014292979 487 LINHNLTQEQVMEAA 501
Cdd:PRK10982 473 VDTKTTTQNEILRLA 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-512 |
4.54e-115 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 349.35 E-value: 4.54e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTER 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS--GTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEiTHNGIMDydlmtlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFGLP-KRQASMQ------KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMM-- 238
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAItp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 239 VGRELT---------ALYPNEP-HTTGDEILRIEHLTAwhpvnrhiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLF 308
Cdd:PRK15439 239 AAREKSlsasqklwlELPGNRRqQAAGAPVLTVEDLTG--------EGFRNISLEVRAGEILGLAGVVGAGRTELAETLY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 309 GVWPgQWEGKIYIDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNItlAALNKFTGGISQldDAAEQKCILES 388
Cdd:PRK15439 311 GLRP-ARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNV--CALTHNRRGFWI--KPARENAVLER 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 389 I-QQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPE 467
Cdd:PRK15439 386 YrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEE 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1014292979 468 VLGLSDRVLVMHEGKLKANLINHNLTQEQVMEAALrSEHHVEKQS 512
Cdd:PRK15439 466 IEQMADRVLVMHQGEISGALTGAAINVDTIMRLAF-GEHQAQEAS 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
255-483 |
7.70e-86 |
|
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: 262.37 E-value: 7.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 255 GDEILRIEHLTAWhpvnrhiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIRNCQQA 334
Cdd:cd03215 1 GEPVLEVRGLSVK-------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-PASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 335 IAQGIAMVPEDRKRDGIVPVMAVGKNITLAALnkftggisqlddaaeqkcilesiqqlkvktsspdlaigrLSGGNQQKA 414
Cdd:cd03215 73 IRAGIAYVPEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-483 |
5.73e-74 |
|
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: 242.89 E-value: 5.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPH-GSYEGEIIFAGEEIQASHIRD 77
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHgGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERKgIAIIHQE--LALVKeLTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAK 155
Cdd:COG1123 81 RGRR-IGMVFQDpmTQLNP-VTVGDQIAEALE---NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDI 234
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 235 ITMMVGRELTALYPNEPHTTGDE-ILRIEHLTAWHPVNR--HIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW 311
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAEpLLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 312 PGQwEGKIYIDGKQVDIRNCQQ--AIAQGIAMVPEDrKRDGIVPVMAVGKNITLAALNKFTGGISQLDDAAEQkcILESI 389
Cdd:COG1123 316 RPT-SGSILFDGKDLTKLSRRSlrELRRRVQMVFQD-PYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAE--LLERV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 390 qQLkvktsSPDLA---IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSEL 465
Cdd:COG1123 392 -GL-----PPDLAdryPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDL 465
|
490
....*....|....*...
gi 1014292979 466 PEVLGLSDRVLVMHEGKL 483
Cdd:COG1123 466 AVVRYIADRVAVMYDGRI 483
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-223 |
8.44e-67 |
|
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: 212.67 E-value: 8.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKGIA 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS--GEILVDGKEVSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQelalvkeltvleniflgneithngimdydlmtlrcqkllaqvslsispdtrvgdLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGT 223
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
2.59e-49 |
|
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: 170.22 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTER 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR--PTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTL------------RCQKLLAQVSLSISPDTRVGDLGLGQQ 148
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLprarreereareRAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 149 QLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-221 |
3.93e-49 |
|
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: 168.77 E-value: 3.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKGIA 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTL-------RCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARReereareRAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 158 NKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-482 |
8.52e-48 |
|
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: 173.33 E-value: 8.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKS----TLMKVLCgiYPHGSYEGEIIFAGEEI-QAS- 73
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLP--DPAAHPSGSILFDGQDLlGLSe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 74 ----HIRDTErkgIAIIHQE--LALVKELTVleniflGNEIT-----HNGIMDYDLMTlRCQKLLAQVSLSiSPDTRVGD 142
Cdd:COG4172 84 relrRIRGNR---IAMIFQEpmTSLNPLHTI------GKQIAevlrlHRGLSGAAARA-RALELLERVGIP-DPERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 143 ----LGLGQQQLVEIAKALNKQVRLLILDEPTASL--TEQETsvLLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICVI 215
Cdd:COG4172 153 yphqLSGGQRQRVMIAMALANEPDLLIADEPTTALdvTVQAQ--ILDLLKDLQReLGMALLLITHDLGVVRRFADRVAVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 216 RDG---------------QHIGTRdaagmseddiitMMVGRELTALyPNEPHTTGDEILRIEHLTAWHPVNR-------- 272
Cdd:COG4172 231 RQGeiveqgptaelfaapQHPYTR------------KLLAAEPRGD-PRPVPPDAPPLLEARDLKVWFPIKRglfrrtvg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 273 HIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGqwEGKIYIDGKQVDIRNcqqaiaqGIAMVPEdRKRDGIV 352
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS--EGEIRFDGQDLDGLS-------RRALRPL-RRRMQVV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 ---------PVMAVGKNIT--LAALNKftggisQLDDAAEQKCILESIQQ--LkvktsSPDlAIGR----LSGGNQQK-A 414
Cdd:COG4172 368 fqdpfgslsPRMTVGQIIAegLRVHGP------GLSAAERRARVAEALEEvgL-----DPA-ARHRypheFSGGQRQRiA 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 415 IlARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:COG4172 436 I-ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-243 |
4.78e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.22 E-value: 4.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTERkgIA 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR--PTSGEVRVLGEDVARDPAEVRRR--IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENI-FLGneithnGI--MDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:COG1131 77 YVPQEPALYPDLTVRENLrFFA------RLygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 162 RLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSE---DDIITMM 238
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKArllEDVFLEL 230
|
....*
gi 1014292979 239 VGREL 243
Cdd:COG1131 231 TGEEA 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-219 |
1.08e-40 |
|
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: 146.54 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQasHIRDTERKGI 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVR--KEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEIthNGIMDYDLmTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAEL--YGLFDEEL-KKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-219 |
3.75e-39 |
|
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: 141.86 E-value: 3.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTE- 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDI--SKLSEKEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 ----RKGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLmtlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAK 155
Cdd:cd03255 77 aafrRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRE---RAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKlNEVKAISDTICVIRDGQ 219
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-219 |
1.37e-38 |
|
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: 138.68 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDteRKGIA 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK--PDSGEIKVLGKDIKKEPEEV--KRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIflgneithngimdydlmtlrcqkllaqvslsispdtrvgDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03230 77 YLPEEPSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-219 |
4.10e-38 |
|
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: 139.63 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS-VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQASHIRD--TERK 81
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL--VEPTSGSVLIDGTDINKLKGKAlrQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLENIFLGNEITHNGI-----MDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:cd03256 79 QIGMIFQQFNLIERLSVLENVLSGRLGRRSTWrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-219 |
6.95e-38 |
|
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: 138.04 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPHGsyeGEIIFAGEEIQAshiRDTERKGI 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDS---GEILIDGRDVTG---VPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLK---LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQrELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-482 |
9.76e-38 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 145.23 E-value: 9.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF---GSVK-AIDNVCLRLNAGEIVSLCGENGSGKS----TLMKVLCG---IYPHGsyegEIIFAGE---- 68
Cdd:PRK15134 5 LLAIENLSVAFrqqQTVRtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPSG----DIRFHGEsllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 69 --EIQASHIRDTErkgIAIIHQE-LALVKELTVLENIFLGNEITHNGiMDYDLM---TLRCqklLAQVSLSiSPDTRVGD 142
Cdd:PRK15134 81 asEQTLRGVRGNK---IAMIFQEpMVSLNPLHTLEKQLYEVLSLHRG-MRREAArgeILNC---LDRVGIR-QAAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 143 ----LGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRD 217
Cdd:PRK15134 153 yphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 218 GQHIGTRDAagmseddiitmmvgrelTALY--PNEPHT--------TGDE---------ILRIEHLTAWHPVNRHIKR-- 276
Cdd:PRK15134 233 GRCVEQNRA-----------------ATLFsaPTHPYTqkllnsepSGDPvplpepaspLLDVEQLQVAFPIRKGILKrt 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 ------VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQweGKIYIDGKQVDIRNCQQaiaqgiaMVPEdRKRDG 350
Cdd:PRK15134 296 vdhnvvVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ--GEIWFDGQPLHNLNRRQ-------LLPV-RHRIQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 351 IV---PVMAVgkNITLAALNKFTGGIS----QLDDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLN 423
Cdd:PRK15134 366 VVfqdPNSSL--NPRLNVLQIIEEGLRvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILK 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
2.69e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.10 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPhgsYEGEIIFAGEEI----- 70
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRP---TSGEVLIDGQDIsslse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 71 -QASHIRdteRKGIAIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQ 149
Cdd:COG1136 78 rELARLR---RRHIGFVFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 150 LVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLnEVKAISDTICVIRDGQ 219
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-219 |
3.62e-37 |
|
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: 136.06 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGS--VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGEEIQASHIRDTeRKGI 83
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKEL-RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQ--ELALVKeLTVLENIFLGNEitHNGiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:cd03225 78 GLVFQnpDDQFFG-PTVEEEVAFGLE--NLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 162 RLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-219 |
3.83e-36 |
|
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: 134.00 E-value: 3.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQASHIRDTeRKGI 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP--TSGEVLVDGKDITKKNLREL-RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQ--ELALVKElTVLENI-F----LGneithngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:COG1122 78 GLVFQnpDDQLFAP-TVEEDVaFgpenLG--------LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
277-499 |
6.50e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 133.83 E-value: 6.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPgqWEGKIYIDGKQVDIRNcqQAIAQGIAMVPEDRkrdGIVPVM 355
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKP--DSGSILIDGEDVRKEP--REARRQIGVLPDER---GLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 AVGKNItlaalnKFTGGISQLDDAAEQKCILESIQQLKVkTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:COG4555 90 TVRENI------RYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 436 IDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQEQVME 499
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-483 |
9.07e-36 |
|
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: 139.55 E-value: 9.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEII----------------FAGE 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 69 EIQ----------------ASHIRDTERKGIAIIHQE-LALVKELTVLENIFLG-NEITHNGimdyDLMTLRCQKLLAQV 130
Cdd:TIGR03269 81 PCPvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEAlEEIGYEG----KEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 131 SLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAIS 209
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 210 DTICVIRDGQHIgtrdAAGMSEDDIITMMVGreLTALYPNEPHTTGDEILRIEHLTA-WHPVNRH-IKRVNDVSFSLKRG 287
Cdd:TIGR03269 237 DKAIWLENGEIK----EEGTPDEVVAVFMEG--VSEVEKECEVEVGEPIIKVRNVSKrYISVDRGvVKAVDNVSLEVKEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 288 EILGIAGLVGAGRTETIQCLFGVWPGQwEGKIY-------IDGKQVDIRNCQQAiAQGIAMVPEDRkrdGIVPVMAVGKN 360
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEPT-SGEVNvrvgdewVDMTKPGPDGRGRA-KRYIGILHQEY---DLYPHRTVLDN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 361 ITLAAlnkftgGISQLDDAAEQKcileSIQQLKVKTSSPDLAIG-------RLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:TIGR03269 386 LTEAI------GLELPDELARMK----AVITLKMVGFDEEKAEEildkypdELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 434 RGIDIGAKYEIYKLI-NQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:TIGR03269 456 GTMDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-219 |
1.23e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.86 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTeRKGIA 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP--PTSGEIYLDGKPLSAMPPPEW-RRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKElTVLENIFLGNEITHngiMDYDLMTLRcqKLLAQVSLSISP-DTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQLRE---RKFDRERAL--ELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
259-485 |
1.38e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.49 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTawhpvnrhiKR------VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQ 332
Cdd:COG1131 1 IEVRGLT---------KRygdktaLDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGE--DVARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 333 QAIAQGIAMVPEDrkrDGIVPVMAVGKNItlaalnKFTGGISQLDDAAEQKCILESIQQLKVkTSSPDLAIGRLSGGNQQ 412
Cdd:COG1131 69 AEVRRRIGYVPQE---PALYPDLTVRENL------RFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVA 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-219 |
1.48e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 132.81 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGS-VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQASHIRD--TER 80
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL--VEPSSGSILLEGTDITKLRGKKlrKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQK-----LLAQVSLSISPDTRVGDLGLGQQQLVEIAK 155
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKeralsALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-200 |
3.39e-35 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 130.68 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQAShiRDTERKGI 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP--PSAGEVLWNGEPIRDA--REDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENI-----FLGNEITHNGIMDydlmtlrcqkLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:COG4133 78 AYLGHADGLKPELTVRENLrfwaaLYGLRADREAIDE----------ALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISH 200
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-253 |
6.26e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 131.33 E-value: 6.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTE--R 80
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE--PTSGEILVDGQDVTALRGRALRrlR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGNEITHNGI-----MDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAK 155
Cdd:COG3638 80 RRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWrsllgLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDdi 234
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDA-- 237
|
250
....*....|....*....
gi 1014292979 235 itmmvgrELTALYPNEPHT 253
Cdd:COG3638 238 -------VLREIYGGEAEE 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-171 |
9.62e-35 |
|
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: 127.38 E-value: 9.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTeRKGIAIIHQELALVKELTVL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 100 ENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:pfam00005 78 ENLRLGLLLKG---LSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-219 |
1.74e-34 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 129.55 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQA--SHIRD 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS--GSIIFDGKDLLKlsRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERKGIAIIHQE--LALVKELTVLENIflgNEI--THNGIMDYDLMTLRCQKLLAQVSLSIS-PDTRVGDLGLGQQQLVE 152
Cdd:cd03257 79 IRRKEIQMVFQDpmSSLNPRMTIGEQI---AEPlrIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 153 IAKALNKQVRLLILDEPTASL---TEQEtsvLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03257 156 IARALALNPKLLIADEPTSALdvsVQAQ---ILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
259-482 |
5.82e-34 |
|
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: 127.55 E-value: 5.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNrHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIRNCQQAIAQG 338
Cdd:cd03224 1 LEVENLNAGYGKS-QI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 IAMVPEDRkrdGIVPVMAVGKNITLAAlnkFTGGISQLDDAAEQkcILESIQQLKVKTSSPDlaiGRLSGGNQQKAILAR 418
Cdd:cd03224 77 IGYVPEGR---RIFPELTVEENLLLGA---YARRRAKRKARLER--VYELFPRLKERRKQLA---GTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 419 CLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-219 |
8.77e-34 |
|
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: 125.76 E-value: 8.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQA-SHIRDTERKGI 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE--PDSGSILIDGEDLTDlEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGneithngimdydlmtlrcqkllaqvsLSispdtrvGdlglGQQQLVEIAKALNKQVRL 163
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG--------------------------LS-------G----GQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-219 |
3.18e-33 |
|
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: 125.47 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDterkgIA 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL--PDSGEVLFDGKPLDIAARNR-----IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLEN-IFLGN-------EITHNgiMDYdlmtlrcqkLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:cd03269 74 YLPEERGLYPKMKVIDQlVYLAQlkglkkeEARRR--IDE---------WLERLELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
5.75e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 128.68 E-value: 5.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRdTER 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET--PDSGRILLDGRDV--TGLP-PEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLG--------NEITHngimdydlmtlRCQKLLAQVSLSISPDTRVGDL-GlGQQQLV 151
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGlrmrgvpkAEIRA-----------RVAELLELVGLEGLADRYPHQLsG-GQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 152 EIAKALNKQVRLLILDEPTASL-------TEQEtsvlldiIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDG--QHI 221
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALdaklreeMREE-------LRRLQRElGITFIYVTHDQEEALALADRIAVMNDGriEQV 217
|
..
gi 1014292979 222 GT 223
Cdd:COG3842 218 GT 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
258-483 |
1.17e-32 |
|
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: 124.54 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPV-NRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDI--RNCQQA 334
Cdd:cd03257 1 LLEVKNLSVSFPTgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-SGSIIFDGKDLLKlsRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 335 IAQGIAMVPED--RKRDgivPVMAVGKNITLAALNKFTGGisqlDDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQ 412
Cdd:cd03257 80 RRKEIQMVFQDpmSSLN---PRMTIGEQIAEPLRIHGKLS----KKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-248 |
1.46e-32 |
|
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: 124.53 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQASHIRDTe 79
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP--WSGEVTFDGRPVTRRRRKAF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQ--ELALVKELTVLEniFLGNEITHNGIMDYDlmtLRCQKLLAQVSLSIS-PDTRVGDLGLGQQQLVEIAKA 156
Cdd:COG1124 78 RRRVQMVFQdpYASLHPRHTVDR--ILAEPLRIHGLPDRE---ERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 157 LNKQVRLLILDEPTASLteqETSV---LLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSED 232
Cdd:COG1124 153 LILEPELLLLDEPTSAL---DVSVqaeILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
250
....*....|....*.
gi 1014292979 233 diITMMVGRELTALYP 248
Cdd:COG1124 230 --PKHPYTRELLAASL 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
277-483 |
4.96e-32 |
|
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: 120.97 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQQAIAQGIAMVPEDrkrDGIVPVMA 356
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-SGEIKVLGK--DIKKEPEEVKRRIGYLPEE---PSLYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNItlaalnkftggisqlddaaeqkcilesiqqlkvktsspdlaigRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:cd03230 90 VRENL-------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1014292979 437 DIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-219 |
5.12e-32 |
|
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: 122.25 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIR-DTERKGI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS--GTIIIDGLKLTDDKKNiNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHNgiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-219 |
6.25e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 120.04 E-value: 6.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRdTERKGIAI 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKLPLE-ELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 86 IHQelalvkeltvleniflgneithngimdydlmtlrcqkllaqvsLSispdtrvgdlgLGQQQLVEIAKALNKQVRLLI 165
Cdd:cd00267 78 VPQ-------------------------------------------LS-----------GGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 166 LDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-219 |
8.22e-32 |
|
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: 121.77 E-value: 8.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEI--QASHIRdtERKG 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGSIRFDGRDItgLPPHER--ARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENIFLGNEITHNG----IMD--YDLMTlRCQKLLAQvslsispdtRVGDLGLGQQQLVEIAKA 156
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAkrkaRLErvYELFP-RLKERRKQ---------LAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-226 |
8.30e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 122.79 E-value: 8.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 3 YLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHGsyeGEIIFAGEEIQASHIRDTERK 81
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG---GTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLENIFLGNEITHN-GIMDYDLMTL-----------RCQKLLAQVSLSISPDTRVGDLGLGQQQ 149
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQHQQLKtGLFSGLLKTPafrraesealdRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 150 LVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHI--GTRDA 226
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLanGTPEE 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
259-482 |
1.31e-31 |
|
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: 119.98 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPvnrHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPgqWEGKIYIDGKQVDirncqqaiaQ 337
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEP--DSGSILIDGEDLT---------D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEDRKRDGIV-------PVMAVGKNITLAalnkftggisqlddaaeqkcilesiqqlkvktsspdlaigrLSGGN 410
Cdd:cd03229 67 LEDELPPLRRRIGMVfqdfalfPHLTVLENIALG-----------------------------------------LSGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-223 |
2.18e-31 |
|
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: 120.40 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHiRDTERKGiA 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS--GEITFDGKSYQKNI-EALRRIG-A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIhQELALVKELTVLENIFLGNEIthngimdYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03268 77 LI-EAPGFYPNLTARENLRLLARL-------LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGT 223
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
4.19e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQAshirdtER 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP--TSGTVRLFGKPPRR------AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKE--LTVLENIFLGNeITHNGIM------DYDlmtlRCQKLLAQVSLSISPDTRVGDL-GlGQQQLV 151
Cdd:COG1121 75 RRIGYVPQRAEVDWDfpITVRDVVLMGR-YGRRGLFrrpsraDRE----AVDEALERVGLEDLADRPIGELsG-GQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 152 EIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQH 220
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-236 |
7.56e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 120.15 E-value: 7.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQASHIRDTERKgI 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP--SSGEVLLDGRDLASLSRRELARR-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNeITHNGIM------DYDlmtlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGR-YPHLGLFgrpsaeDRE----AVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 158 NKQVRLLILDEPTASL-----TEqetsvLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHIgtrdAAGMSE 231
Cdd:COG1120 153 AQEPPLLLLDEPTSHLdlahqLE-----VLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIV----AQGPPE 223
|
....*
gi 1014292979 232 dDIIT 236
Cdd:COG1120 224 -EVLT 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-215 |
1.14e-30 |
|
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: 118.73 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRdter 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS--GEVLVDGEPVTGPGPD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 kgIAIIHQELALVKELTVLENIFLGNEIthNGIMDYDLMTlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:cd03293 75 --RGYVFQQDALLPWLTVLDNVALGLEL--QGVPKAEARE-RAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVI 215
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-223 |
1.61e-30 |
|
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: 118.38 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS--VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShiRDTERKG 82
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS--GTAYINGYSIRTD--RKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENIFLGNEIT--HNGIMDYDlmtlrCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKglPKSEIKEE-----VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQhGIACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKlrCIGS 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-214 |
2.74e-30 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 120.16 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSY-EGEIIFAGEEIQA---SHI 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGItSGEILFDGEDLLKlseKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 76 RDTERKGIAIIHQE--LAL--VkeLTVLEniFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSiSPDTRVGDL-----GlG 146
Cdd:COG0444 81 RKIRGREIQMIFQDpmTSLnpV--MTVGD--QIAEPLRIHGGLSKAEARERAIELLERVGLP-DPERRLDRYphelsG-G 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 147 QQQLVEIAKALNKQVRLLILDEPTASL--TEQetSVLLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICV 214
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALdvTIQ--AQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-223 |
2.93e-30 |
|
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: 117.72 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQAShirDTERKGIA 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF--ETPTSGEILLDGKDITNL---PPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKK---LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDG--QHIGT 223
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGkiQQIGT 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
256-482 |
3.80e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 117.78 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPvNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIRNCQQAI 335
Cdd:COG0410 1 MPMLEVENLHAGYG-GIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-PRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 AQGIAMVPEDRkrdGIVPVMAVGKNITLAALnkftggisQLDDAAEQKCILESIQQLkvktsSPDLA------IGRLSGG 409
Cdd:COG0410 77 RLGIGYVPEGR---RIFPSLTVEENLLLGAY--------ARRDRAEVRADLERVYEL-----FPRLKerrrqrAGTLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 410 NQQK-AIlARCLLLNPRILILDEPTRG-----IDigakyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:COG0410 141 EQQMlAI-GRALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-235 |
7.27e-30 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 116.83 E-value: 7.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQA--SHIRDTERKG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS--GEVLIDGEDISGlsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENI-FLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVaFPLRE---HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 162 RLLILDEPTASLTEQETSVLLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICVIRDGQHI--GTRDAAGMSEDDII 235
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVaeGTPEELRASDDPLV 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-240 |
1.40e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNIT-KTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKG 82
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS--GSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQE---LALVKELTVLENIFLGN----EITHNGIMDYDLMTLRCQKLLAQ--VSLSiSPDTRVGDLGLGQQQLVEI 153
Cdd:COG3845 335 VAYIPEDrlgRGLVPDMSVAENLILGRyrrpPFSRGGFLDRKAIRAFAEELIEEfdVRTP-GPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 154 AKALNKQVRLLILDEPTASL----TEQetsvLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGM 229
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLdvgaIEF----IHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
250
....*....|.
gi 1014292979 230 SEDDIITMMVG 240
Cdd:COG3845 490 TREEIGLLMAG 500
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-233 |
1.79e-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: 115.85 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQASHIRDTERKGI 83
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP--RSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLG-----NEITHNGIMD--YDLMTlRCQKLLAQvslsispdtRVGDLGLGQQQLVEIAKA 156
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGayarrDRAEVRADLErvYELFP-RLKERRRQ---------RAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 157 LNKQVRLLILDEPTA----SLTEQetsvLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSED 232
Cdd:COG0410 151 LMSRPKLLLLDEPSLglapLIVEE----IFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
.
gi 1014292979 233 D 233
Cdd:COG0410 227 P 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
254-500 |
2.02e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 254 TGDEILRIEHLTAW---HPVnrhikrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRN 330
Cdd:COG1121 2 MMMPAIELENLTVSyggRPV------LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT-SGTVRLFGKPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 331 cqqaiaQGIAMVPEDRKRDGIVP-----VMAVGknitLAALNKFTGGISQLDDAAeqkcILESIQQLKVKtsspDLA--- 402
Cdd:COG1121 75 ------RRIGYVPQRAEVDWDFPitvrdVVLMG----RYGRRGLFRRPSRADREA----VDEALERVGLE----DLAdrp 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 403 IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
250
....*....|....*...
gi 1014292979 483 LKANLINHNLTQEQVMEA 500
Cdd:COG1121 217 VAHGPPEEVLTPENLSRA 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-219 |
2.08e-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: 113.68 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTERKgIAI 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK--PSSGEILLDGKDLASLSPKELARK-IAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 86 IHQELALVkeltvleniflgnEITHngimdydlmtlrcqklLAqvslsispDTRVGDLGLGQQQLVEIAKALNKQVRLLI 165
Cdd:cd03214 78 VPQALELL-------------GLAH----------------LA--------DRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 166 LDEPTASL---TEQEtsvLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03214 121 LDEPTSHLdiaHQIE---LLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-219 |
2.48e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.15 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTE---- 79
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER--PTSGQVLVNGQDL--SRLKRREipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTG---KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 160 QVRLLILDEPTASLtEQETSV-LLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG2884 155 RPELLLADEPTGNL-DPETSWeIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
271-478 |
2.96e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.55 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 271 NRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNcqqaiaQGIAMVPEDRKRDG 350
Cdd:cd03235 11 GHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-SGSIRVFGKPLEKER------KRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 351 IVPVMAvgKNITLAALNKFTGGISQLDDAAEQKcILESIQQLKVKtsspDLA---IGRLSGGNQQKAILARCLLLNPRIL 427
Cdd:cd03235 82 DFPISV--RDVVLMGLYGHKGLFRRLSKADKAK-VDEALERVGLS----ELAdrqIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 428 ILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVM 478
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-219 |
6.68e-29 |
|
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: 114.22 E-value: 6.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPHgsyEGEIIFAGEEIQASHIRD- 77
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPT---SGSVLVDGTDLTLLSGKEl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 -TERKGIAIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:cd03258 78 rKARRRIGMIFQHFNLLSSRTVFENVALPLEIAG---VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-218 |
1.77e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 112.50 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIqaSHIRDTE---- 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS--GTIRVNGQDV--SDLRGRAipyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELALVKELTVLENIFLGNEITHNGimdYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVP---PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
259-485 |
2.14e-28 |
|
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: 112.43 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQaIAQG 338
Cdd:COG1122 1 IELENLSFSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-SGEVLVDGKDITKKNLRE-LRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 IAMV---PEDRkrdgIVpvMA-VGKNITLAALNKftgGISqlDDAAEQKcILESIQQL---KVKTSSPDlaigRLSGGNQ 411
Cdd:COG1122 77 VGLVfqnPDDQ----LF--APtVEEDVAFGPENL---GLP--REEIRER-VEEALELVgleHLADRPPH----ELSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 412 QKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-225 |
2.98e-28 |
|
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: 112.43 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQASHIRDterKGIA 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL--ERPDSGTILFGGEDATDVPVQE---RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEITH-NGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPrSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRD 225
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRieQVGTPD 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-219 |
3.32e-28 |
|
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: 117.86 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 2 PYLLEMKNITKTF-----------GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsyEGEIIFAGEEI 70
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS---EGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 71 QASHIRD--TERKGIAIIHQE--LALVKELTVLENIFLGNEItHNGIMDYDLMTLRCQKLLAQVSLSisPDTR------- 139
Cdd:COG4172 350 DGLSRRAlrPLRRRMQVVFQDpfGSLSPRMTVGQIIAEGLRV-HGPGLSAAERRARVAEALEEVGLD--PAARhryphef 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 140 VGdlglGQQQLVEIAKALNKQVRLLILDEPTASLteqETSV---LLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICVI 215
Cdd:COG4172 427 SG----GQRQRIAIARALILEPKLLVLDEPTSAL---DVSVqaqILDLLRDLQReHGLAYLFISHDLAVVRALAHRVMVM 499
|
....
gi 1014292979 216 RDGQ 219
Cdd:COG4172 500 KDGK 503
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
260-482 |
7.12e-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: 108.87 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 260 RIEHLTAWHPvnrHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDiRNCQQAIAQGI 339
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-PTSGEILIDGKDIA-KLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 340 AMVPEdrkrdgivpvmavgknitlaalnkftggisqlddaaeqkcilesiqqlkvktsspdlaigrLSGGNQQKAILARC 419
Cdd:cd00267 76 GYVPQ-------------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 420 LLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-483 |
1.18e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.88 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKS----TLMKVL--------CGIYPHGSYEGEIIFAG 67
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 68 EEIQAsHIRDTERKGIAIIHQElalvkELTVLENIF-LGNEIT-----HNGIMDYDLMtLRCQKLLAQVSLsisPDTRV- 140
Cdd:PRK10261 92 EQSAA-QMRHVRGADMAMIFQE-----PMTSLNPVFtVGEQIAesirlHQGASREEAM-VEAKRMLDQVRI---PEAQTi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 141 -----GDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICV 214
Cdd:PRK10261 162 lsrypHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 215 IRDGQHIGTRDA-------------AGMSEDDIITMMVGRELTALYP---------NEPHTT------GDEILRIEHLTA 266
Cdd:PRK10261 242 MYQGEAVETGSVeqifhapqhpytrALLAAVPQLGAMKGLDYPRRFPlislehpakQEPPIEqdtvvdGEPILQVRNLVT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 267 WHP--------VNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVD-IRNCQ-QAIA 336
Cdd:PRK10261 322 RFPlrsgllnrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRIDtLSPGKlQALR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEDrKRDGIVPVMAVGKNITLAALnkfTGGISQLDDAAEQKCILesIQQLKVKTSSPDLAIGRLSGGNQQKAIL 416
Cdd:PRK10261 401 RDIQFIFQD-PYASLDPRQTVGDSIMEPLR---VHGLLPGKAAAARVAWL--LERVGLLPEHAWRYPHEFSGGQRQRICI 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK10261 475 ARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-221 |
1.25e-27 |
|
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: 110.15 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIqashIRDTE--RKG 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS--GRATVAGHDV----VREPRevRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENIFLgneitHNGIMDY--DLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYI-----HARLYGVpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
258-485 |
1.47e-27 |
|
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: 110.15 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLT-AWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW-PGQweGKIYIDGkqVDIRNCQQAI 335
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDA--GFATVDG--FDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 AQGIAMVPEDRkrdGIVPVMAVGKNItlaalnKFTGGISQLDDAAEQKCILESIQQLKVKTSSpDLAIGRLSGGNQQKAI 415
Cdd:cd03266 77 RRRLGFVSDST---GLYDRLTARENL------EYFAGLYGLKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-235 |
1.81e-27 |
|
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: 110.45 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTE- 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS--GEILVDGQDITGLSEKELYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 -RKGIAIIHQELALVKELTVLENI-FLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:COG1127 80 lRRRIGMLFQGGALFDSLTVFENVaFPLREHTD---LSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 158 NKQVRLLILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDAAGMSEDDI 234
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKiiAEGTPEELLASDDPW 236
|
.
gi 1014292979 235 I 235
Cdd:COG1127 237 V 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-234 |
2.04e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 109.92 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKGIA 84
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKS--GSIRLDGEDITKLPPHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEIT---HNGIMD--YDLMTLrCQKLLAQvslsispdtRVGDLGLGQQQLVEIAKALNK 159
Cdd:TIGR03410 79 YVPQGREIFPRLTVEENLLTGLAALprrSRKIPDeiYELFPV-LKEMLGR---------RGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 160 QVRLLILDEPTASLteqETSVLLDI---IRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDI 234
Cdd:TIGR03410 149 RPKLLLLDEPTEGI---QPSIIKDIgrvIRRLrAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-219 |
2.51e-27 |
|
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: 109.58 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSY---EGEIIFAGEEIQASHIRDTE-R 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVkELTVLENIFLGneITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGL--GQQQLVEIAKALN 158
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIacIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELkKEYTI--VIVTHNMQQAARVADRTAFLLNGR 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-225 |
3.22e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.97 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQASHIRDT-----E 79
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP--DSGEVLWDGEPLDPEDRRRIgylpeE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RkgiaiihqelALVKELTVLENI-FLG-------NEITHNgiMDYdlmtlrcqkLLAQVSLSISPDTRVGDLGLGQQQLV 151
Cdd:COG4152 80 R----------GLYPKMKVGEQLvYLArlkglskAEAKRR--ADE---------WLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 152 EIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHI--GTRD 225
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsGSVD 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
258-485 |
3.37e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 109.75 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPvNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRN-CQQAIA 336
Cdd:COG1120 1 MLEAENLSVGYG-GRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGR--DLASlSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEDRkrdgivpvmAVGKNIT---LAALNKF--TGGISQLDDAAEQKcILESIQQLKVKtsspDLA---IGRLSG 408
Cdd:COG1120 75 RRIAYVPQEP---------PAPFGLTvreLVALGRYphLGLFGRPSAEDREA-VEEALERTGLE----HLAdrpVDELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-219 |
3.65e-27 |
|
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: 107.52 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTfgsvKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTERKGI 83
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP--PASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AII----HQElALVKELTVLENIFLGneithngimdydlmtlrcqkllaqVSLSispdtrvgdlGlGQQQLVEIAKALNK 159
Cdd:cd03215 78 AYVpedrKRE-GLVLDLSVAENIALS------------------------SLLS----------G-GNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 160 QVRLLILDEPTASL---TEQEtsvLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03215 122 DPRVLILDEPTRGVdvgAKAE---IYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-219 |
8.00e-27 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 106.31 E-value: 8.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS--VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQaSHIRDTERKG 82
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP--TSGEILIDGVDLR-DLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENIFLGneithngimdydlmtlrcqkllaqvslsispdtrvgdlglGQQQLVEIAKALNKQVR 162
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENILSG----------------------------------------GQRQRIAIARALLRDPP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 163 LLILDEPTASL---TEQEtsvLLDIIRDLQQhGIACIYISHKLNEVKaISDTICVIRDGQ 219
Cdd:cd03228 117 ILILDEATSALdpeTEAL---ILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-212 |
8.32e-27 |
|
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: 107.62 E-value: 8.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQAshirdtERKGIAI 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK--PTSGSIRVFGKPLEK------ERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 86 IHQELALVKE--LTVLENIFLGNEITHNGIMDYDlmTLRCQK---LLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:cd03235 73 VPQRRSIDRDfpISVRDVVLMGLYGHKGLFRRLS--KADKAKvdeALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTI 212
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-219 |
1.32e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQASHI--RDterkg 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL--EKPTEGQIFIDGEDVTHRSIqqRD----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENIFLGneITHNGIMDYDLMTlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYG--LKMLGVPKEERKQ-RVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 163 LLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-226 |
1.66e-26 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 112.93 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 15 GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTE-RKGIAIIHQELALV 93
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PYSGSILINGVDL--SDLDPASwRRQIAWVPQNPYLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 KElTVLENIFLGN-EIThngimDYDLmtlrcQKLLAQVSLS--IS-----PDTRVGDLGL----GQQQLVEIAKALNKQV 161
Cdd:COG4988 424 AG-TIRENLRLGRpDAS-----DEEL-----EAALEAAGLDefVAalpdgLDTPLGEGGRglsgGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 162 RLLILDEPTASL---TEQEtsvLLDIIRDLQQhGIACIYISHKLNEVKAiSDTICVIRDGQHI--GTRDA 226
Cdd:COG4988 493 PLLLLDEPTAHLdaeTEAE---ILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVeqGTHEE 557
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
275-485 |
2.21e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.60 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 275 KRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQ-QAIAQGIAMVPEdrkrdgivp 353
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGK--DLASLSpKELARKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 354 vmavgknitlaALNKFtgGISQLddaAEQKcilesiqqlkvktsspdlaIGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:cd03214 81 -----------ALELL--GLAHL---ADRP-------------------FNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 434 RGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
259-483 |
3.38e-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: 104.43 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPvnrHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPGqwEGKIYIDGKQVDIRNCQQAIAQ 337
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLyKPD--SGEILVDGKEVSFASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEdrkrdgivpvmavgknitlaalnkftggisqlddaaeqkcilesiqqlkvktsspdlaigrLSGGNQQKAILA 417
Cdd:cd03216 76 GIAMVYQ-------------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-226 |
3.96e-26 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 112.62 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFG--SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQASHIRDTeRKG 82
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP--TSGRILIDGIDLRQIDPASL-RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENIFLGNEithnGIMDYDLMTLrCQklLAQVSLSIS--P---DTRVGDLGL----GQQQLVEI 153
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLGDP----DATDEEIIEA-AR--LAGLHDFIEalPmgyDTVVGEGGSnlsgGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 154 AKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQhGIACIYISHKLnEVKAISDTICVIRDGQ--HIGTRDA 226
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRivEDGTHEE 695
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
278-482 |
4.19e-26 |
|
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: 105.63 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwPGQWEGKIYIDGKQVDiRNCQQAIAQGIAMV---PEDrkrdgivpv 354
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-LGPTSGEVLVDGKDLT-KLSLKELRRKVGLVfqnPDD--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 355 MAVGKNIT--LAalnkFTGGISQLDDAAEQKCILESIQQLKVKtSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:cd03225 87 QFFGPTVEeeVA----FGLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1014292979 433 TRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-232 |
4.48e-26 |
|
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: 106.71 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 2 PYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPhgSYEGEIIFAGEEIQASHIRDTeR 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPP--TYGNDVRLFGERRGGEDVWEL-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELA--LVKELTVLE--------NIFLGNEIThngimdyDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQL 150
Cdd:COG1119 78 KRIGLVSPALQlrFPRDETVLDvvlsgffdSIGLYREPT-------DEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 151 VEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEV-KAISDTIcVIRDGQHIgtrdAAG 228
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIpPGITHVL-LLKDGRVV----AAG 225
|
....
gi 1014292979 229 MSED 232
Cdd:COG1119 226 PKEE 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
259-483 |
5.15e-26 |
|
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: 106.43 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIRNcQQAIAQ 337
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER-PWSGEVTFDGRPVTRRR-RKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEDrKRDGIVPVMAVGKNITLAALnkftggISQLDDAAEQkcILESIQQLKVKTSSPDLAIGRLSGGNQQKAILA 417
Cdd:COG1124 80 RVQMVFQD-PYASLHPRHTVDRILAEPLR------IHGLPDREER--IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
277-483 |
5.38e-26 |
|
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: 105.98 E-value: 5.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAIAQGIAM---VPEdrkrdgIVP 353
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-SGSVLFDGEDITGLPPHEIARLGIGRtfqIPR------LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 354 VMAVGKNITLAALNKFTGGISQLDDAAEQKCILESIQQL--KVK-TSSPDLAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:cd03219 89 ELTVLENVMVAAQARTGSGLLLARARREEREARERAEELleRVGlADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-219 |
8.48e-26 |
|
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: 105.32 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKGIA 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GKILLDGQDITKLPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
259-485 |
1.15e-25 |
|
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: 104.51 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHIKrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQQAIAQG 338
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA-VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYINGY--SIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 IAMVPEDrkrDGIVPVMAVGKNITLAALNKftgGISQLDDAAEQKCILESIQQLKVKtsspDLAIGRLSGGNQQKAILAR 418
Cdd:cd03263 77 LGYCPQF---DALFDELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKA----NKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 419 CLLLNPRILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
3.11e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.71 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPHGSYEGEIIFAGEEIQ-----ASH 74
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlITGDKSAGSHIELLGRTVQregrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 75 IRDTeRKGIAIIHQELALVKELTVLENIF---LGNEITHNGIMDY--DLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQ 149
Cdd:PRK09984 81 IRKS-RANTGYIFQQFNLVNRLSVLENVLigaLGSTPFWRTCFSWftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 150 LVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-223 |
3.68e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 106.31 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDteRkGIA 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTS--GEILIGGRDVTDLPPKD--R-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGneithngimdydlmtLRCQKL--------LAQVS--LSISP--DTRVGDLGLGQQQLVE 152
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFP---------------LKLRKVpkaeidrrVREAAelLGLEDllDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 153 IAKALNKQVRLLILDEPTASL-------TEQEtsvlldiIRDLQQ-HGIACIYISHKLNEVKAISDTICVIRDG--QHIG 222
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLdaklrveMRAE-------IKRLHRrLGTTTIYVTHDQVEAMTLADRIAVMNDGriQQVG 216
|
.
gi 1014292979 223 T 223
Cdd:COG3839 217 T 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-219 |
4.00e-25 |
|
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: 103.10 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAshiRDTERKGIA 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS--GRIYIGGRDVTD---LPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRK---VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 165 ILDEPTASLTEQ-ETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03301 153 LMDEPLSNLDAKlRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
277-433 |
4.06e-25 |
|
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: 100.80 E-value: 4.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAiAQGIAMVPEDrkrDGIVPVMA 356
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-EGTILLDGQDLTDDERKSL-RKEIGYVFQD---PQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 357 VGKNITLAALNKFTGGISQLDDAAEqkcILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEE---ALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-219 |
5.22e-25 |
|
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: 108.70 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 2 PYLLEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHiRDTE 79
Cdd:COG4987 331 GPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD--PQSGSITLGGVDLRDLD-EDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELALVKElTVLENIFLGNEithnGIMDYDLMtlrcqKLLAQVSLS--IS--P---DTRVGDLGL----GQQ 148
Cdd:COG4987 408 RRRIAVVPQRPHLFDT-TLRENLRLARP----DATDEELW-----AALERVGLGdwLAalPdglDTWLGEGGRrlsgGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 149 QLVEIAKALNKQVRLLILDEPTASL---TEQEtsVLLDIIRDLQQHGIacIYISHKLNEVKAIsDTICVIRDGQ 219
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLdaaTEQA--LLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGR 546
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
277-482 |
1.16e-24 |
|
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: 101.59 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIrncqqAIAQGIAMVPEDRkrdGIVPVMA 356
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFDGKPLDI-----AARNRIGYLPEER---GLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKN-ITLAALNkftgGISqLDDAAEQkcILESIQQLKVkTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:cd03269 87 VIDQlVYLAQLK----GLK-KEEARRR--IDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1014292979 436 IDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-227 |
1.30e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEE------IQASHIRDT 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDS--GQLNIAGHQfdfsqkPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 ERKgIAIIHQELALVKELTVLENIF------LGneithngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVE 152
Cdd:COG4161 81 RQK-VGMVFQQYNLWPHLTVMENLIeapckvLG--------LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 153 IAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAA 227
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-279 |
1.37e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.03 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIqaSHIrDTERKGI 83
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--ETPDSGRIMLDGQDI--THV-PAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGneithngimdydlmtLRCQKL------------LAQVSLSISPDTRVGDLGLGQQQLV 151
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFG---------------LRMQKTpaaeitprvmeaLRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 152 EIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDG--QHIGT----- 223
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGriEQDGTpreiy 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 224 --------------------RDAAGMSEDDIITMMVGRELTaLYPNEPHTTGD--------EILRIEHLTAWHPVNRHIK 275
Cdd:PRK09452 234 eepknlfvarfigeinifdaTVIERLDEQRVRANVEGRECN-IYVNFAVEPGQklhvllrpEDLRVEEINDDEHAEGLIG 312
|
....
gi 1014292979 276 RVND 279
Cdd:PRK09452 313 YVRE 316
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
1.38e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 102.26 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiYPHGSyEGEIIFAGEEIQASHIRDTER 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRAT-SGRIVFDGKDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLG------NEITHNGIMDYDLMTlRCQKLLAQvslsispdtRVGDLGLGQQQLVEIA 154
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAMGgffaerDQFQERIKWVYELFP-RLHERRIQ---------RAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 155 KALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
258-483 |
1.67e-24 |
|
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: 103.98 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPV-NRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV--WPGQWEGKIYIDGKQV-------- 326
Cdd:COG0444 1 LLEVRNLKVYFPTrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpPPGITSGEILFDGEDLlklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 327 -DIRncqqaiAQGIAMVPEDrkrdgivPVMAVGKNI--TLAALNKFTGgisqldDAAEQKCI--LEsiqqlKVKTSSPDL 401
Cdd:COG0444 81 rKIR------GREIQMIFQDpmt-slnPVMTVGDQIaePLRIHGGLSK------AEARERAIelLE-----RVGLPDPER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 402 AIGR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVL 476
Cdd:COG0444 143 RLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA 222
|
....*..
gi 1014292979 477 VMHEGKL 483
Cdd:COG0444 223 VMYAGRI 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-219 |
1.93e-24 |
|
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: 101.22 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 30 GEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQASHIR---DTERKGIAIIHQELALVKELTVLENIFLGN 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGL--EKPDGGTIVLNGTVLFDSRKKinlPPQQRKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 107 EITHNGImdydlMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIR 186
Cdd:cd03297 101 KRKRNRE-----DRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....
gi 1014292979 187 DLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03297 176 QIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-203 |
2.14e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 101.71 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTE-RKG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITS--GDLIVDGLKVNDPKVDERLiRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENIFLGnEITHNGIMDYDLMTLrCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFG-PLRVRGASKEEAEKQ-ARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1014292979 163 LLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLN 203
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-218 |
4.13e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.13 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPHGsyeGEIIFAGeeIQASHIRDT 78
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGlLEPDA---GFATVDG--FDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 ERKGIAIIHQELALVKELTVLENI-FLGNEITHNGimdyDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLeYFAGLYGLKG----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 158 NKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-223 |
4.59e-24 |
|
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: 101.57 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 10 ITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQA---SHIRDTERKGIAII 86
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS--GKVLIDGQDIAAmsrKELRELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 87 HQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLIL 166
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQG---VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 167 DEPTASL-----TEQETSVLldiirDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:cd03294 185 DEAFSALdplirREMQDELL-----RLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRlvQVGT 244
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
277-483 |
5.05e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 99.90 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQaiaQGIAMVPEDrkrDGIVPVMA 356
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-SGEILIDGRDVTGVPPER---RNIGMVFQD---YALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITlaalnkFTGGISQLDDAAEQKCILESIQQLKVktsSPDLA--IGRLSGGNQQKAILARCLLLNPRILILDEPTR 434
Cdd:cd03259 89 VAENIA------FGLKLRGVPKAEIRARVRELLELVGL---EGLLNryPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1014292979 435 GIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-219 |
5.52e-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: 99.57 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGeIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShiRDTERKGIA 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS--GTIRIDGQDVLKQ--PQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLEniFLGNEITHNGIMDYDLMTlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03264 76 YLPQEFGVYPNFTVRE--FLDYIAWLKGIPSKEVKA-RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQHgiACIYIS-HKLNEVKAISDTICVIRDGQ 219
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGED--RIVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-223 |
6.74e-24 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 102.81 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLlEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShirDTER 80
Cdd:TIGR03265 2 SPYL-SIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTA--GTIYQGGRDITRL---PPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:TIGR03265 76 RDYGIVFQSYALFPNLTVADNIAYG---LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:TIGR03265 153 PGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVieQVGT 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-225 |
8.12e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 8.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDteRKgIA 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS--GHIRFHGTDVSRLHARD--RK-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLG------NEITHNGIMDYDLMtlrcqKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGltvlprRERPNAAAIKAKVT-----QLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDG--QHIGTRD 225
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGniEQAGTPD 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-221 |
8.20e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 8.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTERKgI 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--PTAGQIMLDGVDL--SHVPPYQRP-I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 164 LILDEPTASLTEQ-ETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK11607 171 LLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
232-483 |
1.81e-23 |
|
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: 104.15 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 232 DDIITMMVGRELTALYPNEPHTTGDeiLRIEHLT-AWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV 310
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGD--IELENVSfRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 311 WPgQWEGKIYIDGkqVDIRNC-QQAIAQGIAMVPEDRK------RDgivpvmavgkNITLAAlnkftGGIS--QLDDAAE 381
Cdd:COG2274 525 YE-PTSGRILIDG--IDLRQIdPASLRRQIGVVLQDVFlfsgtiRE----------NITLGD-----PDATdeEIIEAAR 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 382 QKCILESIQQLkvktssP---DLAIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQ 454
Cdd:COG2274 587 LAGLHDFIEAL------PmgyDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-K 659
|
250 260
....*....|....*....|....*....
gi 1014292979 455 GIAVIVISSELpEVLGLSDRVLVMHEGKL 483
Cdd:COG2274 660 GRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-219 |
2.26e-23 |
|
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: 98.28 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF-----GSVK--AIDNVCLRLNAGEIVSLCGENGSGKSTLMKvlcGIYphGSY---EGEIIF--AGE 68
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLK---CIY--GNYlpdSGSILVrhDGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 69 EI---QAShirdtERKGIAIIHQELALVKE-LTVL----------ENIF-LGneithngiMDYDLMTLRCQKLLAQVSL- 132
Cdd:COG4778 76 WVdlaQAS-----PREILALRRRTIGYVSQfLRVIprvsaldvvaEPLLeRG--------VDREEARARARELLARLNLp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 133 ----SISPDTRVGdlglGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAI 208
Cdd:COG4778 143 erlwDLPPATFSG----GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAV 218
|
250
....*....|.
gi 1014292979 209 SDTICVIRDGQ 219
Cdd:COG4778 219 ADRVVDVTPFS 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
279-483 |
2.62e-23 |
|
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: 98.56 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQqAIAQGIAMVPEDRkrdGIVPVMAVG 358
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGK--DITNLP-PEKRDISYVPQNY---ALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 359 KNITLaalnkftGGISQLDDAAEQKcilesiqqLKVKTSSPDLAI--------GRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:cd03299 90 KNIAY-------GLKKRKVDKKEIE--------RKVLEIAEMLGIdhllnrkpETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-223 |
3.45e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.61 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPhgsYEGEIIFAGEEIQAS-HIRDterKG 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLeTP---DSGRIVLNGRDLFTNlPPRE---RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENIFLG--------NEITHngimdydlmtlRCQKLLAQVSLSispdtrvgdlGL--------- 145
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGlrvrppskAEIRA-----------RVEELLELVQLE----------GLadrypsqls 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 146 -GQQQLVEIAKALNKQVRLLILDEPTASL-----TEQEtSVLLDIIRDLqqhGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG1118 136 gGQRQRVALARALAVEPEVLLLDEPFGALdakvrKELR-RWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGR 211
|
....*.
gi 1014292979 220 --HIGT 223
Cdd:COG1118 212 ieQVGT 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-226 |
3.87e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPyLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTER 80
Cdd:PRK09536 1 MP-MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA--GTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KgIAIIHQELALVKELTVLENIFLGNEiTHNGIMDYDLMTLR--CQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK09536 78 R-VASVPQDTSLSFEFDVRQVVEMGRT-PHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGqhiGTRDA 226
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG---RVRAA 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
277-486 |
3.91e-23 |
|
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: 98.00 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQweGKIYIDGKQVDIRNCQQAIAQGIAMVPED----RKrdgi 351
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPDS--GKILLDGQDITKLPMHKRARLGIGYLPQEasifRK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 352 vpvMAVGKNItLAALNKFTggisqlDDAAEQKCILES-IQQLKVKTSSPDLAIgRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:cd03218 90 ---LTVEENI-LAVLEIRG------LSKKEREEKLEElLEEFHITHLRKSKAS-SLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKAN 486
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-219 |
2.11e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 100.62 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 15 GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQasHI-RDTERKGIAIIHQELALV 93
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP--TSGRILIDGVDIR--DLtLESLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 KElTVLENIFLGN-EITHNGIMDydlmTLRcqklLAQVSLSIS--P---DTRVGDLGL----GQQQLVEIAKALNKQVRL 163
Cdd:COG1132 427 SG-TIRENIRYGRpDATDEEVEE----AAK----AAQAHEFIEalPdgyDTVVGERGVnlsgGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 164 LILDEPTASL---TEQEtsvLLDIIRDLQQhGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:COG1132 498 LILDEATSALdteTEAL---IQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGR 551
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-219 |
3.52e-22 |
|
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: 95.30 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGS---VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGEEIQASHIRDTeRKG 82
Cdd:cd03249 2 EFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFY--DPTSGEILLDGVDIRDLNLRWL-RSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVkELTVLENIFLG-NEIT-------------HNGIMdydlmtlrcqkllaqvSLSISPDTRVGDLGL--- 145
Cdd:cd03249 79 IGLVSQEPVLF-DGTIAENIRYGkPDATdeeveeaakkaniHDFIM----------------SLPDGYDTLVGERGSqls 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 146 -GQQQLVEIAKALNKQVRLLILDEPTASL-TEQETSV--LLDIIRDlqqhGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03249 142 gGQKQRIAIARALLRNPKILLLDEATSALdAESEKLVqeALDRAMK----GRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-215 |
4.67e-22 |
|
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: 99.28 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHiRDTERKGI 83
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD--PTEGSIAVNGVPLADAD-ADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVkELTVLENIFLG-----NEITHNGIMDYDLMTlrcqkLLAQVSLSIspDTRVGD----LGLGQQQLVEIA 154
Cdd:TIGR02857 399 AWVPQHPFLF-AGTIAENIRLArpdasDAEIREALERAGLDE-----FVAALPQGL--DTPIGEggagLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 155 KALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQhGIACIYISHKLnEVKAISDTICVI 215
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
259-482 |
4.92e-22 |
|
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: 94.08 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTawhpVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQQAIAQ 337
Cdd:COG4133 3 LEAENLS----CRRGERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-AGEVLWNGE--PIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEdrkRDGIVPVMAVGKNITL-AALNKFTGGISQLDDAAEQkCILESIQqlkvktsspDLAIGRLSGGNQQKAIL 416
Cdd:COG4133 76 RLAYLGH---ADGLKPELTVRENLRFwAALYGLRADREAIDEALEA-VGLAGLA---------DLPVRQLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGlsDRVLVMHEGK 482
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
279-485 |
5.94e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.10 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvdirnCQQAIAQGIAMVPEdRKRDGIV------ 352
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD-EGEIVLNGR------TLFDSRKGIFLPPE-KRRIGYVfqearl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 -PVMAVGKNITLAAlnKFTggisqldDAAEQKCILESIQQLkvktsspdLAI--------GRLSGGNQQKAILARCLLLN 423
Cdd:TIGR02142 87 fPHLSVRGNLRYGM--KRA-------RPSERRISFERVIEL--------LGIghllgrlpGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-219 |
9.91e-22 |
|
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: 93.09 E-value: 9.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFG-SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQAShirdTERKGIA 84
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK--ESSGSILLNGKPIKAK----ERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQEL--ALVKElTVLENIFLGNEITHNGIMdydlmtlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:cd03226 75 YVMQDVdyQLFTD-SVREELLLGLKELDAGNE-------QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 163 LLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-226 |
1.06e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAG------EEIQASHIRDT 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL--EMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 ERKgIAIIHQELALVKELTVLENIF------LGneithngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVE 152
Cdd:PRK11124 81 RRN-VGMVFQQYNLWPHLTVQQNLIeapcrvLG--------LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 153 IAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDA 226
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
259-483 |
1.31e-21 |
|
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: 98.29 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRN-CQQAIAQ 337
Cdd:COG4988 337 IELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-SGSILING--VDLSDlDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEDrkrdgivPVMAVG---KNITLAALNkftGGISQLDDAAEQKCILESIQQLkvktssP---DLAIG----RLS 407
Cdd:COG4988 412 QIAWVPQN-------PYLFAGtirENLRLGRPD---ASDEELEAALEAAGLDEFVAAL------PdglDTPLGeggrGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 408 GGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELpEVLGLSDRVLVMHEGKL 483
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRL-ALLAQADRILVLDDGRI 549
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
277-482 |
1.85e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.18 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWP--GQWEGKIYIDGKQvdIRNCQQAI-----AQGIAMVPEDrKRD 349
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAanGRIGGSATFNGRE--ILNLPEKElnklrAEQISMIFQD-PMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 350 GIVPVMAVGKNIT-LAALNKftgGISQlDDAAEqkcilESIQQLK-VKTSSPDLAIG----RLSGGNQQKAILARCLLLN 423
Cdd:PRK09473 109 SLNPYMRVGEQLMeVLMLHK---GMSK-AEAFE-----ESVRMLDaVKMPEARKRMKmyphEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-219 |
2.40e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.90 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS-VKAIDnvcLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTERKgI 83
Cdd:COG3840 2 LRLDDLTYRYGDfPLRFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLP--PDSGRILWNGQDL--TALPPAERP-V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLG-------NEITHNGIMDydlmtlrcqkLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGlrpglklTAEQRAQVEQ----------ALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 157 LNKQVRLLILDEPTASL---TEQEtsvLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG3840 144 LVRKRPILLLDEPFSALdpaLRQE---MLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
259-482 |
3.07e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 90.52 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPvNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQA-IAQ 337
Cdd:cd03228 1 IEFKNVSFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-SGEILIDG--VDLRDLDLEsLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEDrkrdgivPVMavgknitlaalnkFTGgisqlddaaeqkCILESIqqlkvktsspdlaigrLSGGNQQKAILA 417
Cdd:cd03228 77 NIAYVPQD-------PFL-------------FSG------------TIRENI----------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELpEVLGLSDRVLVMHEGK 482
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
278-483 |
3.11e-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: 92.56 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQQAIAQGIamvpedRKRDGIV----- 352
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-SGEVLIDGE--DISGLSEAELYRL------RRRMGMLfqsga 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 --PVMAVGKNITLAaLNKFTggisQLDDAAEQKCILESIQQLKVKTSSpDLAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:cd03261 88 lfDSLTVFENVAFP-LREHT----RLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-252 |
3.29e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.90 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGsyEGEIIFAGEEIQAShiRDTERKGIA 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVPAR--ARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEithngimdYDLMTLR-----CQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGR--------YFGMSTReieavIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIgtrdAAGmSEDDIITMMV 239
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI----AEG-RPHALIDEHI 264
|
250
....*....|...
gi 1014292979 240 GRELTALYPNEPH 252
Cdd:PRK13536 265 GCQVIEIYGGDPH 277
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-221 |
4.94e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.26 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKGI 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHNgiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
259-483 |
5.46e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.03 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTaWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDirncqqaiaqg 338
Cdd:COG4619 1 LELEGLS-FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-SGEIYLDGKPLS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 iAMVPED-RKRDGIV---PVM---AVGKNITLAalnkFTGGISQLDDAAeqkcILESIQQLKVKTSSPDLAIGRLSGGNQ 411
Cdd:COG4619 66 -AMPPPEwRRQVAYVpqePALwggTVRDNLPFP----FQLRERKFDRER----ALELLERLGLPPDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 412 QKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-219 |
6.95e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQAS--HIRdtERKG 82
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK--PDSGRIFLDGEDITHLpmHKR--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQvsLSISP--DTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRK---LSKKEREERLEELLEE--FGITHlrKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 161 VRLLILDEPTA-----SLTEqetsvLLDIIRDLQQHGIAcIYIS-HKLNEVKAISDTICVIRDGQ 219
Cdd:COG1137 155 PKFILLDEPFAgvdpiAVAD-----IQKIIRHLKERGIG-VLITdHNVRETLGICDRAYIISEGK 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-207 |
6.98e-21 |
|
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: 90.50 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTERKGIA 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR--PDSGEVRWNGTPL--AEQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEIthngimdYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:TIGR01189 77 YLGHLPGLKPELSALENLHFWAAI-------HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRD-LQQHGIACIYISHKLNEVKA 207
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLVEA 193
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
258-486 |
7.33e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.86 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTawhpvnrhiKR------VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDirnc 331
Cdd:COG4152 1 MLELKGLT---------KRfgdktaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD-SGEVLWDGEPLD---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 332 qQAIAQGIAMVPEDRkrdGIVPVMAVGKNIT-LAALNkftgGISqLDDAAEQkcILESIQQLKVKtSSPDLAIGRLSGGN 410
Cdd:COG4152 67 -PEDRRRIGYLPEER---GLYPKMKVGEQLVyLARLK----GLS-KAEAKRR--ADEWLERLGLG-DRANKKVEELSKGN 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 411 QQKAILARCLLLNPRILILDEPTRGID-IGAKyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKAN 486
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDpVNVE-LLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
277-483 |
8.21e-21 |
|
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: 90.74 E-value: 8.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDirNCQQAIAQGIAMVpedrKRDGIVPVMA 356
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIK-PDSGEITFDGKSYQ--KNIEALRRIGALI----EAPGFYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITLAALnkftggISQLDDAAEQKCI----LESIQQLKVKTsspdlaigrLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:cd03268 89 ARENLRLLAR------LLGIRKKRIDEVLdvvgLKDSAKKKVKG---------FSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 433 TRGID-IGAKyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03268 154 TNGLDpDGIK-ELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
279-483 |
1.06e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 90.43 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKrGEILGIAGLVGAGRTETIQCLFGVW--PGqweGKIYIDGKqvdirnCQQAIAQGIAMVPEDRkRDGIV---- 352
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEkpDG---GTIVLNGT------VLFDSRKKINLPPQQR-KIGLVfqqy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 ---PVMAVGKNITLAAlnKFTGGISQLDDAAEqkcILESIQQLKVKTSSPDlaigRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:cd03297 85 alfPHLNVRENLAFGL--KRKRNREDRISVDE---LLDLLGLDHLLNRYPA----QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 430 DEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
219-496 |
1.16e-20 |
|
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: 95.22 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 219 QHIG-TRDAAGMseddiITMMVGRELTALYPNEP-HTTGDEILRIEHLTAWHPVNRHIkRVNDVSFSLKRGEILGIAGLV 296
Cdd:COG4987 297 QHLGrVRAAARR-----LNELLDAPPAVTEPAEPaPAPGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 297 GAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNC-QQAIAQGIAMVPEDrkrdgiVPVMA--VGKNITLAAlnkftGGI 373
Cdd:COG4987 371 GSGKSTLLALLLRFLDPQ-SGSITLGG--VDLRDLdEDDLRRRIAVVPQR------PHLFDttLRENLRLAR-----PDA 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 374 S--QLDDAAEQKCILESIQQLkvktssP---DLAIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEI 444
Cdd:COG4987 437 TdeELWAALERVGLGDWLAAL------PdglDTWLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 445 YKLINQLVqQGIAVIVISSELPEvLGLSDRVLVMHEGKLKANLINHNLTQEQ 496
Cdd:COG4987 511 LADLLEAL-AGRTVLLITHRLAG-LERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
260-484 |
1.23e-20 |
|
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: 90.01 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 260 RIEHLTawHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAIAqgi 339
Cdd:cd03226 1 RIENIS--FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-SGSILLNGKPIKAKERRKSIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 340 aMVPEDrkrdgivpvmaVGKNI-TLAALNKFTGGISQLDDAAEQK-CILESIQQLKVKTSSPDlaigRLSGGNQQKAILA 417
Cdd:cd03226 75 -YVMQD-----------VDYQLfTDSVREELLLGLKELDAGNEQAeTVLKDLDLYALKERHPL----SLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLK 484
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-218 |
1.33e-20 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 90.82 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVL---CGIYPHGSYEGEIIFAGEEIQASHIRDTE- 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmNDLVPGVRIEGKVLFDGQDIYDKKIDVVEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELALVKeLTVLENIFLGNEIthNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGD--LGL--GQQQLVEIAK 155
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRL--HGIKDKKELDEIVEESLKKAALWDEVKDRLHDsaLGLsgGQQQRLCIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHgIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDG 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-219 |
2.66e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 25 LRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgsYEGEIIFAGEEIqashiRDTE----RKGIAIIHQELALVKElTVLE 100
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFLP---YQGSLKINGIEL-----RELDpeswRKHLSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 101 NIFLGNEithnGIMDYDLMTLRCQkllAQVS--LSISP---DTRVGD----LGLGQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:PRK11174 442 NVLLGNP----DASDEQLQQALEN---AWVSefLPLLPqglDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 172 SL---TEQEtsvlldIIRDLQQ--HGIACIYISHKLNEVKAIsDTICVIRDGQ 219
Cdd:PRK11174 515 SLdahSEQL------VMQALNAasRRQTTLMVTHQLEDLAQW-DQIWVMQDGQ 560
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
254-485 |
2.67e-20 |
|
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: 90.04 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 254 TGDEILRIEHLTawhpvNRHIKRV--NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNC 331
Cdd:COG1127 1 MSEPMIEVRNLT-----KSFGDRVvlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD-SGEILVDGQ--DITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 332 QQAIAQGIamvpedRKRDGIV-------PVMAVGKNITLAaLNKFTGgisqLDDAAEQKCILESIQQLKVKtSSPDLAIG 404
Cdd:COG1127 73 SEKELYEL------RRRIGMLfqggalfDSLTVFENVAFP-LREHTD----LSEAEIRELVLEKLELVGLP-GAADKMPS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:COG1127 141 ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
..
gi 1014292979 484 KA 485
Cdd:COG1127 221 IA 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-484 |
3.20e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 7 MKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGeeiqasHIRdterkgIAII 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP--DSGEVSIPK------GLR------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 87 HQELALVKELTVLENIFLG-----------NEITHN-GIMDYDLMTL-----------------RCQKLLAQVSLSISP- 136
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLDGdaelraleaelEELEAKlAEPDEDLERLaelqeefealggweaeaRAEEILSGLGFPEEDl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 137 DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASlteqetsvlLDI--IRDLQQH----GIACIYISHK---LNEVka 207
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNH---------LDLesIEWLEEFlknyPGTVLVVSHDryfLDRV-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 208 iSDTICVIRDGQ---HIG----------TRDAAGMSE----DDII-----------------TMMVGR-----ELTALYP 248
Cdd:COG0488 216 -ATRILELDRGKltlYPGnysayleqraERLEQEAAAyakqQKKIakeeefirrfrakarkaKQAQSRikaleKLEREEP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 249 -----------NEPHTTGDEILRIEHLTAWHPvNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEG 317
Cdd:COG0488 295 prrdktveirfPPPERLGKKVLELEGLSKSYG-DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD-SG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 318 KIYIdGKQVDIRNCQQaiaQGIAMVPEDRKRDGIVPVMAVGKNIT----LAALNkFTGgisqldDAAEQKcilesiqqlk 393
Cdd:COG0488 371 TVKL-GETVKIGYFDQ---HQEELDPDKTVLDELRDGAPGGTEQEvrgyLGRFL-FSG------DDAFKP---------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 394 vktsspdlaIGRLSGGnqQKA--ILARCLLLNPRILILDEPTRGIDIGAKyEIykLINQLVQ-QGiAVIVIS--SELpeV 468
Cdd:COG0488 430 ---------VGVLSGG--EKArlALAKLLLSPPNVLLLDEPTNHLDIETL-EA--LEEALDDfPG-TVLLVShdRYF--L 492
|
570
....*....|....*.
gi 1014292979 469 LGLSDRVLVMHEGKLK 484
Cdd:COG0488 493 DRVATRILEFEDGGVR 508
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
241-485 |
3.21e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 93.66 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 241 RELTALYPNE------PHTTGDeiLRIEHLTAWHP-VNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPG 313
Cdd:COG4618 309 NELLAAVPAEpermplPRPKGR--LSVENLTVVPPgSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 314 QwEGKIYIDGkqVDIRNC-QQAIAQGIAMVPEDrkrdgivpvmavgknITLaalnkFTGGISQ----LDDAAEQKCIL-- 386
Cdd:COG4618 385 T-AGSVRLDG--ADLSQWdREELGRHIGYLPQD---------------VEL-----FDGTIAEniarFGDADPEKVVAaa 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 387 ------ESIQQLkvktssP---DLAIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ 453
Cdd:COG4618 442 klagvhEMILRL------PdgyDTRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA 515
|
250 260 270
....*....|....*....|....*....|..
gi 1014292979 454 QGIAVIVIsSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:COG4618 516 RGATVVVI-THRPSLLAAVDKLLVLRDGRVQA 546
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-219 |
3.37e-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: 89.19 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGEEIQASHIRDTeRKG 82
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY--KPTSGSVLLDGTDIRQLDPADL-RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENIFLGN-EITHNGIMdyDLMTLRCQKLLAQvslsISP---DTRVGDLGL----GQQQLVEIA 154
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLGApLADDERIL--RAAELAGVTDFVN----KHPnglDLQIGERGRglsgGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 155 KALNKQVRLLILDEPTASL---TEQEtsvlldIIRDLQQ--HGIACIYISHKLNeVKAISDTICVIRDGQ 219
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMdmnSEER------LKERLRQllGDKTLIIITHRPS-LLDLVDRIIVMDSGR 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-225 |
3.75e-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: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGSVK-AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQaSHIRDTERKGIA 84
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP--QKGQILIDGIDIR-DISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKElTVLENIFLGNEIThngimDYDLMTLRCQKLLAQVSLSISP---DTRVGD----LGLGQQQLVEIAKAL 157
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNA-----TDEEVIEAAKEAGAHDFIMKLPngyDTVLGEnggnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 158 NKQVRLLILDEPTASL-TEQETSVLLDIIRdlQQHGIACIYISHKLNEVKAiSDTICVIRDGQHI--GTRD 225
Cdd:cd03254 155 LRDPKILILDEATSNIdTETEKLIQEALEK--LMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIeeGTHD 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-219 |
5.92e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.25 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVL-CGIYPHGsyeGEIIFAGEEI---QA 72
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgCLDKPTS---GTYRVAGQDVatlDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 73 SHIRDTERKGIAIIHQELALVKELTVLEN-----IFLGNEITHNgimdydlmTLRCQKLLAQVSLSISPDTRVGDLGLGQ 147
Cdd:PRK10535 78 DALAQLRREHFGFIFQRYHLLSHLTAAQNvevpaVYAGLERKQR--------LLRAQELLQRLGLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 148 QQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKlNEVKAISDTICVIRDGQ 219
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
278-483 |
6.35e-20 |
|
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: 87.97 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQqaiaqgiamVPEDRKRDGIV----- 352
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-SGTIIIDGLKLTDDKKN---------INELRQKVGMVfqqfn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 --PVMAVGKNITLAALNKFtgGISqlDDAAEQKC--ILESIQQLKVKTSSPdlaiGRLSGGNQQKAILARCLLLNPRILI 428
Cdd:cd03262 87 lfPHLTVLENITLAPIKVK--GMS--KAEAEERAleLLEKVGLADKADAYP----AQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 429 LDEPTRGID---IGakyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03262 159 FDEPTSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
259-483 |
9.02e-20 |
|
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: 88.44 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLT-AWHPvnrHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQ-AIA 336
Cdd:cd03253 1 IEFENVTfAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-SGSILIDG--QDIREVTLdSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEDrkrdgiVPVM--AVGKNITLAALNkftGGISQLDDAAEQKCILESIQQLKVKTSSpdlAIG----RLSGGN 410
Cdd:cd03253 75 RAIGVVPQD------TVLFndTIGYNIRYGRPD---ATDEEVIEAAKAAQIHDKIMRFPDGYDT---IVGerglKLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-219 |
1.02e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.30 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERK 81
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA--GTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 gIAIIHQ--ELALVKElTVLENIFLGNEitHNGImDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:PRK13635 83 -VGMVFQnpDNQFVGA-TVQDDVAFGLE--NIGV-PREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEA-AQADRVIVMNKGE 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-225 |
1.24e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.13 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSV-KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERK-G 82
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTS--GEIFIDGEDIREQDPVELRRKiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIihQELALVKELTVLENIFLGNEITHNGIMDYDlmtLRCQKLLAQVSLSISP--DTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:cd03295 79 YVI--QQIGLFPHMTVEENIALVPKLLKWPKEKIR---ERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDG--QHIGTRD 225
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGeiVQVGTPD 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
259-483 |
1.35e-19 |
|
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: 86.12 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNcqqaiaqg 338
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDG--ADISQ-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 iamVPEDRKRDGIVPVMavgKNITLaalnkFTGGISqlddaaeqkcilESIqqlkvktsspdlaigrLSGGNQQKAILAR 418
Cdd:cd03246 69 ---WDPNELGDHVGYLP---QDDEL-----FSGSIA------------ENI----------------LSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 419 CLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVMHEGKL 483
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-219 |
1.41e-19 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 88.64 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAG-EEIQASHIRDTeR 80
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPT---SGKVTVDGlDTLDEENLWEI-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQ--ELALVKeLTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:TIGR04520 77 KKVGMVFQnpDNQFVG-ATVEDDVAFGLE---NLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEA-VLADRVIVMNKGK 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
255-483 |
1.91e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 255 GDEILRIEHLTAW--HPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQ----WEGKIYIDGKQVDI 328
Cdd:PRK13631 18 DDIILRVKNLYCVfdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKygtiQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 329 RNCQQAIAQGIAMVPEDRKRDGIV---PVM-----AVGKNITLAALNKftgGISQLDDAAEQKCILEsiqQLKVKTSSPD 400
Cdd:PRK13631 98 ELITNPYSKKIKNFKELRRRVSMVfqfPEYqlfkdTIEKDIMFGPVAL---GVKKSEAKKLAKFYLN---KMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 401 LAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHE 480
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
...
gi 1014292979 481 GKL 483
Cdd:PRK13631 252 GKI 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-258 |
2.36e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPHGsyeGEIIFAGEEI--QASHirdtERK 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDA---GSISLCGEPVpsRARH----ARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLENI-----FLGneithngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLlvfgrYFG--------LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIgtrdAAGmSEDDIIT 236
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI----AEG-APHALIE 227
|
250 260
....*....|....*....|..
gi 1014292979 237 MMVGRELTALYPNEPHTTGDEI 258
Cdd:PRK13537 228 SEIGCDVIEIYGPDPVALRDEL 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
277-485 |
2.41e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.74 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNcqqaiaqgiamVPEDRKRDGIV---P 353
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ-SGEIKIDGITISKEN-----------LKEIRKKIGIIfqnP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 354 VmavgknitlaalNKFTGgISQLDDAA---EQKCILESIQQLKVKTSSPDLAIGR--------LSGGNQQKAILARCLLL 422
Cdd:PRK13632 93 D------------NQFIG-ATVEDDIAfglENKKVPPKKMKDIIDDLAKKVGMEDyldkepqnLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVQQGI-AVIVISSELPEVLgLSDRVLVMHEGKLKA 485
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
271-485 |
2.54e-19 |
|
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: 86.49 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 271 NRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQA-IAQGIAMVPEDrkrd 349
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT-SGSVLLDG--TDIRQLDPAdLRRNIGYVPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 350 givPVMAVGK---NITLAALNKFTggiSQLDDAAEQKCILESIQQLKvktSSPDLAIGR----LSGGNQQKAILARCLLL 422
Cdd:cd03245 87 ---VTLFYGTlrdNITLGAPLADD---ERILRAAELAGVTDFVNKHP---NGLDLQIGErgrgLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPeVLGLSDRVLVMHEGKLKA 485
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRIVA 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
256-485 |
2.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.86 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQaI 335
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLTEENVWD-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 AQGIAMVPEDRkrDGIVPVMAVGKNITLAALNKftgGISQLDDAAEQKCILESIQQLKVKTSSPdlaiGRLSGGNQQKAI 415
Cdd:PRK13650 80 RHKIGMVFQNP--DNQFVGATVEDDVAFGLENK---GIPHEEMKERVNEALELVGMQDFKEREP----ARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVlGLSDRVLVMHEGKLKA 485
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
277-485 |
4.16e-19 |
|
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: 85.88 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQAIAQGIAMVPEDRKRDGIvpvMA 356
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT-SGRATVAG--HDVVREPREVRRRIGIVFQDLSVDDE---LT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITL-AALNKFTGgiSQLDDAAEQkcILESIQQLKVKtsspDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:cd03265 90 GWENLYIhARLYGVPG--AERRERIDE--LLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 436 IDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-219 |
4.43e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.75 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPhgsYEGEIIFAGEEIqaSHIRDTER-K 81
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSP---DSGEVRLNGRPL--ADWSPAELaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLENIFLGneITHNGIMDYDLMTLrCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKAL---- 157
Cdd:PRK13548 77 RRAVLPQHSSLSFPFTVEEVVAMG--RAPHGLSRAEDDAL-VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 158 --NKQVRLLILDEPTASL--TEQETsvLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13548 154 epDGPPRWLLLDEPTSALdlAHQHH--VLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
276-486 |
4.44e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.53 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 276 RVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGqwEGKIYIDGKQV-DIRNCQQAI-----AQgiamvpedrkRD 349
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLeAWSAAELARhraylSQ----------QQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 350 GIVPVMAVGKNITL--AALNKFTGGISQLDDAAEQkcilesiQQLKVKTSSPdlaIGRLSGGNQQKAILARCLL-----L 422
Cdd:PRK03695 79 TPPFAMPVFQYLTLhqPDKTRTEAVASALNEVAEA-------LGLDDKLGRS---VNQLSGGEWQRVRLAAVVLqvwpdI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 423 NP--RILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKAN 486
Cdd:PRK03695 149 NPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-241 |
6.20e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITktfGSvkAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKGIA 84
Cdd:PRK10762 258 LKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS--GYVTLDGHEVVTRSPQDGLANGIV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQEL---ALVKELTVLENIFLG--NEITHNGImdydlmTLRCQKLLAQVSLSI--------SPDTRVGDLGLGQQQLV 151
Cdd:PRK10762 331 YISEDRkrdGLVLGMSVKENMSLTalRYFSRAGG------SLKHADEQQAVSDFIrlfniktpSMEQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 152 EIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSE 231
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQ 484
|
250
....*....|
gi 1014292979 232 DDIITMMVGR 241
Cdd:PRK10762 485 EKLMAAAVGK 494
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-219 |
7.69e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 87.55 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 35 LCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGEEIQAshiRDTERKGIAIIHQELALVKELTVLENIFLGNEITHngi 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGfEQPD---SGSIMLDGEDVTN---VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 114 MDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQ-QHG 192
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeQLG 151
|
170 180
....*....|....*....|....*..
gi 1014292979 193 IACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGK 178
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-222 |
1.06e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIfAGEEiQASHIRDTERkgia 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--ETPSAGELL-AGTA-PLAEAREDTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGneithngimdydlmtLR------CQKLLAQVSLSispdTRVGD----LGLGQQQLVEIA 154
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLG---------------LKgqwrdaALQALAAVGLA----DRANEwpaaLSGGQKQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 155 KALNKQVRLLILDEPTA---SLTEQETSVLldIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQhIG 222
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGaldALTRIEMQDL--IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-219 |
1.12e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKV---LCGIYPHGSYEGEIIFAGEEIQASHIRDTERK 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 gIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTlRCQKLLAQVSLSISPDTRV----GDLGLGQQQLVEIAKAL 157
Cdd:PRK14247 84 -VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQE-RVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 158 NKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHgIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
277-484 |
1.34e-18 |
|
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: 84.47 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQ-QAIAQGIAMVPEDrkrdgivPVM 355
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-SGSILIDG--VDISKIGlHDLRSRISIIPQD-------PVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 AVG---KNitLAALNKFTGGisQLDDAAEQKCILESIQQLKVKTSSPDLAIGR-LSGGNQQKAILARCLLLNPRILILDE 431
Cdd:cd03244 90 FSGtirSN--LDPFGEYSDE--ELWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 432 PTRGIDigakYEIYKLINQLVQQGIA---VIVISSELPEVLGlSDRVLVMHEGKLK 484
Cdd:cd03244 166 ATASVD----PETDALIQKTIREAFKdctVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
267-486 |
1.42e-18 |
|
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: 84.69 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 267 WHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPGQweGKIYIDGkqvdirncqqaiaqgiaMVPED 345
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTS--GEVRVAG-----------------LVPWK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 346 RkRDGIVPVMAV--GKNITLA---------ALNKftgGISQLDDAAEQKCILESIQQLKVkTSSPDLAIGRLSGGNQQKA 414
Cdd:cd03267 88 R-RKKFLRRIGVvfGQKTQLWwdlpvidsfYLLA---AIYDLPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKAN 486
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
259-483 |
1.57e-18 |
|
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: 84.54 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPvNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQ----WEGKIYIDGKqvDIRNCQQA 334
Cdd:cd03260 1 IELRDLNVYYG-DKHA--LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapDEGEVLLDGK--DIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 335 iaqgiamVPEDRKRDGIV---PV---MAVGKNITLAAlnKFTG--GISQLDDAAEQkcILESIQqL--KVKTsspDLAIG 404
Cdd:cd03260 76 -------VLELRRRVGMVfqkPNpfpGSIYDNVAYGL--RLHGikLKEELDERVEE--ALRKAA-LwdEVKD---RLHAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-219 |
2.03e-18 |
|
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: 82.65 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKA--IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHiRDTERKG 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS--GRVRLDGADISQWD-PNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENIFLGneithngimdydlmtlrcqkllaqvslsispdtrvgdlglGQQQLVEIAKALNKQVR 162
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENILSG----------------------------------------GQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 163 LLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLnEVKAISDTICVIRDGQ 219
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-219 |
2.19e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTERKgIA 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS--GTVFLGDKPISMLSSRQLARR-LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNE--ITHNGIM-DYDLMtlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRSpwLSLWGRLsAEDNA--RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 162 RLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
248-482 |
2.44e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.37 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 248 PNEPHTTGDEILRIEHLT-AWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQV 326
Cdd:PRK10261 2 PHSDELDARDVLAVENLNiAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-QAGGLVQCDKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 327 DIRNCQ------QAIAQ-------GIAMVPEDrKRDGIVPVMAVGKNItlAALNKFTGGISQLDDAAEQKCILEsiqQLK 393
Cdd:PRK10261 81 RRRSRQvielseQSAAQmrhvrgaDMAMIFQE-PMTSLNPVFTVGEQI--AESIRLHQGASREEAMVEAKRMLD---QVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 394 VKTSSPDLA--IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLG 470
Cdd:PRK10261 155 IPEAQTILSryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAE 234
|
250
....*....|..
gi 1014292979 471 LSDRVLVMHEGK 482
Cdd:PRK10261 235 IADRVLVMYQGE 246
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-192 |
2.47e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.85 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 2 PYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKvlCGIYPHGSYEGEIIFAGEEIQASHIRD---- 77
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLR--CINLLETPDSGEIRVGGEEIRLKPDRDgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 -TERKGIAIIHQELALV-------KELTVLENIF------LGneithngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDL 143
Cdd:COG4598 84 pADRRQLQRIRTRLGMVfqsfnlwSHMTVLENVIeapvhvLG--------RPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1014292979 144 GLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHG 192
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEG 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
258-485 |
2.60e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 84.31 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLtawhpVNRHIKR--VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGqwEGKIYIDGKqvDI------ 328
Cdd:COG1137 3 TLEAENL-----VKSYGKRtvVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlVKPD--SGRIFLDGE--DIthlpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 329 -RncqqaiAQ-GIAMVPED----RKrdgivpvMAVGKNItLAALnKFTGgisqlDDAAEQKCILES-IQQL---KVKTSs 398
Cdd:COG1137 74 kR------ARlGIGYLPQEasifRK-------LTVEDNI-LAVL-ELRK-----LSKKEREERLEElLEEFgitHLRKS- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 399 pdLAIgRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVM 478
Cdd:COG1137 133 --KAY-SLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYII 209
|
....*..
gi 1014292979 479 HEGKLKA 485
Cdd:COG1137 210 SEGKVLA 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-218 |
3.27e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKA--IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQASHIRDTeRK 81
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI--EKVKSGEIFYNNQAITDDNFEKL-RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELalvkeltvlENIFLGNEITH-------NGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIA 154
Cdd:PRK13648 84 HIGIVFQNP---------DNQFVGSIVKYdvafgleNHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 155 KALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQ-HGIACIYISHKLNEVkAISDTICVIRDG 218
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-219 |
3.71e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.62 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPHGsyeGEIIFAGEEIQASHIRD--T 78
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTS---GRVLVDGQDLTALSEKElrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 ERKGIAIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAG---TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
277-483 |
4.42e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.54 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwPGQWEGKIYIDGKQVDIRNCQQaiaQGIAMVPEDRkrdGIVPVMA 356
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDGEDVTHRSIQQ---RDICMVFQSY---ALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITLaalnkftgGISQLDDAAEqkcilESIQQLKVKTSSPDLA------IGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK11432 95 LGENVGY--------GLKMLGVPKE-----ERKQRVKEALELVDLAgfedryVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-219 |
4.87e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.13 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQA---SHIRD 77
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTS--GSVLVDGVDLTAlseRELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 tERKGIAIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:COG1135 80 -ARRKIGMIFQHFNLLSSRTVAENVALPLEIAG---VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 158 NKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-219 |
4.95e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 83.65 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVL-------CGIYPHGSYEgeiIFAGEEI--QASHI 75
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGDIT---IDTARSLsqQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 76 RDTeRKGIAIIHQELALVKELTVLENIFLGNEITHNgiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAK 155
Cdd:PRK11264 81 RQL-RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
277-483 |
5.41e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.09 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQW--EGKIYIDGKQVDIRNCQQAIAqgiaMVPEDrkrDGIVPV 354
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttSGQILFNGQPRKPDQFQKCVA----YVRQD---DILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 355 MAVGKNITLAAL----NKFTGGISQ--LDDAAEQKCILESIQQLKVKTsspdlaigrLSGGNQQKAILARCLLLNPRILI 428
Cdd:cd03234 96 LTVRETLTYTAIlrlpRKSSDAIRKkrVEDVLLRDLALTRIGGNLVKG---------ISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 429 LDEPTRGIDIGAKYEIYKLINQLVQQGIAVIV-ISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
277-483 |
6.32e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.76 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNC-QQAIAQGIAMVPEDrkrdgiVPVM 355
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDG--VDIRDLtLESLRRQIGVVPQD------TFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 A--VGKNITLAALNkftggIS--QLDDAAEQKCILESIQQLkvktssP---DLAIG----RLSGGNQQK-AIlARCLLLN 423
Cdd:COG1132 427 SgtIRENIRYGRPD-----ATdeEVEEAAKAAQAHEFIEAL------PdgyDTVVGergvNLSGGQRQRiAI-ARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-219 |
6.43e-18 |
|
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: 83.05 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS--VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTeRKG 82
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDS--GRILIDGHDVRDYTLASL-RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENIFLGN-EITHNGIMDydlmtlRCQKLLAQVSLSISP---DTRVGDLGL----GQQQLVEIA 154
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGRpGATREEVEE------AARAANAHEFIMELPegyDTVIGERGVklsgGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 155 KALNKQVRLLILDEPTASL-TEQETSVlLDIIRDLQQHGIAcIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03251 151 RALLKDPPILILDEATSALdTESERLV-QAALERLMKNRTT-FVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
259-502 |
7.39e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.24 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTawhpVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDiRNCQQAIAQ 337
Cdd:COG4559 2 LEAENLS----VRLGGRTLlDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNGRPLA-AWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEDrkrdgivpvmavgknitlAALN-KFT-------GGISQLDDAAEQKCILESIQQLkvkTSSPDLAiGR---- 405
Cdd:COG4559 76 RRAVLPQH------------------SSLAfPFTveevvalGRAPHGSSAAQDRQIVREALAL---VGLAHLA-GRsyqt 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLL-------LNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVM 478
Cdd:COG4559 134 LSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLL 213
|
250 260
....*....|....*....|....
gi 1014292979 479 HEGKLKAnlinhNLTQEQVMEAAL 502
Cdd:COG4559 214 HQGRLVA-----QGTPEEVLTDEL 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
7.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVK---AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRD 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES--GQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERKgIAIIHQ--ELALVKElTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAK 155
Cdd:PRK13650 79 IRHK-IGMVFQnpDNQFVGA-TVEDDVAFGLE---NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-219 |
7.95e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 86.31 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 22 NVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQA-SHirDTERKGIAIIHQELALVKElTVLE 100
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP--LTEGEIRLDGRPLSSlSH--SVLRQGVAMVQQDPVVLAD-TFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 101 NIFLGNEITHNGIMDYdLMTLRcqklLAQVSLSIsPD---TRVGD----LGLGQQQLVEIAKALNKQVRLLILDEPTASL 173
Cdd:PRK10790 434 NVTLGRDISEEQVWQA-LETVQ----LAELARSL-PDglyTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1014292979 174 ---TEQETSVLLDIIRdlqQHgIACIYISHKLNE-VKAisDTICVIRDGQ 219
Cdd:PRK10790 508 dsgTEQAIQQALAAVR---EH-TTLVVIAHRLSTiVEA--DTILVLHRGQ 551
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
277-497 |
8.67e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRncQQAIAQGIAMVPEdrkRDGIVPVMA 356
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-AGKITVLGVPVPAR--ARLARARIGVVPQ---FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNitLAALNKFTGGisqldDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:PRK13536 131 VREN--LLVFGRYFGM-----STREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 437 DIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQEQV 497
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-200 |
8.84e-18 |
|
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: 82.48 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIyPHGSyEGEIIFAGEEIQA------S 73
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPT-SGTVRLAGQDLFAldedarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 74 HIRdteRKGIAIIHQELALVKELTVLENIFLGNEITHNGimdyDLMTlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEI 153
Cdd:COG4181 86 RLR---ARHVGFVFQSFQLLPTLTALENVMLPLELAGRR----DARA-RARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 154 AKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISH 200
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTH 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
277-483 |
9.04e-18 |
|
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: 83.08 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGqwEGKIYIDGKQVDIRNCQQAIA---QGIAMVPEDRkrdGIV 352
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEPT--SGKVLIDGQDIAAMSRKELRElrrKKISMVFQSF---ALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 PVMAVGKNITlaalnkFTGGISQLDDAAEQKCILESIQQLKVKTSSpDLAIGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:cd03294 115 PHRTVLENVA------FGLEVQGVPRAEREERAAEALELVGLEGWE-HKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 433 TRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
277-486 |
1.12e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.73 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW-PGQweGKIYIDGKQVDIRNCQQaiaqgIAmvpedrkRDGIVPV- 354
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG--GTILLRGQHIEGLPGHQ-----IA-------RMGVVRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 355 --------MAVGKNITLAA---LNkfTGGISQLDDA-----AEQKCILESIQQLKvKTSSPDLA---IGRLSGGNQQKAI 415
Cdd:PRK11300 87 qhvrlfreMTVIENLLVAQhqqLK--TGLFSGLLKTpafrrAESEALDRAATWLE-RVGLLEHAnrqAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKAN 486
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
259-483 |
1.20e-17 |
|
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: 81.77 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLT-AWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQQAiaq 337
Cdd:cd03255 1 IELKNLSkTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVRVDGT--DISKLSEK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 giAMVPEDRKRDGIV-------PVMAVGKNITLAALNKFTGGISQLDDAAEqkcILESIQQLKVKTSSPdlaiGRLSGGN 410
Cdd:cd03255 75 --ELAAFRRRHIGFVfqsfnllPDLTALENVELPLLLAGVPKKERRERAEE---LLERVGLGDRLNHYP----SELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSElPEVLGLSDRVLVMHEGKL 483
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-219 |
1.22e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF--GSVKA--IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGE---EIQASHIR 76
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS--GDVIFNGQpmsKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 77 DTERKGIAIIHQELALVKELTVLENIFLGNEIthnGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLI---GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTIcVIRDGQ 219
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGR 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
275-505 |
1.25e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 275 KRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAIAQGIAMVPEDR---KR--- 348
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-AGNIIIDDEDISLLPLHARARRGIGYLPQEAsifRRlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 349 -DGIVPVMAVGKNITLaalnkftggiSQLDDAAEQkcILESIQQLKVKTSspdlaIGR-LSGGNQQKAILARCLLLNPRI 426
Cdd:PRK10895 96 yDNLMAVLQIRDDLSA----------EQREDRANE--LMEEFHIEHLRDS-----MGQsLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 427 LILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGklkaNLINHN-----LTQEQVMEAA 501
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG----HLIAHGtpteiLQDEHVKRVY 234
|
....
gi 1014292979 502 LRSE 505
Cdd:PRK10895 235 LGED 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
274-483 |
1.39e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 274 IKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwPGQWEGKIYIDGKqvDIRNCQQA--IAQGIAMVPEDRKrdgI 351
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGK--DITDWQTAkiMREAVAIVPEGRR---V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 352 VPVMAVGKNItlaALNKFTGGISQLDDAAEQKC-ILESIQQLKVKTSspdlaiGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK11614 92 FSRMTVEENL---AMGGFFAERDQFQERIKWVYeLFPRLHERRIQRA------GTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-218 |
1.41e-17 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 81.69 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKN-----ITKTFGSvKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLcGIYPHGSyEGEIIFAGEEIQA---SHI 75
Cdd:NF038007 1 MLNMQNaekcyITKTIKT-KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNII-GMFDSLD-SGSLTLAGKEVTNlsySQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 76 RDTERKGIAIIHQELALVKELTVLENIFLgnEITHNGIMDYDLMTlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAK 155
Cdd:NF038007 78 IILRRELIGYIFQSFNLIPHLSIFDNVAL--PLKYRGVAKKERIE-RVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKlNEVKAISDTICVIRDG 218
Cdd:NF038007 155 AMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
256-483 |
1.46e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIRNCQQaI 335
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-EFEGKVKIDGELLTAENVWN-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 AQGIAMVPEDRkrDGIVPVMAVGKNITLAALNKftgGISQLDDAAEQKCILESIQQLKVKTSSPdlaiGRLSGGNQQKAI 415
Cdd:PRK13642 80 RRKIGMVFQNP--DNQFVGATVEDDVAFGMENQ---GIPREEMIKRVDEALLAVNMLDFKTREP----ARLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-226 |
1.54e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.60 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 16 SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEI---QASHIRDTeRKGIAIIHQE-LA 91
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK--ATDGEVAWLGKDLlgmKDDEWRAV-RSDIQMIFQDpLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 92 -LVKELTVLEnIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRV-GDLGLGQQQLVEIAKALNKQVRLLILDEP 169
Cdd:PRK15079 110 sLNPRMTIGE-IIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 170 TASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDA 226
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHavELGTYDE 248
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
1.56e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF--GSV---KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTE 79
Cdd:COG1101 2 LELKNLSKTFnpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP--PDSGSILIDGKDV--TKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 R-KGIAIIHQELAL--VKELTVLENIF----------LGNEITHNGIMDYdlmtlrcQKLLAQVSLSIS--PDTRVGDLG 144
Cdd:COG1101 78 RaKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrrgLRRGLTKKRRELF-------RELLATLGLGLEnrLDTKVGLLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 145 LGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEvkAIS--DTICVIRDGQ-- 219
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQ--ALDygNRLIMMHEGRii 228
|
250 260
....*....|....*....|....*....
gi 1014292979 220 -HIGTRDAAGMSEDDIITM---MVGRELT 244
Cdd:COG1101 229 lDVSGEEKKKLTVEDLLELfeeIRGEELA 257
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-218 |
1.85e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKvlCGIYPHGSYEGEIIFAGEEIQAshIRDTE----- 79
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGSIVVNGQTINL--VRDKDgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 ---------RKGIAIIHQELALVKELTVLENIfLGNEITHNGIMDYDLMTlRCQKLLAQVSLSISPDTRV-GDLGLGQQQ 149
Cdd:PRK10619 82 adknqlrllRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQEARE-RAVKYLAKVGIDERAQGKYpVHLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 150 LVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
259-478 |
2.17e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.98 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLT-AWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIRNCQqaiaq 337
Cdd:cd03293 1 LEVRNVSkTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-PTSGEVLVDGEPVTGPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 gIAMVPEDrkrDGIVPVMAVGKNITLAALNKFTGGISQLDDAAEqkcILESIQQLKVKTSSPdlaiGRLSGGNQQKAILA 417
Cdd:cd03293 75 -RGYVFQQ---DALLPWLTVLDNVALGLELQGVPKAEARERAEE---LLELVGLSGFENAYP----HQLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVM 478
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
279-485 |
3.04e-17 |
|
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: 83.23 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvdirnCQQAIAQGIAMVPEDRkRDGIV------ 352
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD-SGRIRLGGE------VLQDSARGIFLPPHRR-RIGYVfqearl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 -PVMAVGKNITLAAlnKFTGGIS---QLDDAAEQkcilesiqqlkvktsspdLAIG--------RLSGGNQQKAILARCL 420
Cdd:COG4148 89 fPHLSVRGNLLYGR--KRAPRAErriSFDEVVEL------------------LGIGhlldrrpaTLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 421 LLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-218 |
3.12e-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: 80.84 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 16 SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPHgsyEGEIIFAGEEIQASHIRDTERKGIaIIHQELALVK 94
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPT---SGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 ELTVLENIFLGNEIthngimdYDLMTLRCQKLLAQVS--LSISP--DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:cd03267 109 DLPVIDSFYLLAAI-------YDLPPARFKKRLDELSelLDLEEllDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1014292979 171 ASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-219 |
3.39e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTE-RKGIAIIHQ--ELALVK 94
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS--GKIIIDGVDITDKKVKLSDiRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 ElTVLENIFLGneITHNGIMDYDLMTlRCQKLLAQVSLSISP--DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:PRK13637 99 E-TIEKDIAFG--PINLGLSEEEIEN-RVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 173 LTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13637 175 LDPKGRDEILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-212 |
3.73e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGEEIqASHIRDTERKG 82
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASlISPT---SGTLLFEGEDI-STLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENIFLGNEITHNGImDYDLMtlrcQKLLAQVSLsisPDT----RVGDLGLGQQQLVEIAKALN 158
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFPWQIRNQQP-DPAIF----LDDLERFAL---PDTiltkNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDII-RDLQQHGIACIYISHKLNEVKAISDTI 212
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-219 |
4.68e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.99 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF---------GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASH 74
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS--GELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 75 IRDTERKgIAIIHQELAlvKELTVLENI--FLGNEITHNGIMDYDLMTLRCQKLLAQVSL-----SISPDTrvgdLGLGQ 147
Cdd:PRK15112 82 YSYRSQR-IRMIFQDPS--TSLNPRQRIsqILDFPLRLNTDLEPEQREKQIIETLRQVGLlpdhaSYYPHM----LAPGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 148 QQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
275-482 |
5.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 275 KRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNcqqaiaQGIAMvPEDRKRDGIV-- 352
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-SGKIIIDG--VDITD------KKVKL-SDIRKKVGLVfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 -PVM-----AVGKNITLAALNKftgGISqlDDAAEQKcILESIQQLKV-----KTSSPdlaiGRLSGGNQQKAILARCLL 421
Cdd:PRK13637 91 yPEYqlfeeTIEKDIAFGPINL---GLS--EEEIENR-VKRAMNIVGLdyedyKDKSP----FELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 422 LNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
277-483 |
5.88e-17 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.13 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQWEGKIYIDGKQVDIRNcqqaIAQGIAMVPEDrkrDGIVPVM 355
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVLINGRPLDKRS----FRKIIGYVPQD---DILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 AVGKNITLAAlnkftggisqlddaaeqkcilesiqQLKvktsspdlaigRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:cd03213 98 TVRETLMFAA-------------------------KLR-----------GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 436 IDIGAKYEIYKLINQLVQQGIAVIVI----SSelpEVLGLSDRVLVMHEGKL 483
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRV 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-232 |
5.99e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.70 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF-----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDT 78
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 ER----KGIAIIHQELALVKELTVLENIF--LGNEITHNGIMDYDLMTLRCQKLLAQVSLSI---SPDTrvgdLGLGQQQ 149
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAVITLKMVGFDEEKAEEIldkYPDE----LSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 150 LVEIAKALNKQVRLLILDEPTASLTE-QETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAG 228
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
....
gi 1014292979 229 MSED 232
Cdd:TIGR03269 515 IVEE 518
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-219 |
6.74e-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: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPyLLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgsyEGEII------FAGEEI 70
Cdd:COG4170 1 MP-LLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK----DNWHVtadrfrWNGIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 71 QASHIRDTER---KGIAIIHQElalvkELTVLE-NIFLGNEITHNgIMDYDLMTLRCQKLLAQVSLSISPDTRVG----- 141
Cdd:COG4170 76 LKLSPRERRKiigREIAMIFQE-----PSSCLDpSAKIGDQLIEA-IPSWTFKGKWWQRFKWRKKRAIELLHRVGikdhk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 142 --------DLGLGQQQLVEIAKALNKQVRLLILDEPTASLteqETSVLLDIIRDL----QQHGIACIYISHKLNEVKAIS 209
Cdd:COG4170 150 dimnsyphELTEGECQKVMIAMAIANQPRLLIADEPTNAM---ESTTQAQIFRLLarlnQLQGTSILLISHDLESISQWA 226
|
250
....*....|
gi 1014292979 210 DTICVIRDGQ 219
Cdd:COG4170 227 DTITVLYCGQ 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
259-482 |
6.82e-17 |
|
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: 79.92 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHikRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQV--DIRNCQQAIA 336
Cdd:cd03256 1 IEVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGSVLIDGTDInkLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEDRkrdGIVPVMAVGKNI---TLAALNKFTGGISQLDDAAEQKCI--LESIQQLkvktsspDLAIGR---LSG 408
Cdd:cd03256 78 RQIGMIFQQF---NLIERLSVLENVlsgRLGRRSTWRSLFGLFPKEEKQRALaaLERVGLL-------DKAYQRadqLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-219 |
8.42e-17 |
|
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: 79.58 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITktFG---SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGEEIQASHIrDTERK 81
Cdd:cd03253 1 IEFENVT--FAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY--DVSSGSILIDGQDIREVTL-DSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKElTVLENIFLGNE--------------ITHNGIMdydlmtlrcqkllaqvSLSISPDTRVGDLGL-- 145
Cdd:cd03253 76 AIGVVPQDTVLFND-TIGYNIRYGRPdatdeevieaakaaQIHDKIM----------------RFPDGYDTIVGERGLkl 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 146 --GQQQLVEIAKALNKQVRLLILDEPTASL---TEQEtsvLLDIIRDLQQhGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03253 139 sgGEKQRVAIARAILKNPPILLLDEATSALdthTERE---IQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
277-483 |
9.69e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.59 E-value: 9.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGvWPGQWEGKIYIDGKQvdirncqqaiaqgIAMVPEDRKRDGIV---- 352
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-FETPTSGEILLDGKD-------------ITNLPPHKRPVNTVfqny 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 ---PVMAVGKNITlaalnkFTGGISQLDDAAEQKCILESIQQLKVKtsspDLA---IGRLSGGNQQKAILARCLLLNPRI 426
Cdd:cd03300 82 alfPHLTVFENIA------FGLRLKKLPKAEIKERVAEALDLVQLE----GYAnrkPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 427 LILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
266-512 |
1.04e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 80.23 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 266 AWHPVnrhikrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGK---QVDiRNCQQAIAQGIAMV 342
Cdd:TIGR02769 22 QRAPV------LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA-QGTVSFRGQdlyQLD-RKQRRAFRRDVQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 343 PEDRKrDGIVPVMAVGKNITLAALNkftggISQLDDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLL 422
Cdd:TIGR02769 94 FQDSP-SAVNPRMTVRQIIGEPLRH-----LTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL-----KANLINHNLTQEQ 496
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIveecdVAQLLSFKHPAGR 247
|
250
....*....|....*.
gi 1014292979 497 VMEAALRSEHHVEKQS 512
Cdd:TIGR02769 248 NLQSAVLPEHPVRRSI 263
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
246-478 |
1.21e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 82.72 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 246 LYPNEPHTTGDEI-LRIEHLTAWHPVNRhiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGqwEGKIYIDG 323
Cdd:TIGR02857 308 LAGKAPVTAAPASsLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPT--EGSIAVNG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 324 KQVDIRNcQQAIAQGIAMVPEdrkrdgiVPVM---AVGKNITLAALNkftGGISQLDDAAEQKCILESIQQLKVKTSSPd 400
Cdd:TIGR02857 384 VPLADAD-ADSWRDQIAWVPQ-------HPFLfagTIAENIRLARPD---ASDAEIREALERAGLDEFVAALPQGLDTP- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 401 laIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSElPEVLGLSDRVL 476
Cdd:TIGR02857 452 --IGeggaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIV 527
|
..
gi 1014292979 477 VM 478
Cdd:TIGR02857 528 VL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-219 |
1.86e-16 |
|
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: 78.30 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTeRKG 82
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE--LSSGSILIDGVDISKIGLHDL-RSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQElALVKELTVLENIFLGNEIThngimDYDLM--TLRCQKLLAQVSLSISPDTRVGDLGL----GQQQLVEIAKA 156
Cdd:cd03244 80 ISIIPQD-PVLFSGTIRSNLDPFGEYS-----DEELWqaLERVGLKEFVESLPGGLDTVVEEGGEnlsvGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDlQQHGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-219 |
2.19e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 77.92 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 25 LRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShirDTERKGIAIIHQELALVKELTVLENIFL 104
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLINGVDVTAA---PPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 105 G-------NEITHNGImdydlmtlrcQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQE 177
Cdd:cd03298 94 GlspglklTAEDRQAI----------EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1014292979 178 TSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03298 164 RAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
257-485 |
3.16e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.90 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 257 EILRIEHLTAWHPvNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNcqqaia 336
Cdd:PRK13635 4 EIIRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGMVLSEET------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 qgiamVPEDRKRDGIV---PVmavgknitlaalNKFTGGISQlDDAA------------EQKCILESIQQLKVkTSSPDL 401
Cdd:PRK13635 76 -----VWDVRRQVGMVfqnPD------------NQFVGATVQ-DDVAfglenigvpreeMVERVDQALRQVGM-EDFLNR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 402 AIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGlSDRVLVMHE 480
Cdd:PRK13635 137 EPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVIVMNK 215
|
....*
gi 1014292979 481 GKLKA 485
Cdd:PRK13635 216 GEILE 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
281-482 |
4.14e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.49 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 281 SFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQweGKIYIDGKQVDirncQQAIAQ-GIAMVPEDrkrDGIVPVMAVG 358
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDS--GRILWNGQDLT----ALPPAErPVSMLFQE---NNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 359 KNITLA---ALNKFTGGISQLDDAAEQKCILESIQQLkvktssPdlaiGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:COG3840 90 QNIGLGlrpGLKLTAEQRAQVEQALERVGLAGLLDRL------P----GQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 436 IDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:COG3840 160 LDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-207 |
4.22e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.14 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHG-SYEGEIIFAGEEIQAshiRDTERKGI 83
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGRRLTA---LPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLG--NEITHNgimdydLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFAlpPTIGRA------QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 162 RLLILDEPTASLTEQetsvLLDIIRD-----LQQHGIACIYISHKLNEVKA 207
Cdd:COG4136 153 RALLLDEPFSKLDAA----LRAQFREfvfeqIRQRGIPALLVTHDEEDAPA 199
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-200 |
4.80e-16 |
|
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: 76.31 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 15 GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHGsyeGEIIFAGEEIqashirDTERKGIAIIHQELALV 93
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQS---GAVLIDGEPL------DYSRKGLLERRQRVGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 KE--------LTVLENIFLGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLI 165
Cdd:TIGR01166 74 FQdpddqlfaADVDQDVAFG---PLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1014292979 166 LDEPTASLTEQETSVLLDIIRDLQQHGIACIYISH 200
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-219 |
5.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.30 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVK--AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHGSYEGEIIFAGEEIQASHIRDT-ER 80
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNPNSKITVDGITLTAKTVWDIrEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKElTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK13640 86 VGIVFQNPDNQFVGA-TVGDDVAFGLE---NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
259-484 |
5.30e-16 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 76.85 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAwhpVNRHIKRVNDVSFSLKRGeILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGkqVDIRNCQQAIAQG 338
Cdd:cd03264 1 LQLENLTK---RYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP-PSSGTIRIDG--QDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 IAMVPEDrkrdgivpvMAVGKNIT-------LAALNkftgGISQLDDAAEQKCILESIQQLKVKtsspDLAIGRLSGGNQ 411
Cdd:cd03264 74 IGYLPQE---------FGVYPNFTvrefldyIAWLK----GIPSKEVKARVDEVLELVNLGDRA----KKKIGSLSGGMR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 412 QKAILARCLLLNPRILILDEPTRGIDIGakyEIYKLINQLVQQGIAVIVI-SSELPE-VLGLSDRVLVMHEGKLK 484
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLDPE---ERIRFRNLLSELGEDRIVIlSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
5.62e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.11 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGSVK--AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGEEIQASHIRDTeRKG 82
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQ---SGEIKIDGITISKENLKEI-RKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQ--ELALVKeLTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK13632 85 IGIIFQnpDNQFIG-ATVEDDIAFGLE---NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQHGIAC-IYISHKLNEVkAISDTICVIRDGQHI 221
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTlISITHDMDEA-ILADKVIVFSEGKLI 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
5.82e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFA---GEEIQASHIRD 77
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA--GEVHYRmrdGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERKGIA-----IIHQELA--LVKELTVLENIflGNEITHNGIMDYDlmTLRCQKL--LAQVslSISPDtRVGDL----- 143
Cdd:PRK11701 81 AERRRLLrtewgFVHQHPRdgLRMQVSAGGNI--GERLMAVGARHYG--DIRATAGdwLERV--EIDAA-RIDDLpttfs 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 144 GlGQQQLVEIAKALNKQVRLLILDEPTASLteqETSV---LLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11701 154 G-GMQQRLQIARNLVTHPRLVFMDEPTGGL---DVSVqarLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-207 |
5.97e-16 |
|
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: 76.38 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqaSHIRDTERKGIA 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP--PLAGRVLLNGGPL--DFQRDSIARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENI-FLGNeithngimdyDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03231 77 YLGHAPGIKTTLSVLENLrFWHA----------DHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRD-LQQHGIACIYISHKLNEVKA 207
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMAGhCARGGMVVLTTHQDLGLSEA 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
258-483 |
6.24e-16 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 77.24 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLT-AWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPGqwEGKIYIDGKQV-DIRNCQ-Q 333
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPT--SGSVLVDGTDLtLLSGKElR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 334 AIAQGIAMVPE-----DRKrdgivpvmAVGKNITLAaLNkftggISQLDDAAEQKCILESIQQLKVKTSSpDLAIGRLSG 408
Cdd:cd03258 79 KARRRIGMIFQhfnllSSR--------TVFENVALP-LE-----IAGVPKAEIEERVLELLELVGLEDKA-DAYPAQLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-170 |
6.62e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.94 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIrDTeRKGIAI 85
Cdd:NF033858 268 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP--ASEGEAWLFGQPVDAGDI-AT-RRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 86 IHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLI 165
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARLFH---LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
....*
gi 1014292979 166 LDEPT 170
Cdd:NF033858 421 LDEPT 425
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-224 |
6.74e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPHGsyeGEIIFAGEEIQA---SHIRDTeRKGIAIIHQEL--ALV 93
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQ---GNVSWRGEPLAKlnrAQRKAF-RRDIQMVFQDSisAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 KELTVLENIflGNEITHNGIMDYDLMTLRCQKLLAQVSLSIS-PDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:PRK10419 104 PRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 173 LTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQHIGTR 224
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
6.77e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.81 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF--GSVkAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIqashirDTERK 81
Cdd:PRK13639 1 ILETRDLKYSYpdGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS--GEVLIKGEPI------KYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKE--------LTVLENIFLGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEI 153
Cdd:PRK13639 72 SLLEVRKTVGIVFQnpddqlfaPTVEEDVAFG---PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 154 AKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGT 223
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
279-484 |
6.79e-16 |
|
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: 76.30 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQ-QAIAQGIAMVPEDrkrdgivPVMav 357
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-EGKIEIDG--IDISTIPlEDLRSSLTIIPQD-------PTL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 358 gknitlaalnkFTGGI-SQLD--DAAEQKCILESiqqLKVKTSSPDLaigrlSGGNQQKAILARCLLLNPRILILDEPTR 434
Cdd:cd03369 94 -----------FSGTIrSNLDpfDEYSDEEIYGA---LRVSEGGLNL-----SQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1014292979 435 GIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGLsDRVLVMHEGKLK 484
Cdd:cd03369 155 SIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
277-505 |
9.08e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwpgqwegkIYIDGKQvdIRNCQQAIAQgiaMVPEDRKRDGIVPVM- 355
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL--------THPDAGS--ISLCGEPVPS---RARHARQRVGVVPQFd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 ------AVGKNitLAALNKFTGgISqlddAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK13537 90 nldpdfTVREN--LLVFGRYFG-LS----AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 430 DEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQEQ----VME------ 499
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcdVIEiygpdp 242
|
....*.
gi 1014292979 500 AALRSE 505
Cdd:PRK13537 243 VALRDE 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-221 |
9.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAshirDTERKGIAIIHQELALVK--- 94
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS--GTITIAGYHITP----ETGNKNLKKLRKKVSLVFqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 -----ELTVLENIFLGNEitHNGIMDyDLMTLRCQKLLAQVSLSIS-PDTRVGDLGLGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK13641 95 eaqlfENTVLKDVEFGPK--NFGFSE-DEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 169 PTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
277-483 |
1.02e-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: 76.14 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVdirNCQQAIAQGIAMVPEDRkrdGIVPVMA 356
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGGRDV---TDLPPKDRDIAMVFQNY---ALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITLA-ALNKFTGGI--SQLDDAAEqkcILESIQQLKVKTSspdlaigRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:cd03301 89 VYDNIAFGlKLRKVPKDEidERVREVAE---LLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 434 RGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-225 |
1.49e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.68 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIqaSHIRDTE--- 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI--ERPSAGKIWFSGHDI--TRLKNREvpf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 -RKGIAIIHQELALVKELTVLENIFLGNEITHNGIMDydlMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK10908 77 lRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDD---IRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRD 225
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-221 |
1.52e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.35 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVL---CGIYPHGSYEGEIIFAGEEIQASHIRDTE- 79
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVTITGSIVYNGHNIYSPRTDTVDl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELALVKeLTVLENIFLGNEIthNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGD--LGL--GQQQLVEIAK 155
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRL--KGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsaLGLsgGQQQRVCIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDLqQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-194 |
1.58e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTerkgIA 84
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP--PAAGTIKLDGGDIDDPDVAEA----CH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 II-HQElALVKELTVLENI-----FLGNEIThnGIMDydlmtlrcqkLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK13539 77 YLgHRN-AMKPALTVAENLefwaaFLGGEEL--DIAA----------ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLV 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRD-LQQHGIA 194
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIV 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
1.73e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.77 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 3 YLLEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTeRK 81
Cdd:PRK13652 2 HLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS--GSVLIRGEPITKENIREV-RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELA-LVKELTVLENIFLGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK13652 79 FVGLVFQNPDdQIFSPTVEQDIAFG---PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHIG 222
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
254-483 |
2.07e-15 |
|
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: 78.57 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 254 TGDEILRIEHLTAWHPVNRHIKR-VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQW---EGKIYIDGKqvDIR 329
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEaVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpSGSILFDGQ--DLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 330 NCQQAIAQGIamvpedRKRD-GIV---------PVMAVGKNI--TLAALNKFTGgisqldDAAEQKCI--LEsiqqlKVK 395
Cdd:COG4172 80 GLSERELRRI------RGNRiAMIfqepmtslnPLHTIGKQIaeVLRLHRGLSG------AAARARALelLE-----RVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 396 TSSPDLAIGR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLG 470
Cdd:COG4172 143 IPDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRR 222
|
250
....*....|...
gi 1014292979 471 LSDRVLVMHEGKL 483
Cdd:COG4172 223 FADRVAVMRQGEI 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-219 |
2.63e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 21 DNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQAShiRDTerkgiaiIHQEL------ALVK 94
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR--PDAGEVLWQGEPIRRQ--RDE-------YHQDLlylghqPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 -ELTVLENI-FLGneiTHNGIMDYDlmtlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:PRK13538 87 tELTALENLrFYQ---RLHGPGDDE----ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 173 LTEQETSVLLDIIRD-LQQHGIAcIYISHKlnEVKAISDTICVIRDGQ 219
Cdd:PRK13538 160 IDKQGVARLEALLAQhAEQGGMV-ILTTHQ--DLPVASDKVRKLRLGQ 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
258-502 |
2.98e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPvNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQaIAQ 337
Cdd:PRK11231 2 TLRTENLTVGYG-TKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ-SGTVFLGDKPISMLSSRQ-LAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEdrkrdgivpVMAVGKNITLAAL--------NKFTGGISQLDDAaeqkcileSIQQLKVKTSSPDLAIGR---L 406
Cdd:PRK11231 77 RLALLPQ---------HHLTPEGITVRELvaygrspwLSLWGRLSAEDNA--------RVNQAMEQTRINHLADRRltdL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKAn 486
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA- 218
|
250
....*....|....*.
gi 1014292979 487 linhNLTQEQVMEAAL 502
Cdd:PRK11231 219 ----QGTPEEVMTPGL 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
277-482 |
3.87e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEIL-----------GIAGLVG---AGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNcQQAIAQGIAMV 342
Cdd:PRK10790 343 IDNVSFAYRDDNLVlqninlsvpsrGFVALVGhtgSGKSTLASLLMGYYPLT-EGEIRLDGRPLSSLS-HSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 343 PEDrkrdgivPVMAVGK---NITLAAlnkftggisqldDAAEQKC--ILESIQQLKVKTSSPD---LAIG----RLSGGN 410
Cdd:PRK10790 421 QQD-------PVVLADTflaNVTLGR------------DISEEQVwqALETVQLAELARSLPDglyTPLGeqgnNLSVGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLInQLVQQGIAVIVISSELPEVLGlSDRVLVMHEGK 482
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
258-483 |
4.32e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.68 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTawhpvnrhiKR------VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDirnc 331
Cdd:COG3842 5 ALELENVS---------KRygdvtaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-SGRILLDGRDVT---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 332 qqaiaqgiAMVPEdrKRD-GIV-------PVMAVGKNITlaalnkFtgGISQ--LDDAAEQKCILESIQQLKVktssPDL 401
Cdd:COG3842 71 --------GLPPE--KRNvGMVfqdyalfPHLTVAENVA------F--GLRMrgVPKAEIRARVAELLELVGL----EGL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 402 A---IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLV 477
Cdd:COG3842 129 AdryPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAV 208
|
....*.
gi 1014292979 478 MHEGKL 483
Cdd:COG3842 209 MNDGRI 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-204 |
4.90e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShirDTERkgi 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEGP---GAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1014292979 164 LILDEPTASLT----EQETSVLLDIIRDlqqHGIACIYISHKLNE 204
Cdd:PRK11248 150 LLLDEPFGALDaftrEQMQTLLLKLWQE---TGKQVLLITHDIEE 191
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
279-482 |
6.06e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.58 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKI-YI--DGKQVDIrncqqaiaqgIAMVPEDRK-------- 347
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD-AGEVhYRmrDGQLRDL----------YALSEAERRrllrtewg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 348 ------RDGIVPVMAVGKNI---TLAALNKFTGGISQlddAAeqkciLESIQQLKVKTSSPDLAIGRLSGGNQQKAILAR 418
Cdd:PRK11701 93 fvhqhpRDGLRMQVSAGGNIgerLMAVGARHYGDIRA---TA-----GDWLERVEIDAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 419 CLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
277-480 |
6.10e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGqwEGKIYIDGKqvdIRncqqaiaqgIAMVPEDRKRDGIVPVM 355
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGlVAPD--EGVIKRNGK---LR---------IGYVPQKLYLDTTLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 ---------AVGKNITLAALNKFTGGisQLDDAAEQKcilesiqqlkvktsspdlaigrLSGGNQQKAILARCLLLNPRI 426
Cdd:PRK09544 86 vnrflrlrpGTKKEDILPALKRVQAG--HLIDAPMQK----------------------LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 427 LILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHE 480
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-482 |
6.50e-15 |
|
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: 74.19 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTeTIQCLFGVWPGQWEGKIYIDGkqVDIRNCQ-QAIAQGIAMVPEDRkrdgIVPVM 355
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKS-TLVNLIPRFYDVDSGRILIDG--HDVRDYTlASLRRQIGLVSQDV----FLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 AVGKNITLAALNkftGGISQLDDAAEQKCILESIQQLkvktssP---DLAIG----RLSGGNQQKAILARCLLLNPRILI 428
Cdd:cd03251 91 TVAENIAYGRPG---ATREEVEEAARAANAHEFIMEL------PegyDTVIGergvKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 429 LDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGlSDRVLVMHEGK 482
Cdd:cd03251 162 LDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-219 |
7.12e-15 |
|
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: 74.06 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 19 AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIqASHIRDTERKGIAIIHQELALVKElTV 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV--PENGRVLVDGHDL-ALADPAWLRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 99 LENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSIspDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTASLT 174
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHDFISELPEGY--DTIVGEQGAglsgGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1014292979 175 EQETSVLLDIIRDLQQhGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03252 171 YESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGR 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
258-482 |
7.14e-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: 74.26 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAW---HPVnrhikrVNDVSFSLKRGEILGIAGLVGAGRT---------ETIQclfgvwpgqwEGKIYIDGKQ 325
Cdd:COG1126 1 MIEIENLHKSfgdLEV------LKGISLDVEKGEVVVIIGPSGSGKStllrcinllEEPD----------SGTITVDGED 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 326 VDIRNCQqaiaqgiamVPEDRKRDGIV-------PVMAVGKNITLAALNkfTGGISQldDAAEQKcileSIQQL-KV--- 394
Cdd:COG1126 65 LTDSKKD---------INKLRRKVGMVfqqfnlfPHLTVLENVTLAPIK--VKKMSK--AEAEER----AMELLeRVgla 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 395 --KTSSPdlaiGRLSGGNQQK-AIlARCLLLNPRILILDEPTRGID---IGakyEIYKLINQLVQQGIAVIVISSELP-- 466
Cdd:COG1126 128 dkADAYP----AQLSGGQQQRvAI-ARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGfa 199
|
250
....*....|....*..
gi 1014292979 467 -EVlglSDRVLVMHEGK 482
Cdd:COG1126 200 rEV---ADRVVFMDGGR 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-219 |
7.69e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 72.73 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFG--SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQAshIRDTERKG 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK--PQQGEITLDGVPVSD--LEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENI---FLGneithngimdydlmtlrcqkllaqvslsispdtrvgdlglGQQQLVEIAKALNK 159
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNNLgrrFSG----------------------------------------GERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 160 QVRLLILDEPTASL---TEQET-SVLLDIIRDLqqhgiACIYISHKLNEVKAIsDTICVIRDGQ 219
Cdd:cd03247 116 DAPIVLLDEPTVGLdpiTERQLlSLIFEVLKDK-----TLIWITHHLTGIEHM-DKILFLENGK 173
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-233 |
8.15e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQA-SHIRDTE-RK 81
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH--GEILFDGENIPAmSRSRLYTvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLENIF--------LGNEITHNGIMdydlmtlrcQKLLAqVSLSISPDTRVGDLGLGQQQLVEI 153
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAyplrehtqLPAPLLHSTVM---------MKLEA-VGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 154 AKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSED 232
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
.
gi 1014292979 233 D 233
Cdd:PRK11831 235 P 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-203 |
9.43e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 23 VCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgsYEGEIIFAGEEI------QASHIRdterkgiAIIHQELALVKEL 96
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP---GQGEILLNGRPLsdwsaaELARHR-------AYLSQQQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 97 TVLENIFLGneithngiMDYDLMTLRCQKLLAQVS--LSISP--DTRVGDLGLGQQQLVEIAKAL-------NKQVRLLI 165
Cdd:COG4138 85 PVFQYLALH--------QPAGASSEAVEQLLAQLAeaLGLEDklSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1014292979 166 LDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLN 203
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLN 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-212 |
9.43e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.65 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 14 FGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsyegeiifageeiQASHIRDTERKGIAIIHQELALV 93
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP--------------TSGTVRRAGGARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 KEL--TVLENIFLG--------NEITHNGIMDYDlmtlrcqKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:NF040873 68 DSLplTVRDLVAMGrwarrglwRRLTRDDRAAVD-------DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTI 212
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
256-482 |
1.02e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.50 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDI-RNCQQA 334
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS-SGRILFDGKPIDYsRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 335 IAQGIAMVPEDRkrDGIVPVMAVGKNITLAALNKftgGISQLDDAAEQKCILE--SIQQLKVKTSSPdlaigrLSGGNQQ 412
Cdd:PRK13636 80 LRESVGMVFQDP--DNQLFSASVYQDVSFGAVNL---KLPEDEVRKRVDNALKrtGIEHLKDKPTHC------LSFGQKK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
277-485 |
1.08e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW-PGQweGKIYIDGKQVDIRNCQqAIAQGIAMVPEDRKRDGIVPVM 355
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTA--GTVLVAGDDVEALSAR-AASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 AVGKNITLAALNKFtGGISQLDDAAeqkcILESIQQLKVkTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:PRK09536 96 QVVEMGRTPHRSRF-DTWTETDRAA----VERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1014292979 436 IDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
267-481 |
1.22e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.13 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 267 WHPvNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWP---GQ--WEGKIYIDGKQVDIRncqqAIAQGIAM 341
Cdd:PRK15079 28 WQP-PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKatdGEvaWLGKDLLGMKDDEWR----AVRSDIQM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 342 VPEDrKRDGIVPVMAVGkNITLAALNKFTGGISQLDDAAEQKCILESIQQLkvktssPDLaIGR----LSGGNQQKAILA 417
Cdd:PRK15079 103 IFQD-PLASLNPRMTIG-EIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLL------PNL-INRypheFSGGQCQRIGIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
267-483 |
1.43e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 267 WHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPGqwEGKIYIDGkqvdirncqqaiaqgiaMVPED 345
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVPT--SGEVRVLG-----------------YVPFK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 346 RKRdgivpvmAVGKNIT------------LAALNKFT--GGISQLDDAAEQKCILESIQQLKVKtsspDL---AIGRLSG 408
Cdd:COG4586 89 RRK-------EFARRIGvvfgqrsqlwwdLPAIDSFRllKAIYRIPDAEYKKRLDELVELLDLG----ELldtPVRQLSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
272-483 |
1.71e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 272 RHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAiAQGIAMVPEDrKRDGI 351
Cdd:PRK15112 24 QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYSYR-SQRIRMIFQD-PSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 352 VPVMAVGKNITLA-ALNkftggiSQLDDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK15112 101 NPRQRISQILDFPlRLN------TDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-202 |
2.01e-14 |
|
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: 75.47 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 15 GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQaSHIRDTERKGIAIIHQElALVK 94
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVPVS-SLDQDEVRRRVSVCAQD-AHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 ELTVLENIFLGNEithnGIMDYDLMtlrcqKLLAQVSLSISP-------DTRVGDLGL----GQQQLVEIAKALNKQVRL 163
Cdd:TIGR02868 422 DTTVRENLRLARP----DATDEELW-----AALERVGLADWLralpdglDTVLGEGGArlsgGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 1014292979 164 LILDEPTASLTEQETSVLLDIIRDLQQhGIACIYISHKL 202
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-255 |
2.18e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 25 LRLNAGEIVSLCGENGSGKSTLMKVLcGIYpHGSYEGEIIFAGEEIQASHIRDTERKgIAIIHQELALVKELTVLENIFL 104
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKML-GRH-QPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRELVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 105 GNEITHN-----GIMDYDlmtlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASL-TEQET 178
Cdd:PRK10575 109 GRYPWHGalgrfGAADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALdIAHQV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 179 SVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMVGRELTALypnePHTTG 255
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGIL----PHPAG 257
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
259-485 |
2.44e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTawhpVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQweGKIYIDGKQVDiRNCQQAIA 336
Cdd:PRK13548 3 LEARNLS----VRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDS--GEVRLNGRPLA-DWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEdrkrdgivpvmavgkNITLAAlnKFT-------GGISQLDDAAEQKCILESIQQLkvkTSSPDLAiGR---- 405
Cdd:PRK13548 76 RRRAVLPQ---------------HSSLSF--PFTveevvamGRAPHGLSRAEDDALVAAALAQ---VDLAHLA-GRdypq 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLL------LNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSElpevLGL----SDR 474
Cdd:PRK13548 135 LSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHD----LNLaaryADR 210
|
250
....*....|.
gi 1014292979 475 VLVMHEGKLKA 485
Cdd:PRK13548 211 IVLLHQGRLVA 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-219 |
2.99e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGEEIQAshirDTERKGIAIIHQELALVK--- 94
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVPTQGSVRVDDTLITS----TSKNKDIKQIRKKVGLVFqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 -----ELTVLENIFLGNEitHNGIMDYDLMTLRCQKLlAQVSLSISP-DTRVGDLGLGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK13649 95 esqlfEETVLKDVAFGPQ--NFGVSQEEAEALAREKL-ALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 169 PTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-225 |
3.50e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.30 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAG---EEIQASHIRDTERK 81
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE--PTRGQVLIDGvdiAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLENIFLGNEIThnGIMDYDLMTlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELA--GINAEERRE-KALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 162 RLLILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRD 225
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGTPD 250
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
4.90e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 2 PYLLEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGEEIQASHiRDT 78
Cdd:PRK11160 336 QVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQ---QGEILLNGQPIADYS-EAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 ERKGIAIIHQELALVKElTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSlsiSPDTRVGDLGL----GQQQLVEIA 154
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA-TLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDK---GLNAWLGEGGRqlsgGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 155 KALNKQVRLLILDEPTASL---TEQEtsvlldIIRDLQQH--GIACIYISHKLNEVKAIsDTICVIRDGQHI 221
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLdaeTERQ------ILELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-253 |
5.48e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPyLLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIR 76
Cdd:PRK15093 1 MP-LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 77 DTERK-----GIAIIHQELALVkeLTVLENIflGNEI-------THNG--IMDYDLMTLRCQKLLAQVSLSISPDTRVG- 141
Cdd:PRK15093 80 PRERRklvghNVSMIFQEPQSC--LDPSERV--GRQLmqnipgwTYKGrwWQRFGWRKRRAIELLHRVGIKDHKDAMRSf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 142 --DLGLGQQQLVEIAKALNKQVRLLILDEPTASLteqETSVLLDIIRDL----QQHGIACIYISHKLNEVKAISDTICVI 215
Cdd:PRK15093 156 pyELTEGECQKVMIAIALANQPRLLIADEPTNAM---EPTTQAQIFRLLtrlnQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 1014292979 216 RDGQHIGTrdaaGMSEDDIITmmvgreltalyPNEPHT 253
Cdd:PRK15093 233 YCGQTVET----APSKELVTT-----------PHHPYT 255
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
253-478 |
5.68e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.04 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 253 TTGDEILRIEHLTAWHPVNRHIKRV-NDVSFSLKRGE---ILG------------IAGLVGAGrtetiqclfgvwpgqwE 316
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTAlDDVSLTVAAGEfvaLVGpsgcgkstllrlIAGLEKPT----------------S 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 317 GKIYIDGKQVDirncqqAIAQGIAMVPEDrkrDGIVPVMAVGKNITLAALNKftgGIS--QLDDAAEQkcILESIQQLKV 394
Cdd:COG1116 66 GEVLVDGKPVT------GPGPDRGVVFQE---PALLPWLTVLDNVALGLELR---GVPkaERRERARE--LLELVGLAGF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 395 KTSSPdlaiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSD 473
Cdd:COG1116 132 EDAYP----HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLAD 207
|
....*
gi 1014292979 474 RVLVM 478
Cdd:COG1116 208 RVVVL 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-200 |
5.69e-14 |
|
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: 69.88 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFageeiqashirdTERKGIAIIHQELALVkeltvl 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGS--GRIGM------------PEGEDLLFLPQRPYLP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 100 enifLGneithngimdydlmTLRCQkllaqvslSISPDTRVgdLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETS 179
Cdd:cd03223 77 ----LG--------------TLREQ--------LIYPWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 1014292979 180 VLLDIirdLQQHGIACIYISH 200
Cdd:cd03223 129 RLYQL---LKELGITVISVGH 146
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
256-486 |
5.83e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 71.23 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPgqWEGKIYIDGKQV------- 326
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTAlRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRP--TSGEVLIDGQDIsslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 327 --DIRNcqQAIaqgiamvpedrkrdGIV-------PVMAVGKNITLAALnkfTGGISQLDDAAEQKCILESIQQLKVKTS 397
Cdd:COG1136 80 laRLRR--RHI--------------GFVfqffnllPELTALENVALPLL---LAGVSRKERRERARELLERVGLGDRLDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 398 SPdlaiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSElPEVLGLSDRVL 476
Cdd:COG1136 141 RP----SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVI 215
|
250
....*....|
gi 1014292979 477 VMHEGKLKAN 486
Cdd:COG1136 216 RLRDGRIVSD 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
258-483 |
5.84e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 71.24 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGqwEGKIYIDGKQV-DIRNcqqai 335
Cdd:COG2884 1 MIRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGQDLsRLKR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 aqgiAMVPEDRKRDGIV-------PVMAVGKNITLAAlnKFTG-GISQLDDAAEQkcILESIQQLKVKTSSPDlaigRLS 407
Cdd:COG2884 72 ----REIPYLRRRIGVVfqdfrllPDRTVYENVALPL--RVTGkSRKEIRRRVRE--VLDLVGLSDKAKALPH----ELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 408 GGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-221 |
6.11e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS-----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTE 79
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 ---------------------RKGIAIIHQ--ELALVKElTVLENIFLGnEITHNgiMDYDLMTLRCQKLLAQVSLSISP 136
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFG-PVSMG--VSKEEAKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 137 DTRVG-DLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVI 215
Cdd:PRK13651 159 LQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*.
gi 1014292979 216 RDGQHI 221
Cdd:PRK13651 239 KDGKII 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
274-483 |
8.42e-14 |
|
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: 70.51 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 274 IKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPGQweGKIYIDGKQV-DIRNCQQA-IAQGIAMVPEDRKrdg 350
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTS--GTIRVNGQDVsDLRGRAIPyLRRKIGVVFQDFR--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 351 IVPVMAVGKNITLAALnkftggISQLDDAAEQKCILESIQQLKVKTSSPDLAIGrLSGGNQQKAILARCLLLNPRILILD 430
Cdd:cd03292 89 LLPDRNVYENVAFALE------VTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-226 |
9.28e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 17 VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTE--RKGIAIIHQE--LAL 92
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE--SQGGEIIFNGQRIDTLSPGKLQalRRDIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 93 VKELTVLENIFlgNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRV-GDLGLGQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:PRK10261 415 DPRQTVGDSIM--EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 172 ----SLTEQETSVLLDIIRDLqqhGIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDA 226
Cdd:PRK10261 493 aldvSIRGQIINLLLDLQRDF---GIAYLFISHDMAVVERISHRVAVMYLGQivEIGPRRA 550
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
277-511 |
9.73e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV---------WPGQWEGKIyiDGKQvdirncQQAIAQGIAMVPEDrk 347
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLespsqgnvsWRGEPLAKL--NRAQ------RKAFRRDIQMVFQD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 348 rdgivPVMAVGKNITLAA-----LNKFTGgisqLDDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLL 422
Cdd:PRK10419 98 -----SISAVNPRKTVREiirepLRHLLS----LDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKlkanlinhnLTQEQVMEAA 501
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ---------IVETQPVGDK 239
|
250
....*....|
gi 1014292979 502 LRSEHHVEKQ 511
Cdd:PRK10419 240 LTFSSPAGRV 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.04e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.31 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTe 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL--PQRGRVKVMGREVNAENEKWV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELA-LVKELTVLENIFLGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK13647 78 RSKVGLVFQDPDdQVFSSTVWDDVAFG---PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDII 235
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
253-483 |
1.06e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 72.07 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 253 TTGDEILRIEHLTAWHPVNR--------HIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGK 324
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGglfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT-SGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 325 QVdirncqqAIAQGIAMVPEdRKRDGIV---------PVMAVGKNITLAALnkftggISQLDDAAEQKcilESIQQL--K 393
Cdd:COG4608 81 DI-------TGLSGRELRPL-RRRMQMVfqdpyaslnPRMTVGDIIAEPLR------IHGLASKAERR---ERVAELleL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 394 VKTSsPDLAiGR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEV 468
Cdd:COG4608 144 VGLR-PEHA-DRypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVV 221
|
250
....*....|....*
gi 1014292979 469 LGLSDRVLVMHEGKL 483
Cdd:COG4608 222 RHISDRVAVMYLGKI 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-221 |
1.10e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.28 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF---GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGEEIQASHIRD 77
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE--FEGKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERK-GIAIIHQELALVKElTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:PRK13642 79 LRRKiGMVFQNPDNQFVGA-TVEDDVAFGME---NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 157 LNKQVRLLILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVkAISDTICVIRDGQHI 221
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEA-ASSDRILVMKAGEII 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
277-483 |
1.18e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 72.10 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPgqWEGKIYIDGKQVDIRncqqaiaqgiaMVPEDRkRDGIV--- 352
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP--DSGRIVLNGRDLFTN-----------LPPRER-RVGFVfqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 ----PVMAVGKNItlaalnKFTGGISQLDDAAEQKCILESIQ--QLkvktssPDLAiGR----LSGGNQQKAILARCLLL 422
Cdd:COG1118 84 yalfPHMTVAENI------AFGLRVRPPSKAEIRARVEELLElvQL------EGLA-DRypsqLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-210 |
1.35e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 3 YLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKV---LCGIYPHGSYEGEIIFAGEEIQASHIRDTE 79
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEGKVTFHGKNLYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 -RKGIAIIHQELALVKElTVLENIFLGNEIthNGiMDYDLMTLrCQKLLAQVSLSISPDTRVGDLGL----GQQQLVEIA 154
Cdd:PRK14243 89 vRRRIGMVFQKPNPFPK-SIYDNIAYGARI--NG-YKGDMDEL-VERSLRQAALWDEVKDKLKQSGLslsgGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 155 KALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIacIYISHKLNEVKAISD 210
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELkEQYTI--IIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.47e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 3 YLLEMKNITKTFGS-VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIqashirDTERK 81
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS--GRILFDGKPI------DYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKE--------LTVLENIFLGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEI 153
Cdd:PRK13636 76 GLMKLRESVGMVFQdpdnqlfsASVYQDVSFG---AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 154 AKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
1.91e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFaGEEIQashirdterkgI 83
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE--PDSGTVKL-GETVK-----------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELA-LVKELTVLENIFLGNEithnGIMDYDLMTLrCQKLLaqvslsISPD---TRVGDLGLGQQQLVEIAKALNK 159
Cdd:COG0488 381 GYFDQHQEeLDPDKTVLDELRDGAP----GGTEQEVRGY-LGRFL------FSGDdafKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 160 QVRLLILDEPT-----ASLTeqetsVLLDIIRDLQqhGiACIYISHK---LNevkAISDTICVIRDGQ 219
Cdd:COG0488 450 PPNVLLLDEPTnhldiETLE-----ALEEALDDFP--G-TVLLVSHDryfLD---RVATRILEFEDGG 506
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-464 |
1.91e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 25 LRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEiifageeiQASHIRDTERkgiaiihqeLALVKELTVLENIFL 104
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELP--LLSGE--------RQSQFSHITR---------LSFEQLQKLVSDEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 105 GN-----------------EITHNGIMDydlmTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILD 167
Cdd:PRK10938 85 RNntdmlspgeddtgrttaEIIQDEVKD----PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 168 EPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDAAgMSEDDIITMMVGRELTA 245
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTlaETGEREEI-LQQALVAQLAHSEQLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 246 LYPNEPhttgDEILRIEHLTAWHP--------VNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQWE 316
Cdd:PRK10938 240 VQLPEP----DEPSARHALPANEPrivlnngvVSYNDRPIlHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 317 GKIYIDGKQvdiRNCQQA---IAQGIAMVPEDRKRDGIVPVMAvgKNITLAALnkFTG-GISQLDDAAEQKCILESIQQL 392
Cdd:PRK10938 316 NDLTLFGRR---RGSGETiwdIKKHIGYVSSSLHLDYRVSTSV--RNVILSGF--FDSiGIYQAVSDRQQKLAQQWLDIL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 393 KVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDigakyeiyKLINQLVQQGIAVIVISSE 464
Cdd:PRK10938 389 GIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD--------PLNRQLVRRFVDVLISEGE 452
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-234 |
1.92e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphgsyegeiifageEIQASHIRDTER 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV--------------APDEGVIKRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELTVLENIFLgneITHNGIMDYDLMtlrcqKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK09544 67 LRIGYVPQKLYLDTTLPLTVNRFL---RLRPGTKKEDIL-----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIrdGQHI---GTRDAAGMSEDDI 234
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL--NHHIccsGTPEVVSLHPEFI 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-219 |
2.00e-13 |
|
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: 73.51 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 7 MKNITKTFGSV--KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShiRDTERKGIA 84
Cdd:TIGR01257 931 VKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGKDIETN--LDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEITHNgimDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGR---SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQhGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
259-465 |
2.53e-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: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNcQQAIAQG 338
Cdd:TIGR02868 335 LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-QGEVTLDGVPVSSLD-QDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 IAMVPEDrkrdgiVPVMA--VGKNITLAAlnkftGGIS--QLDDAAEQKCILESIQQLKVKTSSPDLAIG-RLSGGNQQK 413
Cdd:TIGR02868 411 VSVCAQD------AHLFDttVRENLRLAR-----PDATdeELWAALERVGLADWLRALPDGLDTVLGEGGaRLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 414 AILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSEL 465
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
256-501 |
2.94e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.15 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQaI 335
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGREVNAENEKW-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 AQGIAMVPEDRkrDGIVPVMAVGKNITLAALNKFTGGiSQLDDAAEQKCILESIQQLKVKtsspdlAIGRLSGGNQQKAI 415
Cdd:PRK13647 78 RSKVGLVFQDP--DDQVFSSTVWDDVAFGPVNMGLDK-DEVERRVEEALKAVRMWDFRDK------PPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQE 495
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
....*.
gi 1014292979 496 QVMEAA 501
Cdd:PRK13647 229 DIVEQA 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
277-481 |
2.95e-13 |
|
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: 69.42 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPGqwEGKIYIDGKQVDIRNCQQAIA-QGIAMVPEDRKRDGIvpv 354
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPT--SGGVILEGKQITEPGPDRMVVfQNYSLLPWLTVRENI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 355 mAVGKNITLAALNKftggisqlddaAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTR 434
Cdd:TIGR01184 76 -ALAVDRVLPDLSK-----------SERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 435 GIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-219 |
3.10e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIyPHGSyEGEIIFAGEEIqasHIRDTE 79
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGS-SGEVSLVGQPL---HQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 R------KGIAIIHQELALVKELTVLENIFLGNEIthNGIMDYDLMTlRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEI 153
Cdd:PRK10584 81 AraklraKHVGFVFQSFMLIPTLNALENVELPALL--RGESSRQSRN-GAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 154 AKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKlNEVKAISDTICVIRDGQ 219
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-219 |
3.10e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 32 IVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGEEIqashirDTERKGIAIIHQELALVKElTVLENIF---LGNE 107
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLrPQ---KGAVLWQGKPL------DYSKRGLLALRQQVATVFQ-DPEQQIFytdIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 108 ITHN----GIMDyDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLD 183
Cdd:PRK13638 99 IAFSlrnlGVPE-AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1014292979 184 IIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
258-483 |
3.27e-13 |
|
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: 69.04 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQV-DIRNCQqaIA 336
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVLLDGKPIsQYEHKY--LH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEDrkrdgivPVM---AVGKNITLAALNKFTGGISQLDDAAEQKCILESIQQlkvktsSPDLAIG----RLSGG 409
Cdd:cd03248 88 SKVSLVGQE-------PVLfarSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELAS------GYDTEVGekgsQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 410 NQQKAILARCLLLNPRILILDEPTRGIDIgakyEIYKLINQLVQQGI---AVIVISSELPEVlGLSDRVLVMHEGKL 483
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDA----ESEQQVQQALYDWPerrTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-218 |
3.59e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 68.32 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiypHGSYE---GEIIFAGEEIQASHIRDTERK 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKYEvteGEILFKGEDITDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLEniFLgneithngimdydlmtlrcqkllaqvslsispdtRVGDLGL--GQQQLVEIAKALNK 159
Cdd:cd03217 78 GIFLAFQYPPEIPGVKNAD--FL----------------------------------RYVNEGFsgGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHK---LNEVKAisDTICVIRDG 218
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIKP--DRVHVLYDG 181
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
256-485 |
4.55e-13 |
|
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: 68.96 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTawhpVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGK-IYIDGKQ---VDIRn 330
Cdd:COG1119 1 DPLLELRNVT----VRRGGKTIlDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP-PTYGNdVRLFGERrggEDVW- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 331 cqqaiaqgiamvpEDRKRDGIV--------PVMAVGKNITLAALNKFTGGISQLDDAAEQKC--ILES--IQQLKvktss 398
Cdd:COG1119 75 -------------ELRKRIGLVspalqlrfPRDETVLDVVLSGFFDSIGLYREPTDEQRERAreLLELlgLAHLA----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 399 pDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQG-IAVIVISSELPEVLGLSDRVLV 477
Cdd:COG1119 137 -DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLL 215
|
....*...
gi 1014292979 478 MHEGKLKA 485
Cdd:COG1119 216 LKDGRVVA 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-219 |
4.81e-13 |
|
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: 68.65 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 22 NVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTERKgIAIIHQELALVKElTVLEN 101
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ--PQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 102 IflgneithngimDYDLMT--LRCQKLLAQVS--------LSISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILD 167
Cdd:cd03248 108 I------------AYGLQScsFECVKEAAQKAhahsfiseLASGYDTEVGEKGSqlsgGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 168 EPTASL-TEQETSVLLDIIRDLQQHGIacIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03248 176 EATSALdAESEQQVQQALYDWPERRTV--LVIAHRLSTVER-ADQILVLDGGR 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
259-483 |
6.29e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.57 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTawhpVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPG---QWEGKIYIDGKQV---DIRncq 332
Cdd:PRK10418 5 IELRNIA----LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGRVLLDGKPVapcALR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 333 qaiAQGIAMVPEDrKRDGIVPV--MAVGKNITLAALNKftggisQLDDAAEQKCI----LESIQQLkvktssPDLAIGRL 406
Cdd:PRK10418 78 ---GRKIATIMQN-PRSAFNPLhtMHTHARETCLALGK------PADDATLTAALeavgLENAARV------LKLYPFEM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
277-483 |
6.73e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.01 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQqaiaqgiamvpEDRKRDGIV---P 353
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIFYNNQAITDDNFE-----------KLRKHIGIVfqnP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 354 VmavgknitlaalNKFTGGISQLDDA--------------AEQKCILESIQQLKVKTSSPDlaigRLSGGNQQKAILARC 419
Cdd:PRK13648 93 D------------NQFVGSIVKYDVAfglenhavpydemhRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 420 LLLNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-219 |
6.78e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTF----------GSVK-----------AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPHGsyeGEI 63
Cdd:COG4586 3 EVENLSKTYrvyekepglkGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVPTS---GEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 64 IFAGEEIQAshirdtERKGIAiihQELALV---K-----ELTVLENIFLGNEIthngimdYDLMTLRCQKLLAQVS--LS 133
Cdd:COG4586 80 RVLGYVPFK------RRKEFA---RRIGVVfgqRsqlwwDLPAIDSFRLLKAI-------YRIPDAEYKKRLDELVelLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 134 ISP--DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASL--TEQETsvLLDIIRDL-QQHGIACIYISHKLNEVKAI 208
Cdd:COG4586 144 LGEllDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLdvVSKEA--IREFLKEYnRERGTTILLTSHDMDDIEAL 221
|
250
....*....|.
gi 1014292979 209 SDTICVIRDGQ 219
Cdd:COG4586 222 CDRVIVIDHGR 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
275-495 |
7.06e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.09 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 275 KRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW-PGQweGKIYIDGKQVDIRNCQQAIAqgiamvpEDRKRDGIV- 352
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSS--GTITIAGYHITPETGNKNLK-------KLRKKVSLVf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 --PVM-----AVGKNITLAALNkFtgGISqlDDAAEQKCiLESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPR 425
Cdd:PRK13641 92 qfPEAqlfenTVLKDVEFGPKN-F--GFS--EDEAKEKA-LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 426 ILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKlkanLINHNLTQE 495
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK----LIKHASPKE 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
278-491 |
7.54e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTeTIQCLFGVWPGQWEGKIYIDGkqVDIRNCQ-QAIAQGIAMVPEDrkrdgiVPVM- 355
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKS-TIANLLTRFYDIDEGEILLDG--HDLRDYTlASLRNQVALVSQN------VHLFn 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 -AVGKNITLAALNKFTggISQLDDAAEQKCILESIQQLKvktSSPDLAIGR----LSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK11176 431 dTIANNIAYARTEQYS--REQIEEAARMAYAMDFINKMD---NGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGlSDRVLVMHEGKLK-----ANLINHN 491
Cdd:PRK11176 506 EATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVergthAELLAQN 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
277-483 |
8.57e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.76 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNC-QQAIAQGIAMVPED-----RK-RD 349
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ-SGRILIDG--TDIRTVtRASLRRNIAVVFQDaglfnRSiED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 350 GIvpvmAVGK-NITLAalnkftggisQLDDAAEQKCILESIQQlkvKTSSPDLAIG----RLSGGNQQKAILARCLLLNP 424
Cdd:PRK13657 428 NI----RVGRpDATDE----------EMRAAAERAQAHDFIER---KPDGYDTVVGergrQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 425 RILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDE-LMKGRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
273-483 |
9.24e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 273 HIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW-PGQweGKI---YIDGK----------QVDIRNCQQAIAQG 338
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlPDT--GTIewiFKDEKnkkktkekekVLEKLVIQKTRFKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 339 IAMVPEDRKRDGIVPVMA--------VGKNITLAALNKftgGISQldDAAEQKCiLESIQQLKVKTSSPDLAIGRLSGGN 410
Cdd:PRK13651 97 IKKIKEIRRRVGVVFQFAeyqlfeqtIEKDIIFGPVSM---GVSK--EEAKKRA-AKYIELVGLDESYLQRSPFELSGGQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
252-481 |
9.37e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 252 HTTGDEILRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgqW-EGKIyidgkqvdIRN 330
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP--YgSGRI--------ARP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 331 CqqaiAQGIAMVPEDrkrdgivPVMAVGkniTLAALNKFTGGISQLDDAAeqkcILESIQQLKVKTSSPDLAIG-----R 405
Cdd:COG4178 424 A----GARVLFLPQR-------PYLPLG---TLREALLYPATAEAFSDAE----LREALEAVGLGHLAERLDEEadwdqV 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSElPEVLGLSDRVLVMHEG 481
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREEL-PGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-219 |
9.39e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.43 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS--VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGEEIQASHIRDTeRKG 82
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY--DIDEGEILLDGHDLRDYTLASL-RNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENI-------FLGNEITHNGIMDY--DLMTLRCQKLlaqvslsispDTRVGDLGL----GQQQ 149
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIayarteqYSREQIEEAARMAYamDFINKMDNGL----------DTVIGENGVllsgGQRQ 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 150 LVEIAKALNKQVRLLILDEPTASL-TEQETSV--LLDiirDLQQHGIACIyISHKLNEVKAiSDTICVIRDGQ 219
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALdTESERAIqaALD---ELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGE 555
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-219 |
9.60e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.78 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiypHGSYE---GEIIFAGEEIQASHIRDTERK 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG---HPKYEvtsGSILLDGEDILELSPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQELALVKELTVLEniFLGNEITHNGIMDYDLMTLR--CQKLLAQVSLSISPDTRVGDLGL--GQQQLVEIAKAL 157
Cdd:COG0396 78 GIFLAFQYPVEIPGVSVSN--FLRTALNARRGEELSAREFLklLKEKMKELGLDEDFLDRYVNEGFsgGEKKRNEILQML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 158 NKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHK---LNEVKAisDTICVIRDGQ 219
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGR 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-219 |
1.43e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 25 LRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEiqasHIRDT-ERKGIAIIHQELALVKELTVLENIF 103
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS--GSLTLNGQD----HTTTPpSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 104 LGneiTHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLT---EQETSV 180
Cdd:PRK10771 94 LG---LNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQEMLT 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1014292979 181 LLDIIRDLQQhgIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK10771 171 LVSQVCQERQ--LTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
279-483 |
1.44e-12 |
|
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: 67.25 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQA-IAQGIAMVPEDrkrdgivPVMAV 357
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-KGQILIDG--IDIRDISRKsLRSMIGVVLQD-------TFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 358 G---KNITLAALNkftggiSQLDD---AAEQKCILESIQQLK--VKTSSPDLAiGRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:cd03254 91 GtimENIRLGRPN------ATDEEvieAAKEAGAHDFIMKLPngYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 430 DEPTRGIDIGAKYEIYKLInQLVQQGIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:cd03254 164 DEATSNIDTETEKLIQEAL-EKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-219 |
1.46e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.20 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 9 NITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGS---YEGEIIFAGEEIqaSHIRDTE--RKGI 83
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSgyrYSGDVLLGGRSI--FNYRDVLefRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKeLTVLENIFLGneITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGD----LGLGQQQLVEIAKALNK 159
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAG--VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 160 QVRLLILDEPTASLTEQETSVLLDIIRDLQQHgIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGR 239
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
281-484 |
1.50e-12 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 66.81 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 281 SFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQweGKIYIDGKQVdirncqqaiaqgIAMVPEDR------KRDGIVP 353
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGfIEPAS--GSIKVNDQSH------------TGLAPYQRpvsmlfQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 354 VMAVGKNITLA--------ALNKftggiSQLDDAAEQKCILESIQQLKvktsspdlaiGRLSGGNQQKAILARCLLLNPR 425
Cdd:TIGR01277 84 HLTVRQNIGLGlhpglklnAEQQ-----EKVVDAAQQVGIADYLDRLP----------EQLSGGQRQRVALARCLVRPNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 426 ILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGKLK 484
Cdd:TIGR01277 149 ILLLDEPFSALDPLLREEMLALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
1.51e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF----------------------GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE--P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 59 YEGEIifageeiqashirdtERKGI--AIIhqELA--LVKELTVLENIFLG--------NEITHN--------GIMDY-D 117
Cdd:COG1134 79 TSGRV---------------EVNGRvsALL--ELGagFHPELTGRENIYLNgrllglsrKEIDEKfdeivefaELGDFiD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 118 L--------MTLRcqklLA-QVSLSISPDTrvgdlglgqqqlveiakalnkqvrlLILDEptaslteqetsVL------- 181
Cdd:COG1134 142 QpvktyssgMRAR----LAfAVATAVDPDI-------------------------LLVDE-----------VLavgdaaf 181
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1014292979 182 ----LDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG1134 182 qkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-249 |
1.82e-12 |
|
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: 70.43 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFG--SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShirdterk 81
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS--GDATVAGKSILTN-------- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 gIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKL----LAQVSLSISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:TIGR01257 2007 -ISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 158 NKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDG--------QHIGTRDAAGM 229
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafqclgtiQHLKSKFGDGY 2165
|
250 260
....*....|....*....|
gi 1014292979 230 seddIITMMVGRELTALYPN 249
Cdd:TIGR01257 2166 ----IVTMKIKSPKDDLLPD 2181
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
279-483 |
1.99e-12 |
|
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: 66.74 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAIAQgIAMVPEDRK------RDGIV 352
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLALADPAWLRRQ-VGVVLQENVlfnrsiRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 ---PVMAVGKNITLAALNKFTGGISQLDDAAEQkcilesiqqlkvktsspdlAIGR----LSGGNQQKAILARCLLLNPR 425
Cdd:cd03252 98 ladPGMSMERVIEAAKLAGAHDFISELPEGYDT-------------------IVGEqgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 426 ILILDEPTRGIDigakYEIYKLINQLVQQ---GIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:cd03252 159 ILIFDEATSALD----YESEHAIMRNMHDicaGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
264-482 |
2.04e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 264 LTAWHPVNR-------HIKRVNDVSFSLKRGEILGIAGLVGAGRTeTIQCLFGVWPGQWEGKIYIDGKQVdIRNCQQAIA 336
Cdd:PRK11308 11 LKKHYPVKRglfkperLVKALDGVSFTLERGKTLAVVGESGCGKS-TLARLLTMIETPTGGELYYQGQDL-LKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QgiamvpedRKRDgivpVMAVGKNiTLAALN--KFTGGI--------SQLDDAAEQKCILESIQQLKVKTSSPDLAIGRL 406
Cdd:PRK11308 89 L--------LRQK----IQIVFQN-PYGSLNprKKVGQIleepllinTSLSAAERREKALAMMAKVGLRPEHYDRYPHMF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
277-483 |
2.23e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 66.98 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQaiaQGIAMVPEDRkrdGIVPVMA 356
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-SGTILFGGEDATDVPVQE---RNVGFVFQHY---ALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITLAALNKftgGISQLDDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:cd03296 91 VFDNVAFGLRVK---PRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 437 DIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03296 168 DAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-219 |
2.25e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYP--HGSYEGEIIFAGEEIQASHIRdTERKGIAIIHQ--ELALV 93
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKptTGTVTVDDITITHKTKDKYIR-PVRKRIGMVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 kELTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVS-----LSISPDTRVGdlglGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK13646 100 -EDTVEREIIFGPK---NFKMNLDEVKNYAHRLLMDLGfsrdvMSQSPFQMSG----GQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 169 PTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-255 |
2.72e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.83 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF----GSVKAIDNVCLRLNAGEIVSLCGENGSGKS----TLMKVLCGiypHGSYEGEIIFAGEEI-- 70
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA---NGRIGGSATFNGREIln 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 71 ----QASHIRDTErkgIAIIHQElalvkELTVLeNIFL--GNEIT-----HNGiMDYDLMTLRCQKLLAQVSLsisPDTR 139
Cdd:PRK09473 86 lpekELNKLRAEQ---ISMIFQD-----PMTSL-NPYMrvGEQLMevlmlHKG-MSKAEAFEESVRMLDAVKM---PEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 140 V------GDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTI 212
Cdd:PRK09473 153 KrmkmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1014292979 213 CVIRDGQhigtrdaagmseddiiTMMVGRELTALY-PNEPHTTG 255
Cdd:PRK09473 233 LVMYAGR----------------TMEYGNARDVFYqPSHPYSIG 260
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-219 |
3.41e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 27 LNAGEIVSLCGENGSGKSTLMKVLCGIY-PHGsyeGEIIFAGEEI-QASHirdterkgiAIIHQELALVKELTVLENIFL 104
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYqPTG---GQVLLDGVPLvQYDH---------HYLHRQVALVGQEPVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 105 GNEITHnGIMDYDLMTLRCQKLLAQVSLSISP-----DTRVGDLG----LGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:TIGR00958 572 RENIAY-GLTDTPDEEIMAAAKAANAHDFIMEfpngyDTEVGEKGsqlsGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1014292979 176 QETSVLLDiirDLQQHGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:TIGR00958 651 ECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
278-482 |
3.57e-12 |
|
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: 68.69 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQA-IAQGIAMVPEDrkrdgivPVM- 355
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT-SGRILIDG--QDIRDVTQAsLRAAIGIVPQD-------TVLf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 --AVGKNITLAALnkftgGISQ--LDDAAEQKCILESIQQLkvktssPDlaiG----------RLSGGNQQK-AIlARCL 420
Cdd:COG5265 445 ndTIAYNIAYGRP-----DASEeeVEAAARAAQIHDFIESL------PD---GydtrvgerglKLSGGEKQRvAI-ARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 421 LLNPRILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSELPEVLGlSDRVLVMHEGK 482
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
278-495 |
3.74e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRncQQAIAQGIAMVpedRKRDGIV----- 352
Cdd:COG4161 19 FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPD-SGQLNIAGHQFDFS--QKPSEKAIRLL---RQKVGMVfqqyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 --PVMAVGKNITLAALNKFtgGISQLDDAAEQKCILESIQQLKVKTSSPDlaigRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:COG4161 93 lwPHLTVMENLIEAPCKVL--GLSKEQAREKAMKLLARLRLTDKADRFPL----HLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL----KANLINHNLTQE 495
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIieqgDASHFTQPQTEA 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-173 |
3.75e-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: 65.76 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 16 SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPHGSYEGEIIFAGEEIQashiRDTERKGIAIIHQELALVK 94
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTSGQILFNGQPRK----PDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 ELTVLE-----NIFLGNEITHNGIMdydlmtlrcQKLLAQVSLSISPDTRVGD-----LGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03234 95 GLTVREtltytAILRLPRKSSDAIR---------KKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVL 165
|
....*....
gi 1014292979 165 ILDEPTASL 173
Cdd:cd03234 166 ILDEPTSGL 174
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-201 |
3.85e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQAShiRDTERKGIAIIHQELALVKELTVL 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK--GEILFERQSIKKD--LCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 100 ENIFlgneithngimdYDLMT----LRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:PRK13540 93 ENCL------------YDIHFspgaVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 1014292979 176 QETSVLLDIIRDLQQHGIACIYISHK 201
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-219 |
4.47e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGEEIQASHIRDTERK 81
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQ---KGKVLVSGIDTGDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAIIHQ--ELALVKElTVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSI----SPDTRVGdlglGQQQLVEIAK 155
Cdd:PRK13644 78 LVGIVFQnpETQFVGR-TVEEDLAFGPE---NLCLPPIEIRKRVDRALAEIGLEKyrhrSPKTLSG----GQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGK 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
251-483 |
5.69e-12 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 68.20 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 251 PHTTGDeiLRIEHLTAWHPvNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTeTIQCLFGVWPGQWEGKIYIDGkqVDIRN 330
Cdd:TIGR02203 325 ERARGD--VEFRNVTFRYP-GRDRPALDSISLVIEPGETVALVGRSGSGKS-TLVNLIPRFYEPDSGQILLDG--HDLAD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 331 CQ-QAIAQGIAMVPEDrkrdgivpVM----AVGKNITLAALNkfTGGISQLDDAAEQKCILESIQQLKVKTSSPdlaIG- 404
Cdd:TIGR02203 399 YTlASLRRQVALVSQD--------VVlfndTIANNIAYGRTE--QADRAEIERALAAAYAQDFVDKLPLGLDTP---IGe 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 405 ---RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGlSDRVLVMHEG 481
Cdd:TIGR02203 466 ngvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEK-ADRIVVMDDG 543
|
..
gi 1014292979 482 KL 483
Cdd:TIGR02203 544 RI 545
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
277-484 |
6.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTeTIQCLFGVWPGQWEGKIYIDGKQV-------DIRNC---------QQAIA---- 336
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKS-TIAKHMNALLIPSEGKVYVDGLDTsdeenlwDIRNKagmvfqnpdNQIVAtive 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEDRkrdGIVPvmavgKNITlaalnkftggiSQLDDAaeqkciLESIQQLKVKTSSPDLaigrLSGGNQQKAIL 416
Cdd:PRK13633 105 EDVAFGPENL---GIPP-----EEIR-----------ERVDES------LKKVGMYEYRRHAPHL----LSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGlSDRVLVMHEGKLK 484
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
278-482 |
6.57e-12 |
|
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: 65.25 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLfgvwpgQ-----WEGKIYIDGkqVDIR--NCQQAIAQgIAMVPEDrkrdg 350
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLL------ErfydpTSGEILLDG--VDIRdlNLRWLRSQ-IGLVSQE----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 351 ivPV---MAVGKNItlaALNKFTGGISQLDDAAEQKCILESIQQLkvktssP---DLAIG----RLSGGNQQKAILARCL 420
Cdd:cd03249 86 --PVlfdGTIAENI---RYGKPDATDEEVEEAAKKANIHDFIMSL------PdgyDTLVGergsQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 421 LLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGK 482
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
402-478 |
7.26e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 7.26e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 402 AIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVM 478
Cdd:NF040873 116 QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-214 |
7.93e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTF----------GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEI 70
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIET--PTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 71 qASHIRDTE---RKGIAIIHQ----ELALVKEL-TVLENIFLGNEithngimdyDL----MTLRCQKLLAQVSLSISPDT 138
Cdd:PRK11308 80 -LKADPEAQkllRQKIQIVFQnpygSLNPRKKVgQILEEPLLINT---------SLsaaeRREKALAMMAKVGLRPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 139 RV-----GdlglGQQQLVEIAKALNKQVRLLILDEPTASLteqETSV---LLDIIRDLQQH-GIACIYISHKLNEVKAIS 209
Cdd:PRK11308 150 RYphmfsG----GQRQRIAIARALMLDPDVVVADEPVSAL---DVSVqaqVLNLMMDLQQElGLSYVFISHDLSVVEHIA 222
|
....*
gi 1014292979 210 DTICV 214
Cdd:PRK11308 223 DEVMV 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
280-484 |
8.43e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 280 VSFSLKRGEILGIAGLVGAGRTETIQCL-FGVWPGqwEGKIYIDGKQVDI------------RNCQQAIAQGIAMVpedR 346
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCInFLEKPS--EGSIVVNGQTINLvrdkdgqlkvadKNQLRLLRTRLTMV---F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 347 KRDGIVPVMAVGKNITLAALNKFtgGISQLDdaAEQKCILeSIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRI 426
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAPIQVL--GLSKQE--ARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 427 LILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLK 484
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
406-483 |
1.00e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 1.00e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
277-483 |
1.35e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.86 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGE---ILG------------IAGLvgagrtETIQclfgvwpgqwEGKIYIDGKQV-DI----RNcqqaia 336
Cdd:COG3839 19 LKDIDLDIEDGEflvLLGpsgcgkstllrmIAGL------EDPT----------SGEILIGGRDVtDLppkdRN------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 qgIAMVPEDrkrDGIVPVMAVGKNITLAALNKftgGIS------QLDDAAEqkcILEsIQQL---KVKTsspdlaigrLS 407
Cdd:COG3839 77 --IAMVFQS---YALYPHMTVYENIAFPLKLR---KVPkaeidrRVREAAE---LLG-LEDLldrKPKQ---------LS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 408 GGNQQKAILARCLLLNPRILILDEPTRGIDigAK------YEIYKLINQLvqqGIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLD--AKlrvemrAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDG 210
|
..
gi 1014292979 482 KL 483
Cdd:COG3839 211 RI 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
280-483 |
1.71e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.55 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 280 VSFSLKRGEILGIAGLVGAGRTETIQC---LFGVWP-GQWEGKIYIDGKQV---DIRNCQQAIaQGIAMVPEDrkrdgiV 352
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPeARVSGEVYLDGQDIfkmDVIELRRRV-QMVFQIPNP------I 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 PVMAVGKNITLA-ALNKFTGGISQLDDAAEQKciLESIQ---QLKVKTSSPdlaIGRLSGGNQQKAILARCLLLNPRILI 428
Cdd:PRK14247 95 PNLSIFENVALGlKLNRLVKSKKELQERVRWA--LEKAQlwdEVKDRLDAP---AGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 429 LDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
249-483 |
2.11e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.29 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 249 NEPHTTGDEILRIEHLTAWHpVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW---PGQ-WEGKIYIDGK 324
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY-GDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdliPGArVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 325 qvDIRNCQQAiaqgiamVPEDRKRDGIV---PV---MAVGKNITLAA-LNkftgGI---SQLDDAAEqkcilESIQQL-- 392
Cdd:COG1117 79 --DIYDPDVD-------VVELRRRVGMVfqkPNpfpKSIYDNVAYGLrLH----GIkskSELDEIVE-----ESLRKAal 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 393 --KVKTSSPDLAIGrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLG 470
Cdd:COG1117 141 wdEVKDRLKKSALG-LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAAR 218
|
250
....*....|...
gi 1014292979 471 LSDRVLVMHEGKL 483
Cdd:COG1117 219 VSDYTAFFYLGEL 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-219 |
2.16e-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: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGS--VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTeRKG 82
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE--AEEGKIEIDGIDISTIPLEDL-RSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKElTVLENIFLGNEIThngimDYDLMTlrcqkllaqvSLSISPdtrvGDLGL--GQQQLVEIAKALNKQ 160
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDPFDEYS-----DEEIYG----------ALRVSE----GGLNLsqGQRQLLCLARALLKR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDLQQhGIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAGE 200
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
278-483 |
2.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.33 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNcqqaiaqgiAMVPEDRKRDGIV----- 352
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT-SGEVLIKGEPIKYDK---------KSLLEVRKTVGIVfqnpd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 -PVMA--VGKNITLAALNKftgGISQLDDAAEQKCILESIQQLKVKTSSPDlaigRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK13639 89 dQLFAptVEEDVAFGPLNL---GLSKEEVEKRVKEALKAVGMEGFENKPPH----HLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 430 DEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-482 |
2.37e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 9 NITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG---IyphgsYEGEIIFAGEEIQASHIRDTERKGIAI 85
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkI-----QQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 86 IHQELA--LVKELTVLENI-FLGNEITHNG------IMDydlmtlrcqkLLAQVSLSISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:NF033858 81 MPQGLGknLYPTLSVFENLdFFGRLFGQDAaerrrrIDE----------LLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 157 LNKQVRLLILDEPTaslteqeTSV----------LLDIIRDlQQHGIAciyishklnevkaisdticVIrdgqhIGTrda 226
Cdd:NF033858 151 LIHDPDLLILDEPT-------TGVdplsrrqfweLIDRIRA-ERPGMS-------------------VL-----VAT--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 227 AGMSE----DDIITMMVGR--------EL-------------TALYPNEPHT------------TGDEILRIE--HLTaw 267
Cdd:NF033858 196 AYMEEaerfDWLVAMDAGRvlatgtpaELlartgadtleaafIALLPEEKRRghqpvvipprpaDDDDEPAIEarGLT-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 268 hpvnrhiKR------VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDirncqqaiAQGIAM 341
Cdd:NF033858 274 -------MRfgdftaVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPVD--------AGDIAT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 342 vpedRKRdgiVPVMA----------VGKNITL-AALnkFtggisQLDDAAEQKCILESIQQL---KVKTSSPD-LAIG-- 404
Cdd:NF033858 338 ----RRR---VGYMSqafslygeltVRQNLELhARL--F-----HLPAAEIAARVAEMLERFdlaDVADALPDsLPLGir 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 405 -RLSggnqqkaiLARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAvIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:NF033858 404 qRLS--------LAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVT-IFISTHFMNEAERCDRISLMHAGR 474
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
2.62e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNIT-----KTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYP--HGSYEGEIIFAGEEIQASHIR 76
Cdd:PRK13631 21 ILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKskYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 77 DTE-----------RKGIAIIHQ--ELALVKElTVLENIFLGNeiTHNGIMDYDLMTLRCQKL----LAQVSLSISPdtr 139
Cdd:PRK13631 101 TNPyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGP--VALGVKKSEAKKLAKFYLnkmgLDDSYLERSP--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 140 vGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13631 175 -FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
278-482 |
2.70e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.84 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPG--QWEGKIYIDGKQVDiRNCQQAIAqgiAMVPEDrkrDGIVPVM 355
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLNGMPID-AKEMRAIS---AYVQQD---DLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 AVGKNITLAALNKFtggisQLDDAAEQKC--ILESIQQL------KVKTSSPDLAIGrLSGGNQQKAILARCLLLNPRIL 427
Cdd:TIGR00955 115 TVREHLMFQAHLRM-----PRRVTKKEKRerVDEVLQALglrkcaNTRIGVPGRVKG-LSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 428 ILDEPTRGIDIGAKYEIYKLINQLVQQG-IAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-218 |
2.91e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLcgiypHGSYE---GEIIFAGEEIqASHIRDTE 79
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-----QRVFDpqsGRILIDGTDI-RTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQElALVKELTVLENIFLGNE-ITHNGIMD-------YDLMTLRCQKLlaqvslsispDTRVGDLGL----GQ 147
Cdd:PRK13657 408 RRNIAVVFQD-AGLFNRSIEDNIRVGRPdATDEEMRAaaeraqaHDFIERKPDGY----------DTVVGERGRqlsgGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 148 QQLVEIAKALNKQVRLLILDEPTASL---TEQETSVLLDIIRdlqqHGIACIYISHKLNEVKAiSDTICVIRDG 218
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALdveTEAKVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNG 545
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-200 |
3.07e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGsyEGEIIFAGEEIQASHIRDTER--- 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD--DGRIIYEQDLIVARLQQDPPRnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 --------KGIA-------IIHQELALV------KELTVLENifLGNEITHNGIMDYDlmtLRCQKLLAQvsLSISPDTR 139
Cdd:PRK11147 81 gtvydfvaEGIEeqaeylkRYHDISHLVetdpseKNLNELAK--LQEQLDHHNLWQLE---NRINEVLAQ--LGLDPDAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 140 VGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQhgiACIYISH 200
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISH 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-479 |
3.13e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.90 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 275 KRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwpGQWEGKIYIDGKqVDIRNcqQAIAQGIAMVPEDRKRDGIV-- 352
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM--NELESEVRVEGR-VEFFN--QNIYERRVNLNRLRRQVSMVhp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 -----PvMAVGKNITLAAlnKFTGGIS--QLDDAAEQKC----ILESIQQlKVKTSSPDLaigrlSGGNQQKAILARCLL 421
Cdd:PRK14258 96 kpnlfP-MSVYDNVAYGV--KIVGWRPklEIDDIVESALkdadLWDEIKH-KIHKSALDL-----SGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 422 LNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
259-483 |
3.38e-11 |
|
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: 63.47 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRhiKRVNDVSFSLKRGEILGIAGLVGAGRTET---IQCLFGvwPGqwEGKIYIDGK---QVDIRNCQ 332
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTmkmINRLIE--PT--SGEIFIDGEdirEQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 333 QAIAQGIAMVpedrkrdGIVPVMAVGKNITLaalnkftggISQLDDAAEQKCILESIQQLKVKTSSPDLAIGR----LSG 408
Cdd:cd03295 75 RKIGYVIQQI-------GLFPHMTVEENIAL---------VPKLLKWPKEKIRERADELLALVGLDPAEFADRypheLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:cd03295 139 GQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
279-483 |
3.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW-PGQWE---GKIYIDG--KQVDIRNCQQAIAQgIAMVPEDRKRDGIV 352
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKvtvGDIVVSStsKQKEIKPVRKKVGV-VFQFPESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 PvmavgKNITLAALNKftgGISQLDdaaEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:PRK13643 103 L-----KDVAFGPQNF---GIPKEK---AEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 433 TRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-219 |
3.61e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSV----KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI--YPHGSYEGEIIFAGEEIQAshIRD 77
Cdd:PRK11022 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEKLEFNGQDLQR--ISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERKgiAIIHQELALVKE--LTVLENIF-LGNEI-----THNGiMDYDLMTLRCQKLLAQVSLSiSPDTRVG----DLGL 145
Cdd:PRK11022 81 KERR--NLVGAEVAMIFQdpMTSLNPCYtVGFQImeaikVHQG-GNKKTRRQRAIDLLNQVGIP-DPASRLDvyphQLSG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 146 GQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQ-HGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
280-483 |
3.73e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 280 VSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgqWEGKIYIDG---KQVDIRNCQQAIA---QGiAMVPEDRKRDgivp 353
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP--YQGSLKINGielRELDPESWRKHLSwvgQN-PQLPHGTLRD---- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 354 vmavgkNITLAALNkftGGISQLDDAAEQKCILESIQQLkvkTSSPDLAIG----RLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK11174 442 ------NVLLGNPD---ASDEQLQQALENAWVSEFLPLL---PQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 430 DEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELpEVLGLSDRVLVMHEGKL 483
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQL-EDLAQWDQIWVMQDGQI 561
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-483 |
4.21e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 275 KRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV--WPG-------QWEGKiyiDGKQVDIRNCQQAIAQGIAMVPED 345
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGrvmaeklEFNGQ---DLQRISEKERRNLVGAEVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 346 rKRDGIVPVMAVGKNItLAALNKFTGGisqlDDAAEQKCILESIQQLKVK--TSSPDLAIGRLSGGNQQKAILARCLLLN 423
Cdd:PRK11022 98 -PMTSLNPCYTVGFQI-MEAIKVHQGG----NKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
277-483 |
4.75e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDG-------KQVDIRNcqqaIAQGIAMV---PEDR 346
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT-TGTVTVDDitithktKDKYIRP----VRKRIGMVfqfPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 347 KRDGivpvmAVGKNITLAALNkFTGGISQLDDAAeQKCILESIQQLKVKTSSPdlaiGRLSGGNQQKAILARCLLLNPRI 426
Cdd:PRK13646 98 LFED-----TVEREIIFGPKN-FKMNLDEVKNYA-HRLLMDLGFSRDVMSQSP----FQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 427 LILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-219 |
4.89e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 62.55 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 17 VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIfageeiqashirdTERKGIAIIHQELALVKEL 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS--GTVT-------------VRGRVSSLLGLGGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 97 TVLENIFLgneithNGI---MDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTAS- 172
Cdd:cd03220 100 TGRENIYL------NGRllgLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVg 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 173 -LTEQETSvlLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03220 174 dAAFQEKC--QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
257-484 |
4.95e-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: 65.81 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 257 EILRIEHLTAWHPVNRHiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwPGQWEGKIYIDGKQVdIRNCQQaIA 336
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGKSI-LTNISD-VH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 QGIAMVPEdrkRDGIVPVMAVGKNITLAAlnKFTGGISQlddaAEQKCILESIQQLKVKTSSPDLAiGRLSGGNQQKAIL 416
Cdd:TIGR01257 2012 QNMGYCPQ---FDAIDDLLTGREHLYLYA--RLRGVPAE----EIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKLST 2081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLK 484
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
287-482 |
5.40e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 287 GEILGIAGLVGAGRTETIQCLFGVWPGQ-WEGKIYIDGkqvdiRNCQQAIAQGIAMVPEDrkrDGIVPVMAVGKNITLAA 365
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnFTGTILANN-----RKPTKQILKRTGFVTQD---DILYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 366 LNKFTGGISQLDDAAEQKCILESIQQLKVK-TSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEI 444
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAESVISELGLTKCEnTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1014292979 445 YKLINQLVQQGiAVIVISSELP--EVLGLSDRVLVMHEGK 482
Cdd:PLN03211 246 VLTLGSLAQKG-KTIVTSMHQPssRVYQMFDSVLVLSEGR 284
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
257-478 |
5.79e-11 |
|
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: 62.45 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 257 EILRIEHLT---AWHpvNRHIKR---VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYI--DGKQVDI 328
Cdd:COG4778 3 TLLEVENLSktfTLH--LQGGKRlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPD-SGSILVrhDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 329 rncQQAIAQGIAMVpedRKRD-G-------IVP-VMAVgkNITLAALnkFTGGISqlDDAAEQKCiLESIQQLKVKTSSP 399
Cdd:COG4778 80 ---AQASPREILAL---RRRTiGyvsqflrVIPrVSAL--DVVAEPL--LERGVD--REEARARA-RELLARLNLPERLW 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 400 DLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVM 478
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-218 |
6.05e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 7 MKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIyphgsyegEIIFAGE-EIQASHIRDTE--RKGI 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL--------EDITSGDlFIGEKRMNDVPpaERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHNGIMDYDlmtLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEIN---QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 164 LILDEP----TASLTEQetsVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:PRK11000 155 FLLDEPlsnlDAALRVQ---MRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
276-485 |
6.09e-11 |
|
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: 62.13 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 276 RVNDVSFSL-----------KRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQAiAQGIAMVPE 344
Cdd:cd03298 2 RLDKIRFSYgeqpmhfdltfAQGEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLING--VDVTAAPPA-DRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 345 DrkrDGIVPVMAVGKNITLaalnkftGGISQLDDAAEQKCILESI-QQLKVKTSSPDLAiGRLSGGNQQKAILARCLLLN 423
Cdd:cd03298 78 E---NNLFAHLTVEQNVGL-------GLSPGLKLTAEDRQAIEVAlARVGLAGLEKRLP-GELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-70 |
6.10e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 6.10e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 3 YLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiypHGSY---EGEIIFAGEEI 70
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAYkilEGDILFKGESI 73
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
277-485 |
6.19e-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: 61.18 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQAIAQGIAMVPEdrkrdgivpvma 356
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-QGEITLDG--VPVSDLEKALSSLISVLNQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 vgknitlaALNKFTGGISQlddaaeqkcilesiqqlkvktsspdlAIG-RLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:cd03247 83 --------RPYLFDTTLRN--------------------------NLGrRFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 436 IDIGAKYEIYKLINQlVQQGIAVIVISSELpevLGLS--DRVLVMHEGKLKA 485
Cdd:cd03247 129 LDPITERQLLSLIFE-VLKDKTLIWITHHL---TGIEhmDKILFLENGKIIM 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
277-483 |
7.57e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.90 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCQQAIAQGIAmvpedRKRDGIV-PVM 355
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-RGQVLIDG--VDIAKISDAELREVR-----RKKIAMVfQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 AVGKNITLAALNKFTGGISQLDDAAEQKCILESIQQLKVKTSS---PDlaigRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAhsyPD----ELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 433 TRGIDIGAKYEIY-KLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK10070 192 FSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-200 |
8.01e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.44 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIF-AGEEI----QASHI-----RDterkgiAII--- 86
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS--GRIARpAGARVlflpQRPYLplgtlRE------ALLypa 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 87 ------HQELAlvkelTVLENIFLGNEITHngimdydlmtLRCQKLLAQVslsispdtrvgdLGLGQQQLVEIAKALNKQ 160
Cdd:COG4178 451 taeafsDAELR-----EALEAVGLGHLAER----------LDEEADWDQV------------LSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1014292979 161 VRLLILDEPTASLTEQETSVLLDIIRDlQQHGIACIYISH 200
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-483 |
8.15e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKqvdIRNCQQAIAQGIAMvpEDRKRDGIV---- 352
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIE-IYDSKIKVDGK---VLYFGKDIFQIDAI--KLRKEVGMVfqqp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 ---PVMAVGKNItlaALNKFTGGISqlDDAAEQKCILESIQQLKV------KTSSPdlaIGRLSGGNQQKAILARCLLLN 423
Cdd:PRK14246 100 npfPHLSIYDNI---AYPLKSHGIK--EKREIKKIVEECLRKVGLwkevydRLNSP---ASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-221 |
8.67e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.83 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY--PHGSYE-GEIIFAGEEIQaSHIRDTERK-GIAIIHQELALV 93
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqpTEGKVTvGDIVVSSTSKQ-KEIKPVRKKvGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 KElTVLENIFLGNEitHNGIMDYDLMTLRCQKL----LAQVSLSISPdtrvGDLGLGQQQLVEIAKALNKQVRLLILDEP 169
Cdd:PRK13643 99 EE-TVLKDVAFGPQ--NFGIPKEKAEKIAAEKLemvgLADEFWEKSP----FELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 170 TASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
279-483 |
1.03e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLfGVWPGQWEGKIYIDGKQVDIRNcQQAIAQGIAMvpedRKRDGIV------ 352
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNHFDFSK-TPSDKAIREL----RRNVGMVfqqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 -PVMAVGKNITLAALNkftggISQLDDAAEQKCILESIQQLKVKtsspDLAiGR----LSGGNQQKAILARCLLLNPRIL 427
Cdd:PRK11124 94 wPHLTVQQNLIEAPCR-----VLGLSKDQALARAEKLLERLRLK----PYA-DRfplhLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 428 ILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-217 |
1.07e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIifageEIQASHIRDterkgiaiihqelalvkELTVL 99
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----DVPDNQFGR-----------------EASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 100 ENIFLGNEIThngimdyDLMtlrcqKLLAQVSLSISPD--TRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQE 177
Cdd:COG2401 104 DAIGRKGDFK-------DAV-----ELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1014292979 178 TSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRD 217
Cdd:COG2401 172 AKRVARNLQKLaRRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-219 |
1.08e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVL---CGIYPHG-SYEGEIIFAGEEI-QASHIRdtERKGIAIIHQELALVK 94
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKiKVDGKVLYFGKDIfQIDAIK--LRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 ELTVLENIflGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRV----GDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PRK14246 104 HLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspaSQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1014292979 171 ASLTEQETSVLLDIIRDLQQHgIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGE 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-483 |
1.12e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQQAIAQGIAMVPEdrkRDGIVPVMA 356
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLVGGK--DIETNLDAVRQSLGMCPQ---HNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITLAALNKftgGISQLDDAAEQKCILESIQ-QLKVKTSSPDLaigrlSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:TIGR01257 1020 VAEHILFYAQLK---GRSWEEAQLEMEAMLEDTGlHHKRNEEAQDL-----SGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 436 IDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-219 |
1.34e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.91 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGS-YEGEIIFAGEEIQASHIrdteRKGIAIIHQELALVKELTV 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEM----RAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 99 LENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGL------GQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkglsgGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 173 LTEQETSVLLDIIRDLQQHG-IACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
1.37e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKV---LCGIYPHGSYEGEIIFAGEEIQASHIRD 77
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TE-RKGIAIIHQELALVKELTVLENIFLGneITHNGIM-DYDLMTLRCQKLLAQVSLSISPDTRVGD----LGLGQQQLV 151
Cdd:PRK14267 81 IEvRREVGMVFQYPNPFPHLTIYDNVAIG--VKLNGLVkSKKELDERVEWALKKAALWDEVKDRLNDypsnLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 152 EIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHgIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
254-483 |
1.40e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.33 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 254 TGDEILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQWEGKIYIDgkqvdirncqQ 333
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD----------Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 334 AIAQGIAMVPED---RKRDGIV---PVM-----AVGKNITLAALNKftggisqlddAAEQKCILESIQQLKVKTSSPDLA 402
Cdd:PRK13645 74 AIPANLKKIKEVkrlRKEIGLVfqfPEYqlfqeTIEKDIAFGPVNL----------GENKQEAYKKVPELLKLVQLPEDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 403 IGR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLV 477
Cdd:PRK13645 144 VKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
....*.
gi 1014292979 478 MHEGKL 483
Cdd:PRK13645 224 MHEGKV 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-225 |
1.45e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.49 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 27 LNAGEIVSLCGENGSGKSTLMKVLCGIYPhgsYEGEIIFAGEEIQA------SHIR----DTERKGIAI-IHQELAL-VK 94
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLP---GSGSIQFAGQPLEAwsaaelARHRaylsQQQTPPFAMpVFQYLTLhQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 95 ELTVLENIflgneithngimdYDLMTLRCQKLLAQVSLSISpdtrVGDLGLGQQQLVEIA-------KALNKQVRLLILD 167
Cdd:PRK03695 96 DKTRTEAV-------------ASALNEVAEALGLDDKLGRS----VNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 168 EPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHI--GTRD 225
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLasGRRD 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-231 |
1.76e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 19 AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQashiRDTERKGIAIIHQELALVKELTV 98
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS--GKISILGQPTR----QALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 99 L-ENIFLGNEITHNGIM------DYDLMTlrcqKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:PRK15056 96 LvEDVVMMGRYGHMGWLrrakkrDRQIVT----AALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 172 SLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRdgqhiGTRDAAGMSE 231
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-----GTVLASGPTE 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-219 |
2.02e-10 |
|
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: 63.30 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 21 DNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEI----QAShirdtERKGIAIIHQELALVKEl 96
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTS--GRILIDGQDIrdvtQAS-----LRAAIGIVPQDTVLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 97 TVLENIFLGN-EITHNGIMDydlmTLRcqklLAQVSLSIS--PD---TRVGDLGL----GQQQLVEIAKALNKQVRLLIL 166
Cdd:COG5265 447 TIAYNIAYGRpDASEEEVEA----AAR----AAQIHDFIEslPDgydTRVGERGLklsgGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 167 DEPTASL---TEQEtsvLLDIIRDLQQHGIACIyISHKLNEVkAISDTICVIRDGQ 219
Cdd:COG5265 519 DEATSALdsrTERA---IQAALREVARGRTTLV-IAHRLSTI-VDADEILVLEAGR 569
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-219 |
2.05e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 59.00 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiyphgsyegeiifageeiqashiRDTERKGIA 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-----------------------ELEPDEGIV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQelalvkeltvleniflGNEITHngimdydlmtlrcqklLAQVSlsispdtrvGdlglGQQQLVEIAKALNKQVRLL 164
Cdd:cd03221 58 TWGS----------------TVKIGY----------------FEQLS---------G----GEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 165 ILDEPTASLtEQETSVLLdiIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03221 93 LLDEPTNHL-DLESIEAL--EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
279-486 |
2.19e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQweGKIYIDGKQVdirncQQAIAQG-IAMVPEDRKRDGIVPVMA 356
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGfVRLAS--GKISILGQPT-----RQALQKNlVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 -----VGKNITLAALNKFTGGISQLDDAAeqkciLESIQQLKVKTSSpdlaIGRLSGGNQQKAILARCLLLNPRILILDE 431
Cdd:PRK15056 98 edvvmMGRYGHMGWLRRAKKRDRQIVTAA-----LARVDMVEFRHRQ----IGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 432 PTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVlVMHEGKLKAN 486
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLAS 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
256-485 |
2.36e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPvNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW--PGQWEGKIYIDGKQVDIRNcqq 333
Cdd:PRK13640 3 DNIVEFKHVSFTYP-DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpDDNPNSKITVDGITLTAKT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 334 aiaqgiamVPEDRKRDGIV---P----VMA-VGKNITLAALNKftgGISQLDDAAEQKCILESIQQLKVKTSSPdlaiGR 405
Cdd:PRK13640 79 --------VWDIREKVGIVfqnPdnqfVGAtVGDDVAFGLENR---AVPRPEMIKIVRDVLADVGMLDYIDSEP----AN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVlGLSDRVLVMHEGKLK 484
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
.
gi 1014292979 485 A 485
Cdd:PRK13640 223 A 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-77 |
2.58e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 62.89 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKA--------IDnvcLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGEEIQASHI 75
Cdd:COG4615 328 LELRGVTYRYPGEDGdegftlgpID---LTIRRGELVFIVGGNGSGKSTLAKLLTGLYrPE---SGEILLDGQPVTADNR 401
|
..
gi 1014292979 76 RD 77
Cdd:COG4615 402 EA 403
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
3.14e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.19 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-P-HGSyegeiIFAGEEIQASHIRDTE----RKGIAIIHQ--E 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPtSGT-----VTIGERVITAGKKNKKlkplRKKVGIVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 90 LALVKElTVLENIFLGNeiTHNGIMDYDLMtLRCQKLLAQVSLSISPDTRVG-DLGLGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK13634 96 HQLFEE-TVEKDICFGP--MNFGVSEEDAK-QKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 169 PTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHIGT 223
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-483 |
3.51e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 3.51e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
277-510 |
4.66e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.04 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRT---ETIQCLFGVWPGqwegkiyidgkqvDIRNCQQAIAQgiAMVPEDRKRDGIV- 352
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKStllSLIQRHFDVSEG-------------DIRFHDIPLTK--LQLDSWRSRLAVVs 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 --PVM---AVGKNItlaALNKFTGGISQLDDAAEQKCILESIQQLKvktSSPDLAIGR----LSGGNQQKAILARCLLLN 423
Cdd:PRK10789 396 qtPFLfsdTVANNI---ALGRPDATQQEIEHVARLASVHDDILRLP---QGYDTEVGErgvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQgiAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQE-------- 495
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQsgwyrdmy 547
|
250
....*....|....*..
gi 1014292979 496 --QVMEAALRSEHHVEK 510
Cdd:PRK10789 548 ryQQLEAALDDAPEIRE 564
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-221 |
4.73e-10 |
|
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: 59.10 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKT-----FGSVKAI-DNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIqashIRDT 78
Cdd:cd03213 4 LSFRNLTVTvksspSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPL----DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 ERKGIAIIHQELALVKELTVLENIflgneithngimdydLMTLRCQkllaqvslSISpdtrvGdlglGQQQLVEIAKALN 158
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRETL---------------MFAAKLR--------GLS-----G----GERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKL-NEVKAISDTICVIRDGQHI 221
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-477 |
4.86e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 30 GEIVSLCGENGSGKSTLMKVLCG-IYPH-GSYEG-----EII--FAGEEIQaSHIRDTERKGIAIIH--QELAL------ 92
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGeLIPNlGDYEEepswdEVLkrFRGTELQ-NYFKKLYNGEIKVVHkpQYVDLipkvfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 93 --VKELtvLENIflgNEithNGIMDYDLMTLRCQKLLaqvslsispDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PRK13409 178 gkVREL--LKKV---DE---RGKLDEVVERLGLENIL---------DRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 171 ASLTEQETSVLLDIIRDLQQhGIACIYISHKLNEVKAISDTIcvirdgqHI--GTRDAAGmseddIITMMVG-RE----- 242
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNV-------HIayGEPGAYG-----VVSKPKGvRVginey 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 243 LTALYPNE--------------PHTTGDEIlriEHLTAWHPVnrhIKRVNDvsFSL-------KRGEILGIAGLVGAGRT 301
Cdd:PRK13409 308 LKGYLPEEnmrirpepiefeerPPRDESER---ETLVEYPDL---TKKLGD--FSLeveggeiYEGEVIGIVGPNGIGKT 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 302 ETIQCLFGVW-PGqwEGKIYIDGKqvdirncqqaiaqgIAMVPEDRKRDGIVPVMAVGKNITlaalnkftggiSQLDDAA 380
Cdd:PRK13409 380 TFAKLLAGVLkPD--EGEVDPELK--------------ISYKPQYIKPDYDGTVEDLLRSIT-----------DDLGSSY 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 381 EQKCI-----LESIQQLKVKTsspdlaigrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQ 454
Cdd:PRK13409 433 YKSEIikplqLERLLDKNVKD---------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeER 503
|
490 500
....*....|....*....|...
gi 1014292979 455 GIAVIVISSELPEVLGLSDRVLV 477
Cdd:PRK13409 504 EATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
219-483 |
4.88e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.76 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 219 QHIGTRDAAGMSEDDIITmmvgRELTALYPNEPHTTGDEI-LRIEHLTAWHPvNRHIKRVNDVSFSLKRGEILGIAGLVG 297
Cdd:PRK11160 302 QHLGQVIASARRINEITE----QKPEVTFPTTSTAAADQVsLTLNNVSFTYP-DQPQPVLKGLSLQIKAGEKVALLGRTG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 298 AGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNcQQAIAQGIAMVPE------DRKRDgivpvmavgkNITLAalnKFTG 371
Cdd:PRK11160 377 CGKSTLLQLLTRAWDPQ-QGEILLNGQPIADYS-EAALRQAISVVSQrvhlfsATLRD----------NLLLA---APNA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 372 GISQLDDAAEQ---KCILESIQQLkvktsspDLAIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEI 444
Cdd:PRK11160 442 SDEALIEVLQQvglEKLLEDDKGL-------NAWLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQI 514
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1014292979 445 YKLINQlVQQGIAVIVISSELpevLGLS--DRVLVMHEGKL 483
Cdd:PRK11160 515 LELLAE-HAQNKTVLMITHRL---TGLEqfDRICVMDNGQI 551
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-438 |
5.14e-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: 61.87 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 3 YLLEMKNITKTFGSVKAI-DNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAgeeiqashirdterK 81
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--DKDFNGEARPQ--------------P 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAI--IHQELALVKELTVLENIFLG-----------NEITHN-------------------GIMD-YDLMTLRCQKLLA 128
Cdd:TIGR03719 67 GIKVgyLPQEPQLDPTKTVRENVEEGvaeikdaldrfNEISAKyaepdadfdklaaeqaelqEIIDaADAWDLDSQLEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 129 QVSLSISP-DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLtEQETSVLLDiiRDLQQHGIACIYISHK---LNE 204
Cdd:TIGR03719 147 MDALRCPPwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL-DAESVAWLE--RHLQEYPGTVVAVTHDryfLDN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 205 V-----------------------------------------KAISDTICVIRDG---------------QHIGTRDAAG 228
Cdd:TIGR03719 224 VagwileldrgrgipwegnysswleqkqkrleqeekeesarqKTLKRELEWVRQSpkgrqakskarlaryEELLSQEFQK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 229 MSEDDIITMMVGRELtalypnephttGDEILRIEHLTawhpvnrhiKR------VNDVSFSLKRGEILGIAGLVGAGRTE 302
Cdd:TIGR03719 304 RNETAEIYIPPGPRL-----------GDKVIEAENLT---------KAfgdkllIDDLSFKLPPGGIVGVIGPNGAGKST 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 303 tiqcLFGVWPGQWE---GKIYIdGKQVDirncqqaiaqgIAMVpeDRKRDGIVP-------------VMAVGKNIT---- 362
Cdd:TIGR03719 364 ----LFRMITGQEQpdsGTIEI-GETVK-----------LAYV--DQSRDALDPnktvweeisggldIIKLGKREIpsra 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 363 -LAALNkFTGGisqlDdaaeqkcilesiQQLKVktsspdlaiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:TIGR03719 426 yVGRFN-FKGS----D------------QQKKV---------GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
280-500 |
5.63e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.19 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 280 VSFSLKRGEILGIAGLVGAGRTeTIQCLFGVWPGQWEGKIYIDGKQVDIRNcQQAIAQGIAMVPED-RKRDGIV--PVMA 356
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQQlPAAEGMTvrELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITLAALNKFTggisqlddAAEQKCILESIQQLKVKTSSPDLaIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:PRK10575 108 IGRYPWHGALGRFG--------AADREKVEEAISLVGLKPLAHRL-VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 437 DIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQEQVMEA 500
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
404-485 |
6.02e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGK 206
|
...
gi 1014292979 483 LKA 485
Cdd:PRK11144 207 VKA 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
280-459 |
7.32e-10 |
|
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: 58.66 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 280 VSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRncQQAIAQGIAMVPEdrkRDGIVPVMAVGK 359
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-AGRVLLNGGPLDFQ--RDSIARGLLYLGH---APGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 360 NIT-LAALNkftggisqlDDAAeqkcILESIQQLKVkTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:cd03231 93 NLRfWHADH---------SDEQ----VEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|.
gi 1014292979 439 GAKYEIYKLINQLVQQGIAVI 459
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVV 179
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
405-494 |
7.68e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKl 483
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR- 234
|
90
....*....|.
gi 1014292979 484 kanLINHNLTQ 494
Cdd:PRK15134 235 ---CVEQNRAA 242
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
376-501 |
8.92e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 376 LDDAAEQKCILESIQQlKVKTSSPDLAIGrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQG 455
Cdd:PRK14239 121 LDEAVEKSLKGASIWD-EVKDRLHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1014292979 456 IAVIVISSeLPEVLGLSDRVLVMHEGklkaNLINHNLTQEQVMEAA 501
Cdd:PRK14239 199 TMLLVTRS-MQQASRISDRTGFFLDG----DLIEYNDTKQMFMNPK 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
277-482 |
1.00e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.35 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTeTIQCLFGVWPGQWEGKIYIDGkqvdirncqqaiaQGIAMVPEDrKRD------- 349
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIAGFETPDSGRIMLDG-------------QDITHVPAE-NRHvntvfqs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 350 -GIVPVMAVGKNI-----------------TLAALNkftggISQLDDAAEQKcilesIQQLkvktsspdlaigrlSGGNQ 411
Cdd:PRK09452 95 yALFPHMTVFENVafglrmqktpaaeitprVMEALR-----MVQLEEFAQRK-----PHQL--------------SGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 412 QKAILARCLLLNPRILILDEPTRGIDigakyeiYKL-------INQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALD-------YKLrkqmqneLKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-219 |
1.06e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTERKgIA 84
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT--PAHGHVWLDGEHIQHYASKEVARR-IG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGnEITHNGIM------DYDLMTlrcqKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK10253 85 LLAQNATTPGDITVQELVARG-RYPHQPLFtrwrkeDEEAVT----KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 159 KQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGK 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-221 |
1.15e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.64 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 12 KTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQAS--HIRDTE--RKGIAIIH 87
Cdd:PRK13645 19 KTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLII--SETGQTIVGDYAIPANlkKIKEVKrlRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 88 Q--ELALVKElTVLENIFLGNeiTHNGiMDYDLMTLRCQKLLAQVSLSISPDTRVG-DLGLGQQQLVEIAKALNKQVRLL 164
Cdd:PRK13645 97 QfpEYQLFQE-TIEKDIAFGP--VNLG-ENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-221 |
1.37e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.04 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 8 KNITKTFGS----VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPH-GSYEGEIIFAGEEIQASHirDTERKG 82
Cdd:cd03233 7 RNISFTTGKgrskIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNGIPYKEFA--EKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 83 IAIIHQELALVKELTVLEniflgneithngIMDYdlmTLRCQKllAQVSLSISPdtrvgdlglGQQQLVEIAKALNKQVR 162
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRE------------TLDF---ALRCKG--NEFVRGISG---------GERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 163 LLILDEPTASLteqETSVLLDIIRDLQQhgiaciyISHKLNEVKAIS------------DTICVIRDGQHI 221
Cdd:cd03233 139 VLCWDNSTRGL---DSSTALEILKCIRT-------MADVLKTTTFVSlyqasdeiydlfDKVLVLYEGRQI 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
273-483 |
1.41e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.71 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 273 HIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwPGQWEGKIYIDGKQVDirncqqaiaqgiAMVPEDRkRDGIV 352
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTDVS------------RLHARDR-KVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 -------PVMAVGKNITLaalnkftgGISQL-------DDAAEQK--CILESIQQLKVKTSSPdlaiGRLSGGNQQKAIL 416
Cdd:PRK10851 80 fqhyalfRHMTVFDNIAF--------GLTVLprrerpnAAAIKAKvtQLLEMVQLAHLADRYP----AQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
279-502 |
1.42e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVW-PGqwEGKIYIDGKQVDIRNCQqAIAQGIAMVpedrkrdGIVPVM-- 355
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPT--GGQVLLDGVPLVQYDHH-YLHRQVALV-------GQEPVLfs 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 356 -AVGKNITLAaLNKFTggISQLDDAAEQKCILESIQQLkvkTSSPDLAIG----RLSGGNQQKAILARCLLLNPRILILD 430
Cdd:TIGR00958 569 gSVRENIAYG-LTDTP--DEEIMAAAKAANAHDFIMEF---PNGYDTEVGekgsQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 431 EPTRGIDIGAKYEIYKLINqlvQQGIAVIVISSELPEVLGlSDRVLVMHEGKLKANLINHNLTQEQVMEAAL 502
Cdd:TIGR00958 643 EATSALDAECEQLLQESRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
259-478 |
1.50e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 58.72 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVdirncqqaiaQ 337
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPAlQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-SGEITLDGVPV----------T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GiamvP-EDR----KRDGIVPVMAVGKNITLAAlnKFTGgisqLDDAAEQKCILESIQQLKVKtsspDLA---IGRLSGG 409
Cdd:COG4525 73 G----PgADRgvvfQKDALLPWLNVLDNVAFGL--RLRG----VPKAERRARAEELLALVGLA----DFArrrIWQLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 410 NQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVM 478
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVM 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
258-483 |
1.53e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.85 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPVNrhIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqvdIRNCQQAIAQ 337
Cdd:PRK13644 1 MIRLENVSYSYPDG--TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSG----IDTGDFSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIamvpedRKRDGIV----PVMAVGK-----------NITLAALNkftggISQLDDAAeqkciLESIQQLKVKTSSPDla 402
Cdd:PRK13644 74 GI------RKLVGIVfqnpETQFVGRtveedlafgpeNLCLPPIE-----IRKRVDRA-----LAEIGLEKYRHRSPK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 403 igRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEvLGLSDRVLVMHEGK 482
Cdd:PRK13644 136 --TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGK 212
|
.
gi 1014292979 483 L 483
Cdd:PRK13644 213 I 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
274-482 |
1.64e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.66 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 274 IKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPG--QWEGKIYIDGKQVDIrNCQQAIAQgIAMVPEDrkrDGI 351
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPYKE-FAEKYPGE-IIYVSEE---DVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 352 VPVMAVGKNITLAAL---NKFTGGISqlddaaeqkcilesiqqlkvktsspdlaigrlsGGNQQKAILARCLLLNPRILI 428
Cdd:cd03233 95 FPTLTVRETLDFALRckgNEFVRGIS---------------------------------GGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 429 LDEPTRGIDIGAKYEIYKLINQLVQQ--GIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGR 197
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-240 |
1.91e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-----IYPHG-SYEGEIIFAGEEIQASHIRDTERKGiAIIHQELALV 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltggGAPRGaRVTGDVTLNGEPLAAIDAPRLARLR-AVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 94 KELTVLENIFLG--------NEITHN--GIMDYDLMTLRCQKLLAQvslsispdtRVGDLGLGQQQLVEIAKALNK---- 159
Cdd:PRK13547 96 FAFSAREIVLLGrypharraGALTHRdgEIAWQALALAGATALVGR---------DVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 160 -----QVRLLILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDD 233
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPA 246
|
....*..
gi 1014292979 234 IITMMVG 240
Cdd:PRK13547 247 HIARCYG 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-254 |
2.20e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.12 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGS---YEGEIIFAGEEIQASHIR-DTER 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrVEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKeLTVLENIFLGNEITH-------NGIMDydlMTLRCQKLLAQVSLSISPDTRvgDLGLGQQQLVEI 153
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpkleiDDIVE---SALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 154 AKALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQ-QHGIACIYISHKLNEVKAISDTICVIRdgqhigtrdaagmSED 232
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFK-------------GNE 228
|
250 260
....*....|....*....|..
gi 1014292979 233 DIITMMVGRELTALYPNEPHTT 254
Cdd:PRK14258 229 NRIGQLVEFGLTKKIFNSPHDS 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
279-484 |
2.26e-09 |
|
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: 59.82 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwpGQWE---GKI-----------YIDGKQVDIRNCQQAiaqGIAMVPE 344
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEptsGRIiyhvalcekcgYVERPSKVGEPCPVC---GGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 345 DRkrDGIVPVMAVGKNIT--LAALNKFTGGISQLDDAAEQkcILESIQQL----------------KVKTSSPDLAIGR- 405
Cdd:TIGR03269 93 EV--DFWNLSDKLRRRIRkrIAIMLQRTFALYGDDTVLDN--VLEALEEIgyegkeavgravdlieMVQLSHRITHIARd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLG-LSDRVLVMHEGKLK 484
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENGEIK 248
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
279-487 |
2.52e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.52 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFG---------VWPGQWEGKIYIDGKqVDIRNCQQA-IAQGIAMVPEdrkr 348
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGldtptsgdvIFNGQPMSKLSSAAK-AELRNQKLGfIYQFHHLLPD---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 349 dgivpvMAVGKNITLAALnkftggISQLDDAAEQKCILESIQQLKVKTSSPDLAiGRLSGGNQQKAILARCLLLNPRILI 428
Cdd:PRK11629 102 ------FTALENVAMPLL------IGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 429 LDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELpEVLGLSDRVLVMHEGKLKANL 487
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAEL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
281-502 |
2.57e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.67 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 281 SFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvdirNCQqaiaqgiAMVPEDR------KRDGIVPV 354
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGQ-----DHT-------TTPPSRRpvsmlfQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 355 MAVGKNITLaalnkftgGISQ-LDDAAEQKCILESI-QQLKVKTSSPDLAiGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:PRK10771 86 LTVAQNIGL--------GLNPgLKLNAAQREKLHAIaRQMGIEDLLARLP-GQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 433 TRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQEQVMEAAL 502
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCqERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
259-483 |
2.88e-09 |
|
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: 59.75 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNC-QQAIAQ 337
Cdd:TIGR01193 474 IVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGF--SLKDIdRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 GIAMVPEDrkrdgivPVMAVG---KNITLAALNKFTggISQLDDAAEQKCILESIQQLKVKTSSpDLAI--GRLSGGNQQ 412
Cdd:TIGR01193 549 FINYLPQE-------PYIFSGsilENLLLGAKENVS--QDEIWAACEIAEIKDDIENMPLGYQT-ELSEegSSISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKliNQLVQQGIAVIVISSELpEVLGLSDRVLVMHEGKL 483
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVN--NLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
406-485 |
3.08e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
277-482 |
3.54e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqvdirncqqaiaQGIAMVPEDRK-------RD 349
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT-AGQIMLDG-------------VDLSHVPPYQRpinmmfqSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 350 GIVPVMAVGKNITLAaLNKFTGGISQLDDAAEQKCILESIQQLKVKTSSpdlaigRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK11607 101 ALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPH------QLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 430 DEPTRGIDIGAKYEI-YKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK11607 174 DEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
259-483 |
3.97e-09 |
|
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: 56.38 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAwhPVN-RHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwPGQ--WEGKIYIDGKqvDIrncqqai 335
Cdd:cd03217 1 LEIKDLHV--SVGgKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYevTEGEILFKGE--DI------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 aqgIAMVPEDRKRDGIvpvmavgkniTLAALNKftggisqlddaaeqkcilESIQQLKVKTSSPDLAIGrLSGGNQQKAI 415
Cdd:cd03217 67 ---TDLPPEERARLGI----------FLAFQYP------------------PEIPGVKNADFLRYVNEG-FSGGEKKRNE 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIsSELPEVLGL--SDRVLVMHEGKL 483
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDYikPDRVHVLYDGRI 183
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-173 |
4.72e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 26 RLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIifageEIQASHIRDTER-KGIAIIHQELALVKELTVLENI-F 103
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVES--GQI-----QIDGKTATRGDRsRFMAYLGHLPGLKADLSTLENLhF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 104 LgneithNGIMDYdlmtlRCQKL----LAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASL 173
Cdd:PRK13543 106 L------CGLHGR-----RAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
406-483 |
5.98e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 5.98e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
259-482 |
6.26e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.61 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAwHPVNRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwPGQ--WEGKIYIDGKqvDIrncqqaia 336
Cdd:COG0396 1 LEIKNLHV-SVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYevTSGSILLDGE--DI-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 qgIAMVPEDRKRDGI-------VPVMAVgKNITL--AALNKFTGgiSQLDDAAEQKCILESIQQLKVKTS--SPDLAIGr 405
Cdd:COG0396 67 --LELSPDERARAGIflafqypVEIPGV-SVSNFlrTALNARRG--EELSAREFLKLLKEKMKELGLDEDflDRYVNEG- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIsSELPEVLGL--SDRVLVMHEGK 482
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILII-THYQRILDYikPDFVHVLVDGR 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-477 |
7.11e-09 |
|
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: 58.26 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 30 GEIVSLCGENGSGKSTLMKVLCG-IYPH-GSYEG-----EII--FAGEEIQaSHIRDTERKGIAIIH--QELAL------ 92
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGeLKPNlGDYDEepswdEVLkrFRGTELQ-DYFKKLANGEIKVAHkpQYVDLipkvfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 93 --VKELtvLENIflgNEithNGIMDYdlmtlrcqkLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:COG1245 178 gtVREL--LEKV---DE---RGKLDE---------LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 171 ASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTIcvirdgqHI--GTRDAAGmseddIITMMVG-RE----- 242
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYV-------HIlyGEPGVYG-----VVSKPKSvRVginqy 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 243 LTALYPNE--------------PHT---TGDEILRIEHLTawhpvnrhiKRVNDvsFSL-------KRGEILGIAGLVGA 298
Cdd:COG1245 309 LDGYLPEEnvrirdepiefevhAPRrekEEETLVEYPDLT---------KSYGG--FSLeveggeiREGEVLGIVGPNGI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 299 GRTETIQCLFGVW-PGqwEGKIYIDGKqvdirncqqaiaqgIAMVPEDRKRDGIVPVMAVGKNitlAALNKFTGGISQLD 377
Cdd:COG1245 378 GKTTFAKILAGVLkPD--EGEVDEDLK--------------ISYKPQYISPDYDGTVEEFLRS---ANTDDFGSSYYKTE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 378 DAaeQKCILESIQQLKVKTsspdlaigrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGI 456
Cdd:COG1245 439 II--KPLGLEKLLDKNVKD---------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGK 507
|
490 500
....*....|....*....|.
gi 1014292979 457 AVIVISSELPEVLGLSDRVLV 477
Cdd:COG1245 508 TAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-195 |
8.65e-09 |
|
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: 55.33 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 20 IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEiqashIRDTERKGIAIIHQELALVKELTVL 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRP-----LDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 100 EniflgneithngimdydlmtlrcqkllaqvSLSISPDTRvgDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETS 179
Cdd:cd03232 98 E------------------------------ALRFSALLR--GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170
....*....|....*...
gi 1014292979 180 VLLDIIRDLQQHG--IAC 195
Cdd:cd03232 146 NIVRFLKKLADSGqaILC 163
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-219 |
8.79e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 19 AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAG-EEIQASHIRDTERK-GIAIIHQELALVKE 95
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPS---EGKVYVDGlDTSDEENLWDIRNKaGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 96 LtVLENIFLGNEithNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:PRK13633 102 I-VEEDVAFGPE---NLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1014292979 176 QETSVLLDIIRDL-QQHGIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13633 178 SGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-205 |
8.94e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 22 NVCLRLNAGEIVSLCGENGSGKSTLmkVLCGIYPHGSYEGEIIFAGEEIQASHIRDTeRKGIAIIHQELALVKELTVL-- 99
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDPVLFSGSLRMnl 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 100 --------ENIFLGNEITHNgimdYDLMTLRCQKLLAQVSLSISpdtrvgDLGLGQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:TIGR00957 1381 dpfsqysdEEVWWALELAHL----KTFVSALPDKLDHECAEGGE------NLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190
....*....|....*....|....*....|....
gi 1014292979 172 SLTEQETSVLLDIIRDlQQHGIACIYISHKLNEV 205
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTI 1483
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
406-485 |
9.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.57 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGKLK 484
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
.
gi 1014292979 485 A 485
Cdd:PRK13634 226 L 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
406-476 |
9.32e-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: 54.47 E-value: 9.32e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvqqGIAVIVISSElPEVLGLSDRVL 476
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR-PSLWKFHDRVL 158
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
406-483 |
1.26e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 1.26e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-169 |
1.36e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTERKgI 83
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRGSGETIWDIKKH-I 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKEL-TVLENIFLGNEITHNGImdYDLMTLRcQKLLAQVSLSI-SPDTRVGD-----LGLGQQQLVEIAKA 156
Cdd:PRK10938 339 GYVSSSLHLDYRVsTSVRNVILSGFFDSIGI--YQAVSDR-QQKLAQQWLDIlGIDKRTADapfhsLSWGQQRLALIVRA 415
|
170
....*....|...
gi 1014292979 157 LNKQVRLLILDEP 169
Cdd:PRK10938 416 LVKHPTLLILDEP 428
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
256-460 |
1.44e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.94 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 256 DEILRIEHLTAWHPVNRHIKrvnDVSFSLKRGEILGIAGLVGAGRTETIQC---LFGVWPG-QWEGKIYIDGKQVdirnc 331
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfRVEGKVTFHGKNL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 332 qqaIAQGIAMVpEDRKRDGIV-----PV-MAVGKNITLAA-LNKFTGGISQLDDAAEQKCILESIQQLKVKTSSpdLAig 404
Cdd:PRK14243 80 ---YAPDVDPV-EVRRRIGMVfqkpnPFpKSIYDNIAYGArINGYKGDMDELVERSLRQAALWDEVKDKLKQSG--LS-- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 405 rLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIV 460
Cdd:PRK14243 152 -LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
259-459 |
1.45e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.18 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTawhpVNRHIKR-VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPG--QWEGKIYIDGKQVDirnCQQAI 335
Cdd:COG4136 2 LSLENLT----ITLGGRPlLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafSASGEVLLNGRRLT---ALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 AQGIAMVPEDrkrDGIVPVMAVGKNITLAALNKFTGgiSQLDDAAEQkcILESIQQLKVKTSSPDlaigRLSGGNQQKAI 415
Cdd:COG4136 75 QRRIGILFQD---DLLFPHLSVGENLAFALPPTIGR--AQRRARVEQ--ALEEAGLAGFADRDPA----TLSGGQRARVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1014292979 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLI-NQLVQQGIAVI 459
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPAL 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-240 |
1.70e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 21 DNVCLRlNAGEIvSLCGENGSGK-STLMKvlcgiyphgsYEGEIIFAGEEIQASHIRDTeRKGIAIIHQELALVKeLTVL 99
Cdd:PTZ00265 1248 QNVGMK-NVNEF-SLTKEGGSGEdSTVFK----------NSGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLFN-MSIY 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 100 ENIFLGNEithngimDYDLMTLRCQKLLAQV-----SLSISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PTZ00265 1314 ENIKFGKE-------DATREDVKRACKFAAIdefieSLPNKYDTNVGPYGKslsgGQKQRIAIARALLREPKILLLDEAT 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 171 ASLTEQETSVLLDIIRDLQQHG-IACIYISHKLNEVKAiSDTICVIRDGQHIGTRDAAGMSEDDIITMMVG 240
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFNNPDRTGSFVQAHGTHEELLSVQDG 1456
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-224 |
2.03e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 19 AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGeeIQASHIR-DTERKGIAIIHQELALVKElT 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF--DVSEGDIRFHD--IPLTKLQlDSWRSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 98 VLENIFLGN------EITHNGimdydlmtlrcqkLLAQVSLSI-----SPDTRVGDLGL----GQQQLVEIAKALNKQVR 162
Cdd:PRK10789 405 VANNIALGRpdatqqEIEHVA-------------RLASVHDDIlrlpqGYDTEVGERGVmlsgGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 163 LLILDEPTASL---TEQEtsvlldIIRDLQQ--HGIACIYISHKLNEVKAiSDTICVIRDGqHIGTR 224
Cdd:PRK10789 472 ILILDDALSAVdgrTEHQ------ILHNLRQwgEGRTVIISAHRLSALTE-ASEILVMQHG-HIAQR 530
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
404-486 |
2.16e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVMHEGKL 483
Cdd:PRK10535 143 SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
...
gi 1014292979 484 KAN 486
Cdd:PRK10535 222 VRN 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
280-468 |
2.23e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 54.29 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 280 VSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvDIRNCQQAIAQGIAMVPEdrkRDGIVPVMAVGK 359
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD-SGEVRWNGT--PLAEQRDEPHENILYLGH---LPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 360 NITLaaLNKFTGGisqlddaaEQKCILESIQQLKVkTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIG 439
Cdd:TIGR01189 93 NLHF--WAAIHGG--------AQRTIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|
gi 1014292979 440 AKYEIYKLINQ-LVQQGIAVIVISSELPEV 468
Cdd:TIGR01189 162 GVALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-218 |
2.38e-08 |
|
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: 54.64 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 13 TFGS-VKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiyPHGSYEGEIIFAG---EEIQASHIRDTERKGIAIIHQ 88
Cdd:cd03290 9 SWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNkneSEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 89 ELALVKElTVLENIFLGNEITHNgimDYDLMTLRCQkllAQVSLSISP---DTRVGDLGL----GQQQLVEIAKALNKQV 161
Cdd:cd03290 87 KPWLLNA-TVEENITFGSPFNKQ---RYKAVTDACS---LQPDIDLLPfgdQTEIGERGInlsgGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 162 RLLILDEPTASLTEQETSVLLD--IIRDLQQHGIACIYISHKLNEVKAiSDTICVIRDG 218
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
405-483 |
2.69e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.76 E-value: 2.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-483 |
2.72e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 344 EDRKRDGIV-------PVMAVGKNITLAA-LNKFTGGISQLDDAAE---QKCILESiqqlKVKTSSPDLAiGRLSGGNQQ 412
Cdd:PRK14267 82 EVRREVGMVfqypnpfPHLTIYDNVAIGVkLNGLVKSKKELDERVEwalKKAALWD----EVKDRLNDYP-SNLSGGQRQ 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVMHEGKL 483
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSP-AQAARVSDYVAFLYLGKL 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
278-482 |
2.74e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.09 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDiRNCQQAIAQGIAMVPEDRKRdGIVPVMAV 357
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-SGSILIDGKDVT-KLPEYKRAKYIGRVFQDPMM-GTAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 358 GKNITLAAL----NKFTGGISQlDDAAEQKCILESI-----QQLKVKtsspdlaIGRLSGGNQQKAILARCLLLNPRILI 428
Cdd:COG1101 100 EENLALAYRrgkrRGLRRGLTK-KRRELFRELLATLglgleNRLDTK-------VGLLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 429 LDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKIVEeNNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
277-485 |
2.84e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 54.46 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIrncqqaIAQGIAMVPEDRKRDgivpvma 356
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP-PDSGTVTVRGRVSSL------LGLGGGFNPELTGRE------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 vgkNITLAALNKftgGISQ-LDDAAEQKCI----LESIQQLKVKTSSpdlaigrlSGgnqQKAILARCL--LLNPRILIL 429
Cdd:cd03220 104 ---NIYLNGRLL---GLSRkEIDEKIDEIIefseLGDFIDLPVKTYS--------SG---MKARLAFAIatALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 430 DEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
259-482 |
3.22e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLTAWHPVnrhiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQWegKIY--------IDGKQVDIRN 330
Cdd:PRK15093 9 LTIEFKTSDGWV----KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNW--RVTadrmrfddIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 331 CQQAIAQGIAMVPEDrKRDGIVPVMAVGKNITLAALN-KFTGGISQLDDAAEQKCIlESIQQLKVK------TSSPdlai 403
Cdd:PRK15093 83 RRKLVGHNVSMIFQE-PQSCLDPSERVGRQLMQNIPGwTYKGRWWQRFGWRKRRAI-ELLHRVGIKdhkdamRSFP---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGK 482
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
271-485 |
3.25e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 271 NRHIkrVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQV---------DIRNCQQAIAQGIAM 341
Cdd:PRK11831 19 NRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGENIpamsrsrlyTVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 342 VPEdrkrdgivpvMAVGKNITLAaLNKFTggisQLDDAaeqkcILESIQQLKVKT----SSPDLAIGRLSGGNQQKAILA 417
Cdd:PRK11831 96 FTD----------MNVFDNVAYP-LREHT----QLPAP-----LLHSTVMMKLEAvglrGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-191 |
3.36e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.34 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 27 LNAGEIVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIifageeiqashirDTERKGIAIIHQELALVKELTVLEniFLG 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGvLKPD---EGDI-------------EIELDTVSYKPQYIKADYEGTVRD--LLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 106 NEITHNGIMDY---DLMT-LRCQKLLaqvslsispDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVL 181
Cdd:cd03237 84 SITKDFYTHPYfktEIAKpLQIEQIL---------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170
....*....|
gi 1014292979 182 LDIIRDLQQH 191
Cdd:cd03237 155 SKVIRRFAEN 164
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
274-485 |
4.82e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 274 IKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQaIAQGIAMV---PEDRkrdg 350
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT-SGSVLIRGEPITKENIRE-VRKFVGLVfqnPDDQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 351 iVPVMAVGKNITLAALNKftggisQLDDAAEQKCILESIQQLKVKTSSpDLAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK13652 91 -IFSPTVEQDIAFGPINL------GLDEETVAHRVSSALHMLGLEELR-DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-219 |
5.07e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 30 GEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTerkgiAIIHQELALVKELTVLENIFLGNEIT 109
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRT-----GFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 110 HNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGD-----LGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDI 184
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190
....*....|....*....|....*....|....*.
gi 1014292979 185 IRDLQQHGIACIYISHK-LNEVKAISDTICVIRDGQ 219
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
279-488 |
5.30e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQV------DIRNcqqaiaqGIAMVPEDrkrdgiv 352
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDGLNIakiglhDLRF-------KITIIPQD------- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 353 PVMAVGK------------------NITLAALNKFtggISQLDDAAEQKCIlESIQQLKVktsspdlaigrlsgGNQQKA 414
Cdd:TIGR00957 1369 PVLFSGSlrmnldpfsqysdeevwwALELAHLKTF---VSALPDKLDHECA-EGGENLSV--------------GQRQLV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 415 ILARCLLLNPRILILDEPTRGIDIgakyEIYKLINQLVQ---QGIAVIVISSELPEVLGLSdRVLVMHEGKLK-----AN 486
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDL----ETDNLIQSTIRtqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAefgapSN 1505
|
..
gi 1014292979 487 LI 488
Cdd:TIGR00957 1506 LL 1507
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
406-462 |
5.95e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 51.68 E-value: 5.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAkyeIYKLINQLVQQGIAVIVIS 462
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVS 124
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
406-507 |
6.50e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.53 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGklk 484
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCG--- 235
|
90 100
....*....|....*....|....*...
gi 1014292979 485 anlinhnltqeQVMEAA-----LRSEHH 507
Cdd:COG4170 236 -----------QTVESGpteqiLKSPHH 252
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
258-481 |
7.80e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPVNRHIKrvnDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAIaq 337
Cdd:PRK11248 1 MLQISHLYADYGGKPALE---DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAERGV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 338 giamVPEDrkrDGIVPVMAVGKNItlaALNKFTGGISQlddaaEQKciLESIQQLKVKTsspDLA------IGRLSGGNQ 411
Cdd:PRK11248 75 ----VFQN---EGLLPWRNVQDNV---AFGLQLAGVEK-----MQR--LEIAHQMLKKV---GLEgaekryIWQLSGGQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 412 QKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:PRK11248 135 QRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQeTGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
375-438 |
8.84e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 8.84e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 375 QLDDAaeqkcILESIQQLKVktsSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:PRK11147 134 QLENR-----INEVLAQLGL---DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-219 |
9.67e-08 |
|
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: 52.61 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 37 GENGSGKSTLMK-VLCGIYPHGSYEGEIIFAGEEIqashIRDTERKGIAIIHQELALVKELTVLE--NIFLGNEITHNGI 113
Cdd:cd03240 29 GQNGAGKTTIIEaLKYALTGELPPNSKGGAHDPKL----IREGEVRAQVKLAFENANGKKYTITRslAILENVIFCHQGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 114 MDYDL--MTLRC---QKLLAqvSLSIspdtRVGdlglgqqqlveIAKALNKQVRLLILDEPTASLTEQE-TSVLLDIIRD 187
Cdd:cd03240 105 SNWPLldMRGRCsggEKVLA--SLII----RLA-----------LAETFGSNCGILALDEPTTNLDEENiEESLAEIIEE 167
|
170 180 190
....*....|....*....|....*....|...
gi 1014292979 188 LQQHGI-ACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03240 168 RKSQKNfQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-219 |
9.87e-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: 52.47 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVK-----AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGeeiqashirdte 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK--LSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 rkGIAIIHQElALVKELTVLENIFLGNEITHngiMDYDlMTLRCQKLlaQVSLSISPD---TRVGDLGL----GQQQLVE 152
Cdd:cd03250 67 --SIAYVSQE-PWIQNGTIRENILFGKPFDE---ERYE-KVIKACAL--EPDLEILPDgdlTEIGEKGInlsgGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 153 IAKALNKQVRLLILDEPTASLtEQETSVLL--DIIRDLQQHGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAV-DAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
277-459 |
1.19e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQvdirncqqaiaqgIAMVPEDRKRDGI----- 351
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT-SGTLLFEGED-------------ISTLKPEIYRQQVsycaq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 352 VPVM---AVGKNItlaalnKFTGGISQldDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILI 428
Cdd:PRK10247 89 TPTLfgdTVYDNL------IFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|..
gi 1014292979 429 LDEPTRGIDIGAKYEIYKLINQLV-QQGIAVI 459
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVrEQNIAVL 192
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
280-483 |
1.21e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 280 VSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGkqVDIRNCqqaiaqGIAmvpEDRKRDGIVPVMAVgk 359
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-RGRILIDG--CDISKF------GLM---DLRKVLGIIPQAPV-- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 360 nitlaalnKFTGGIS-QLDDAAEQKC--ILESIQQLKVKTSSPDLAIG----------RLSGGNQQKAILARCLLLNPRI 426
Cdd:PLN03130 1324 --------LFSGTVRfNLDPFNEHNDadLWESLERAHLKDVIRRNSLGldaevseageNFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 427 LILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGKL 483
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEF-KSCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-232 |
1.24e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAID---NVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIfageeIQASH-IRDTE- 79
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDII-----INDSHnLKDINl 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 ---RKGIAIIHQE---------------LALVKELTVLENIF--------------------------------LGNEIT 109
Cdd:PTZ00265 456 kwwRSKIGVVSQDpllfsnsiknnikysLYSLKDLEALSNYYnedgndsqenknkrnscrakcagdlndmsnttDSNELI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 110 H-----NGIMDYDLMTLRcQKLLAQVSLSISPD---TRVGD----LGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQE 177
Cdd:PTZ00265 536 EmrknyQTIKDSEVVDVS-KKVLIHDFVSALPDkyeTLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 178 TSVLLDIIRDLQ-QHGIACIYISHKLNEVKaISDTICVIRDGQHIGTRDAAGMSED 232
Cdd:PTZ00265 615 EYLVQKTINNLKgNENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGED 669
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-234 |
1.37e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 53.47 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGeIVSLCGENGSGKSTLMKVLCGIYPHGSYEG-------------------EIIFAG--EEIQASHIR 76
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKfdeedfylgddpdlpeieiELTFGSllSRLLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 77 DTERKGIAIIHQEL--ALVKELTVLENIF--LGNEITHNGIMDYDLMTLRCQKLLAQVSLSIS--PDTRVGDLGLGQQQL 150
Cdd:COG3593 91 EEDKEELEEALEELneELKEALKALNELLseYLKELLDGLDLELELSLDELEDLLKSLSLRIEdgKELPLDRLGSGFQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 151 VEIA-------KALNKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHK---LNEVKaISDTICVIRDGQH 220
Cdd:COG3593 171 ILLAllsalaeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSphlLSEVP-LENIRRLRRDSGG 249
|
250
....*....|....
gi 1014292979 221 IGTRDAAGMSEDDI 234
Cdd:COG3593 250 TTSTKLIDLDDEDL 263
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-214 |
1.61e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKaidnvcLR-----LNAGEIVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIifageeiqashirD 77
Cdd:PRK13409 340 LVEYPDLTKKLGDFS------LEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPD---EGEV-------------D 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERKgIAIIHQELALVKELTV---LENI-------FLGNEITHngimdydlmTLRCQKLLaqvslsispDTRVGDLGLGQ 147
Cdd:PRK13409 398 PELK-ISYKPQYIKPDYDGTVedlLRSItddlgssYYKSEIIK---------PLQLERLL---------DKNVKDLSGGE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1014292979 148 QQLVEIAKALNKQVRLLILDEPTASL-TEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICV 214
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLdVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-170 |
1.98e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFaGEEIQASHIrDTERKGIA 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDS--GTIKI-GETVKLAYV-DQSRDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 iihqelalvKELTVLENIFLGNEITHNGimDYDlMTLRC------------QKllaqvslsispdtRVGDLGLGQQQLVE 152
Cdd:PRK11819 401 ---------PNKTVWEEISGGLDIIKVG--NRE-IPSRAyvgrfnfkggdqQK-------------KVGVLSGGERNRLH 455
|
170
....*....|....*...
gi 1014292979 153 IAKALNKQVRLLILDEPT 170
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPT 473
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
258-483 |
2.82e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.39 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLT-AWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwpgqwE----GKIYIDGKQV------ 326
Cdd:COG1135 1 MIELENLSkTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL-----ErptsGSVLVDGVDLtalser 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 327 DIRncqqAIAQGIAMVPE-----DRKrdgivpvmAVGKNITL----------------AALNKFTGgisqLDDAAEQKci 385
Cdd:COG1135 76 ELR----AARRKIGMIFQhfnllSSR--------TVAENVALpleiagvpkaeirkrvAELLELVG----LSDKADAY-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 386 lesiqqlkvktssPDlaigRLSGGNQQK-AIlARCLLLNPRILILDEPTRGIDIGAKYEIYKL---INQlvQQGIAVIVI 461
Cdd:COG1135 138 -------------PS----QLSGGQKQRvGI-ARALANNPKVLLCDEATSALDPETTRSILDLlkdINR--ELGLTIVLI 197
|
250 260
....*....|....*....|..
gi 1014292979 462 SSELPEVLGLSDRVLVMHEGKL 483
Cdd:COG1135 198 THEMDVVRRICDRVAVLENGRI 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-219 |
3.36e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 31 EIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGEEIQASHIRDTeRKGIAIIHQELALVKElTVLENIFLGNEitH 110
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVE--LEKGRIMIDDCDVAKFGLTDL-RRVLSIIPQSPVLFSG-TVRFNIDPFSE--H 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 111 NgimDYDLMTLRCQKLLAQVsLSISP---DTRVGDLG----LGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLD 183
Cdd:PLN03232 1337 N---DADLWEALERAHIKDV-IDRNPfglDAEVSEGGenfsVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR 1412
|
170 180 190
....*....|....*....|....*....|....*.
gi 1014292979 184 IIRDlQQHGIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:PLN03232 1413 TIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
279-485 |
4.10e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDiRNCQQAIAQGIAMVPEDRKRDGIVPVMAVG 358
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA-HGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 359 KNITLAALNKFTGGISQLDDAAEQKCILESIQQLKVKTsspdlaIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:PRK10253 103 ARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQS------VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 439 GAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:PRK10253 177 SHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-228 |
4.10e-07 |
|
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: 50.01 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 16 SVKAIDNVCLRLNAGEIVSLCGENGSGKSTLmkVLCGIYphgsyegeiifagEEIQASHIRDTERKGiaiiHQELALVKE 95
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY-------------ASGKARLISFLPKFS----RNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 96 LTVLENIFLGneithngimdYdlmtlrcqkllaqvslsISPDTRVGDLGLGQQQLVEIAKALNKQVR--LLILDEPTASL 173
Cdd:cd03238 68 LQFLIDVGLG----------Y-----------------LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 174 TEQETSVLLDIIRDLQQHGIACIYISHKLnEVKAISDTICVI--RDGQHIGTRDAAG 228
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWIIDFgpGSGKSGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-215 |
5.24e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.83 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 30 GEIVSLCGENGSGKSTLMKVLCG-IYPH-GSYEG-----EII--FAGEEIQA--SHIRDTERKgIAIIHQELALVKEL-- 96
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNlGKFDDppdwdEILdeFRGSELQNyfTKLLEGDVK-VIVKPQYVDLIPKAvk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 97 -TVLENIflgNEITHNGIMDYDLMTLRCQKLLaqvslsispDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:cd03236 105 gKVGELL---KKKDERGKLDELVDQLELRHVL---------DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1014292979 176 QETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVI 215
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
405-451 |
7.43e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 7.43e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1014292979 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL 451
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-200 |
7.69e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTFG----SVKAIDnvcLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTeR 80
Cdd:PRK10522 323 LELRNVTFAYQdngfSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS--GEILLDGKPVTAEQPEDY-R 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 KGIAIIHQELALVKELtvlenifLGNEITHNGIMDYD--LMTLrcqKLLAQVSLSispDTRVGDLGL--GQQQLVEIAKA 156
Cdd:PRK10522 397 KLFSAVFTDFHLFDQL-------LGPEGKPANPALVEkwLERL---KMAHKLELE---DGRISNLKLskGQKKRLALLLA 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 157 LNKQVRLLILDEPTAsltEQET-------SVLLDIirdLQQHGIACIYISH 200
Cdd:PRK10522 464 LAEERDILLLDEWAA---DQDPhfrrefyQVLLPL---LQEMGKTIFAISH 508
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
277-464 |
8.21e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCqqAIAQGIAMVPEdrkRDGIVPVMA 356
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-KGEILFERQSIKKDLC--TYQKQLCFVGH---RSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNiTLAALNKFTG--GISQLddaaeqkCILESIQQLKvktsspDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTR 434
Cdd:PRK13540 91 LREN-CLYDIHFSPGavGITEL-------CRLFSLEHLI------DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 1014292979 435 GIDIGAKYEIYKLINQLVQQGIAVIVISSE 464
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
258-487 |
9.91e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPVNRhiKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGV-WPGqwEGKIYIDGKQVD-IRNCQQA- 334
Cdd:PRK10908 1 MIRFEHVSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPS--AGKIWFSGHDITrLKNREVPf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 335 IAQGIAMVPEDRKrdgIVPVMAVGKNItlaALNKFTGGISQLDDAAEQKCILESIQQLKVKTSSPDlaigRLSGGNQQKA 414
Cdd:PRK10908 77 LRRQIGMIFQDHH---LLMDRTVYDNV---AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI----QLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKANL 487
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
406-483 |
1.09e-06 |
|
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: 49.74 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGID--IGAKyeIYKLINQLVQ-QGIAVIVISSElPEVLGLSDRVLVMHEGK 482
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQ--IIDLLFELNReRGTTLVLVTHD-PALAARCDRVLRLRAGR 223
|
.
gi 1014292979 483 L 483
Cdd:COG4181 224 L 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
367-479 |
1.19e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 367 NKFTGGISQLDDAAEQKCILES-IQQLKVKTSSpDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIY 445
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLDElVDQLELRHVL-DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
90 100 110
....*....|....*....|....*....|....
gi 1014292979 446 KLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:cd03236 180 RLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
279-459 |
1.76e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.72 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKQVDIRNCQQAIAQ-GiamvpedrKRDGIVPVMAV 357
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA-AGTIKLDGGDIDDPDVAEACHYlG--------HRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 358 GKNITLAAlNKFTGGISQLDDAAEqkCI-LESIQqlkvktsspDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:PRK13539 91 AENLEFWA-AFLGGEELDIAAALE--AVgLAPLA---------HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....
gi 1014292979 437 DIGAKYEIYKLI-NQLVQQGIAVI 459
Cdd:PRK13539 159 DAAAVALFAELIrAHLAQGGIVIA 182
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
396-486 |
1.88e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 396 TSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRV 475
Cdd:NF000106 135 TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHEL 214
|
90
....*....|.
gi 1014292979 476 LVMHEGKLKAN 486
Cdd:NF000106 215 TVIDRGRVIAD 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
406-482 |
2.06e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIS---SELPEVLG----LSDRVLVm 478
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLnrfDEIPDFVQfagvLADCTLA- 214
|
....
gi 1014292979 479 HEGK 482
Cdd:PRK10938 215 ETGE 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-227 |
2.16e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 1 MPYLLEMKNITKTfGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHG--SYEGEIIFAGEEIQASHIRdt 78
Cdd:PRK10418 1 MPQQIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 79 erkGIAIIhqelalvkelTVLENIFLGNEITHNgIMDYDLMTLRCQKLLAQVSLSISPDTRVG-------------DLGL 145
Cdd:PRK10418 78 ---GRKIA----------TIMQNPRSAFNPLHT-MHTHARETCLALGKPADDATLTAALEAVGlenaarvlklypfEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 146 GQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIRDL-QQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTR 224
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
...
gi 1014292979 225 DAA 227
Cdd:PRK10418 224 DVE 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-195 |
2.24e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 6 EMKNITKTFGsVKA-----IDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYE-GEIIFAGEEIQASHIRDte 79
Cdd:TIGR00956 761 HWRNLTYEVK-IKKekrviLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITgGDRLVNGRPLDSSFQRS-- 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 rkgIAIIHQELALVKELTVLEN-IF-----LGNEITHNGIMDYdlmtlrCQKLLAQVSLSISPDTRVGDLGLG----QQQ 149
Cdd:TIGR00956 838 ---IGYVQQQDLHLPTSTVRESlRFsaylrQPKSVSKSEKMEY------VEEVIKLLEMESYADAVVGVPGEGlnveQRK 908
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1014292979 150 LVEIAKALNKQVRLLI-LDEPTASLTEQETSVLLDIIRDLQQHG--IAC 195
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGqaILC 957
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-207 |
2.30e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 18 KAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIfageeIQASHIRDTERKGIAIIHQELALVKELT 97
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSS--GNIY-----YKNCNINNIAKPYCTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 98 VLENIFLGNEITHNGIMDYDLMT-LRCQKLLaqvslsispDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQ 176
Cdd:PRK13541 87 VFENLKFWSEIYNSAETLYAAIHyFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180 190
....*....|....*....|....*....|.
gi 1014292979 177 ETSVLLDIIRDLQQHGIACIYISHKLNEVKA 207
Cdd:PRK13541 158 NRDLLNNLIVMKANSGGIVLLSSHLESSIKS 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-214 |
2.54e-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: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKaidnvcLR-----LNAGEIVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIifageeiqashirD 77
Cdd:COG1245 341 LVEYPDLTKSYGGFS------LEveggeIREGEVLGIVGPNGIGKTTFAKILAGvLKPD---EGEV-------------D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 78 TERKgIAIIHQELALVKELTVLEniFLGNEITHngimdyDLMTLRCQKLLAQvSLSISP--DTRVGDLGLGQQQLVEIAK 155
Cdd:COG1245 399 EDLK-ISYKPQYISPDYDGTVEE--FLRSANTD------DFGSSYYKTEIIK-PLGLEKllDKNVKDLSGGELQRVAIAA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 156 ALNKQVRLLILDEPTASL-TEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICV 214
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLdVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-250 |
2.82e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 23 VCLRLNAGEIVSLCGENGSGKSTL------MKVLCGiyphgsyeGEIIFAGEEIQASHIRDTERKgIAIIHQELALVkEL 96
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLlltfmrMVEVCG--------GEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLF-DG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 97 TVLENI--FLgnEITHNGI-MDYDLMTLRcqKLLAQVSLSIspDTRVGDLGL----GQQQLVEIAKALNKQVRLLIL-DE 168
Cdd:PTZ00243 1399 TVRQNVdpFL--EASSAEVwAALELVGLR--ERVASESEGI--DSRVLEGGSnysvGQRQLMCMARALLKKGSGFILmDE 1472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 169 PTASLTEQetsvlLDiiRDLQQ------HGIACIYISHKLNEVkAISDTICVIRDG--QHIGTRDAAGMSEDDIITMMVg 240
Cdd:PTZ00243 1473 ATANIDPA-----LD--RQIQAtvmsafSAYTVITIAHRLHTV-AQYDKIIVMDHGavAEMGSPRELVMNRQSIFHSMV- 1543
|
250
....*....|
gi 1014292979 241 relTALYPNE 250
Cdd:PTZ00243 1544 ---EALGRSE 1550
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-63 |
2.94e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 2.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 5 LEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEI 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS--GTV 376
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
279-481 |
3.36e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGqwEGKIYIDGKqvdIRNCQQaiaqgIAMVPEDRKRDGIVPVMAV 357
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPS--EGKIKHSGR---ISFSPQ-----TSWIMPGTIKDNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 358 GKNitlaalnKFTGGIsqlddaaeQKCILES-IQQLKVKTSSPDLAIG-RLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:TIGR01271 514 DEY-------RYTSVI--------KACQLEEdIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1014292979 436 IDIGAKYEIYK--LINQLVQQgiAVIVISSELpEVLGLSDRVLVMHEG 481
Cdd:TIGR01271 579 LDVVTEKEIFEscLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
317-500 |
3.36e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 317 GKIYIDGKQV------DIRNCQQAIAQgiamvpedrkrDGIVPVMAVGKNItlaalnKFTGGISQLDD---AAEQKCILE 387
Cdd:PTZ00265 1277 GKILLDGVDIcdynlkDLRNLFSIVSQ-----------EPMLFNMSIYENI------KFGKEDATREDvkrACKFAAIDE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 388 SIQQLKVKTSSPDLAIGR-LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELP 466
Cdd:PTZ00265 1340 FIESLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
170 180 190
....*....|....*....|....*....|....
gi 1014292979 467 EVLGLSDRVLVMHEGKLKANLINHNLTQEQVMEA 500
Cdd:PTZ00265 1420 ASIKRSDKIVVFNNPDRTGSFVQAHGTHEELLSV 1453
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-476 |
3.65e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 126 LLAQVSLS-ISPDTRVGDLGLGQQQLVEIAKALNKQVR--LLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKl 202
Cdd:PRK00635 459 ILIDLGLPyLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 203 NEVKAISDTICVIRDGQHI--------GTRDAAGMSEDDIITMMVGRELTALYPnEPHTTGDEILRIEHLTawhpvnrhI 274
Cdd:PRK00635 538 EQMISLADRIIDIGPGAGIfggevlfnGSPREFLAKSDSLTAKYLRQELTIPIP-EKRTNSLGTLTLSKAT--------K 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 275 KRVNDVSFSLKRGEILGIAGLVGAGRTETIQ-----CLFGVWPGQWEGKIYIDGKQV----------------------- 326
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVEEFIEQGFCSNLSIQWGAIsrlvhitrdlpgrsqrsipltyi 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 327 ----DIRN--------------------------CQQaiAQGIAMVPEDRKRDGIVPVMAVGKNITLAAL-----NKFTG 371
Cdd:PRK00635 689 kafdDLRElfaeqprskrlgltkshfsfntplgaCAE--CQGLGSITTTDNRTSIPCPSCLGKRFLPQVLevrykGKNIA 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 372 GIsqLDDAA--------EQKCILESIQQLkVKTSSPDLAIGR----LSGGNQQKAILARCLLL---NPRILILDEPTRGI 436
Cdd:PRK00635 767 DI--LEMTAyeaekfflDEPSIHEKIHAL-CSLGLDYLPLGRplssLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGL 843
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1014292979 437 DigaKYEIYKLIN---QLVQQGIAVIVISSELpEVLGLSDRVL 476
Cdd:PRK00635 844 H---THDIKALIYvlqSLTHQGHTVVIIEHNM-HVVKVADYVL 882
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-170 |
4.60e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 3 YLLEMKNITKTFGSVKAI-DNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAgeeiqashirdterK 81
Cdd:PRK11819 5 YIYTMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--EFEGEARPA--------------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 82 GIAI--IHQELALVKELTVLENIFLG-----------NEITHN---GIMDYD-LMT------------------------ 120
Cdd:PRK11819 69 GIKVgyLPQEPQLDPEKTVRENVEEGvaevkaaldrfNEIYAAyaePDADFDaLAAeqgelqeiidaadawdldsqleia 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 121 ---LRCQkllaqvslsiSPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PRK11819 149 mdaLRCP----------PWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
278-481 |
4.76e-06 |
|
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: 47.24 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 278 NDVSFSLKRGEILGIAGLVGAGRTETIQCLFG-VWPGQWEGKIYIDGKQVDIrncqqAIAQGIAMVPedrKRDGIVPVMA 356
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGrKTAGVITGEILINGRPLDK-----NFQRSTGYVE---QQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGKNITLAALNKftgGISqlddaaeqkcilesIQQLKVKTSSPDLAIgrlsggnqqkailarclllNPRILILDEPTRGI 436
Cdd:cd03232 96 VREALRFSALLR---GLS--------------VEQRKRLTIGVELAA-------------------KPSILFLDEPTSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1014292979 437 DIGAKYEIYKLINQLVQQGIAVIV-ISSELPEVLGLSDRVLVMHEG 481
Cdd:cd03232 140 DSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKRG 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
401-478 |
8.70e-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: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 401 LAIGR----LSGGNQQKAILARCLLLNPR--ILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDR 474
Cdd:cd03238 79 LTLGQklstLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADW 157
|
....
gi 1014292979 475 VLVM 478
Cdd:cd03238 158 IIDF 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
258-512 |
1.29e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.93 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAwhpVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQW--EGKIYIDGKQVdirNCQQAI 335
Cdd:PRK09984 4 IIRVEKLAK---TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsaGSHIELLGRTV---QREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 336 AQGIAmvpEDRKRDG-------IVPVMAVGKNITLAALNK----------FTGGISQLDDAAEQKCILESIQQLKVKTss 398
Cdd:PRK09984 78 ARDIR---KSRANTGyifqqfnLVNRLSVLENVLIGALGStpfwrtcfswFTREQKQRALQALTRVGMVHFAHQRVST-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 399 pdlaigrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAK---YEIYKLINQlvQQGIAVIVISSELPEVLGLSDRV 475
Cdd:PRK09984 153 -------LSGGQQQRVAIARALMQQAKVILADEPIASLDPESArivMDTLRDINQ--NDGITVVVTLHQVDYALRYCERI 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 1014292979 476 LVMHEGKLKANLINHNLTQEQvMEAALRSEHHVEKQS 512
Cdd:PRK09984 224 VALRQGHVFYDGSSQQFDNER-FDHLYRSINRVEENA 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
279-460 |
1.71e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.95 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKqvDIRNCQQAIAQGIAMVPEdrkRDGIVPVMAVG 358
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR-PDAGEVLWQGE--PIRRQRDEYHQDLLYLGH---QPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 359 KNItlaalnKFTGGISQL--DDAAEQkcILESIQQLKVKtsspDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:PRK13538 93 ENL------RFYQRLHGPgdDEALWE--ALAQVGLAGFE----DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....
gi 1014292979 437 DIGAKYEIYKLINQLVQQGIAVIV 460
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVIL 184
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
369-479 |
1.72e-05 |
|
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: 47.47 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 369 FTGGISQ-LDDAAEQKCILESIQQLKVKTSSpDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKL 447
Cdd:COG1245 176 FKGTVRElLEKVDERGKLDELAEKLGLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARL 254
|
90 100 110
....*....|....*....|....*....|...
gi 1014292979 448 INQLVQQGIAVIVISSELpEVLG-LSDRVLVMH 479
Cdd:COG1245 255 IRELAEEGKYVLVVEHDL-AILDyLADYVHILY 286
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
258-484 |
2.44e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.54 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 258 ILRIEHLTAWHPVNRH-IKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGK---QVDIRNCQQ 333
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHeLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-SGEVSLVGQplhQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 334 AIAQGIAMVPEDRKrdgIVPVMAVGKNITLAALNKftgGISQLDDAAEQKCILESIQQLKVKTSSPdlaiGRLSGGNQQK 413
Cdd:PRK10584 85 LRAKHVGFVFQSFM---LIPTLNALENVELPALLR---GESSRQSRNGAKALLEQLGLGKRLDHLP----AQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 414 AILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLK 484
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
279-503 |
2.47e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.21 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwpGQWEGKIYIDGKQVDIRNCQQAiaqgiamvpedRKRDGIVPvmavg 358
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL--LSTEGEIQIDGVSWNSVTLQTW-----------RKAFGVIP----- 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 359 KNITLaalnkFTGGISQLDDAAEQKC------ILESIQQLKVKTSSPD-----LAIGR--LSGGNQQKAILARCLLLNPR 425
Cdd:TIGR01271 1299 QKVFI-----FSGTFRKNLDPYEQWSdeeiwkVAEEVGLKSVIEQFPDkldfvLVDGGyvLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 426 ILILDEPTRGIDIGAkyeiYKLINQLVQQGIA--VIVISSELPEVLGLSDRVLVMHEGKLK-----ANLINHNLTQEQVM 498
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVT----LQIIRKTLKQSFSncTVILSEHRVEALLECQQFLVIEGSSVKqydsiQKLLNETSLFKQAM 1449
|
....*
gi 1014292979 499 EAALR 503
Cdd:TIGR01271 1450 SAADR 1454
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-219 |
3.67e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 9 NITKTFGSVKAidNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGEEIQASHIR---DTERKGIA 84
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGlTRPQ---KGRIVLNGRVLFDAEKGiclPPEKRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 85 IIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISpdtrvgdlGlGQQQLVEIAKALNKQVRLL 164
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLS--------G-GEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1014292979 165 ILDEPTASLTEQETSVLLDIIRDLQQH-GIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-239 |
3.94e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 31 EIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIQASHIRDTeRKGIAIIHQELALVKElTVLENIFLGNEitH 110
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELER--GRILIDGCDISKFGLMDL-RKVLGIIPQAPVLFSG-TVRFNLDPFNE--H 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 111 NgimDYDLMTLRCQKLLAQV--SLSISPDTRVGDLG----LGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSVLLDI 184
Cdd:PLN03130 1340 N---DADLWESLERAHLKDVirRNSLGLDAEVSEAGenfsVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 185 IRDLQQhgiAC--IYISHKLNEVkaI-SDTICVIRDGQ--HIGTRDAAGMSEDDIITMMV 239
Cdd:PLN03130 1417 IREEFK---SCtmLIIAHRLNTI--IdCDRILVLDAGRvvEFDTPENLLSNEGSAFSKMV 1471
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
253-483 |
4.34e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 253 TTGDEILRIEHLTAwhPVNrHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGvWPGQ--WEGKIYIDGKQVdirn 330
Cdd:CHL00131 2 NKNKPILEIKNLHA--SVN-ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYkiLEGDILFKGESI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 331 cqqaiaqgIAMVPEDRKRDGIV-----PVMAVG-KNITL--AALN---KFTGgISQLDDAAEQKCILESIQQLKVKTS-- 397
Cdd:CHL00131 74 --------LDLEPEERAHLGIFlafqyPIEIPGvSNADFlrLAYNskrKFQG-LPELDPLEFLEIINEKLKLVGMDPSfl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 398 SPDLAIGrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIS--SELPEVLgLSDRV 475
Cdd:CHL00131 145 SRNVNEG-FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyQRLLDYI-KPDYV 222
|
....*...
gi 1014292979 476 LVMHEGKL 483
Cdd:CHL00131 223 HVMQNGKI 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-52 |
6.69e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 6.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1014292979 9 NITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG 52
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGG 49
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
404-485 |
6.80e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 404 GRLSGGNQQKaiLARC--LLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ--GIAVIVISSELPEVLGLsDRVLVMH 479
Cdd:NF033858 135 GKLSGGMKQK--LGLCcaLIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMD 211
|
....*.
gi 1014292979 480 EGKLKA 485
Cdd:NF033858 212 AGRVLA 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
406-479 |
7.59e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 7.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGI-AVIVISSELPEVLGLSDRVLVMH 479
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-207 |
8.53e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 19 AIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGI-YPH-------GSYEGEIIFAGEEIQASHIRDTERKGIAI-IHQE 89
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNkgtvdikGSAALIAISSGLNGQLTGIENIELKGLMMgLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 90 laLVKELT--VLENIFLGNEItHNGIMDYDL-MTLRcqkLLAQVSLSISPDtrvgdlglgqqqlveiakalnkqvrLLIL 166
Cdd:PRK13545 119 --KIKEIIpeIIEFADIGKFI-YQPVKTYSSgMKSR---LGFAISVHINPD-------------------------ILVI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1014292979 167 DEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKA 207
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKS 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
274-481 |
1.05e-04 |
|
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: 43.47 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 274 IKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVP 353
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ-TLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 354 VmAVGKNITLAA-LNKftggisQLDDAAEQKCILESiqQLKVKTSSPDLAIGR----LSGGNQQKAILARCLLLNPRILI 428
Cdd:cd03290 93 A-TVEENITFGSpFNK------QRYKAVTDACSLQP--DIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 429 LDEPTRGIDIgakyeiyKLINQLVQQGI---------AVIVISSELpEVLGLSDRVLVMHEG 481
Cdd:cd03290 164 LDDPFSALDI-------HLSDHLMQEGIlkflqddkrTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
283-482 |
1.07e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.94 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 283 SLKRGEILGIAGLVGAGRTETIQCLFGVW-PGqwEGKIYIDGKQVDIRNcQQAIAqgiamvpedrKRDGIVPVMavgkni 361
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLkPD--EGDIEIELDTVSYKP-QYIKA----------DYEGTVRDL------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 362 tLAALNKFTGGISQLDDAAEQKCILESIQQLKVKTsspdlaigrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAK 441
Cdd:cd03237 82 -LSSITKDFYTHPYFKTEIAKPLQIEQILDREVPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1014292979 442 YEIYKLINQLVQQGIA-VIVISSELPEVLGLSDRVLVMhEGK 482
Cdd:cd03237 152 LMASKVIRRFAENNEKtAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
277-485 |
2.18e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.76 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 277 VNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQwEGKIYIDGKqvdirncqqaiaqgiamvpedrkrdgIVPVMA 356
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT-SGRVEVNGR--------------------------VSALLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 357 VGknitlAALN-KFTG-----------GISQlddaAEQKCILESIQQ---------LKVKTSSpdlaigrlSGgnqqkaI 415
Cdd:COG1134 95 LG-----AGFHpELTGreniylngrllGLSR----KEIDEKFDEIVEfaelgdfidQPVKTYS--------SG------M 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 416 LAR-----CLLLNPRILILDEptrGIDIG-----AKyeIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKA 485
Cdd:COG1134 152 RARlafavATAVDPDILLVDE---VLAVGdaafqKK--CLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
259-482 |
2.97e-04 |
|
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: 42.07 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 259 LRIEHLT-AWHPVNRHIKRV-NDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPgQWEGKIYIDGkqvdirncqqaia 336
Cdd:cd03250 1 ISVEDASfTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-KLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 337 qGIAMVPE------DRKRDgivpvmavgkNITLAalnkftggiSQLD----DAAEQKCILEsiqqlkvktssPDLA---- 402
Cdd:cd03250 67 -SIAYVSQepwiqnGTIRE----------NILFG---------KPFDeeryEKVIKACALE-----------PDLEilpd 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 403 -----IGR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIG-AKYEIYKLINQLVQQGIAVIVISSELpEVLGLS 472
Cdd:cd03250 116 gdlteIGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQL-QLLPHA 194
|
250
....*....|
gi 1014292979 473 DRVLVMHEGK 482
Cdd:cd03250 195 DQIVVLDNGR 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-219 |
4.01e-04 |
|
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: 43.40 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 3 YLLEMKNITKTF--GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiyPHGSYEGEIIFAGEeiqashirdter 80
Cdd:TIGR00957 635 NSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--EMDKVEGHVHMKGS------------ 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 81 kgIAIIHQElALVKELTVLENIFLGNEITHNgimdYDLMTLRCQKLLAQVSLSISPD-TRVGDLGL----GQQQLVEIAK 155
Cdd:TIGR00957 701 --VAYVPQQ-AWIQNDSLRENILFGKALNEK----YYQQVLEACALLPDLEILPSGDrTEIGEKGVnlsgGQKQRVSLAR 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014292979 156 ALNKQVRLLILDEPTASLTEQ-----------ETSVLLDIIRDLQQHGIAciYISHklnevkaiSDTICVIRDGQ 219
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHvgkhifehvigPEGVLKNKTRILVTHGIS--YLPQ--------VDVIIVMSGGK 838
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-212 |
5.41e-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: 40.81 E-value: 5.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 146 GQQQLVEIAKAL----NKQVRLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKlNEVKAISDTI 212
Cdd:cd03227 81 GEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL-PELAELADKL 150
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
383-476 |
6.68e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 383 KCILESIQQLKVKTS----------SPDLAIGRLSGGNQQKAILARCL--LLNPRILILDEPTRGIDIGAKYEIYKLINQ 450
Cdd:PRK00635 444 LSIEEVLQGLKSRLSilidlglpylTPERALATLSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKK 523
|
90 100
....*....|....*....|....*.
gi 1014292979 451 LVQQGIAVIVISSElPEVLGLSDRVL 476
Cdd:PRK00635 524 LRDQGNTVLLVEHD-EQMISLADRII 548
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
279-484 |
6.82e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.76 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 279 DVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWpgQWEGKIYIDGKQVDIRNCQQAiaqgiamvpedRKRDGIVPvmavg 358
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL--NTEGDIQIDGVSWNSVPLQKW-----------RKAFGVIP----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 359 knitlAALNKFTGGISQLDDAAEQ---KCILESIQQLKVKT---SSPD-----LAIGR--LSGGNQQKAILARCLLLNPR 425
Cdd:cd03289 84 -----QKVFIFSGTFRKNLDPYGKwsdEEIWKVAEEVGLKSvieQFPGqldfvLVDGGcvLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1014292979 426 ILILDEPTRGIDIGAkyeiYKLINQLVQQGIA--VIVISSELPEVLGLSDRVLVMHEGKLK 484
Cdd:cd03289 159 ILLLDEPSAHLDPIT----YQVIRKTLKQAFAdcTVILSEHRIEAMLECQRFLVIEENKVR 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-52 |
7.08e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 7.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCG 52
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
8-219 |
7.49e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 8 KNITKTFgsvKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYE----GEI----IFAGEEIQASHIRDTE 79
Cdd:PRK13546 31 KHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKvdrnGEVsviaISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 80 RKGIAIIHQELAlVKELT--VLENIFLGnEITHNGIMDYDlMTLRCqKLLAQVSLSISPDtrvgdlglgqqqlveiakal 157
Cdd:PRK13546 108 FKMLCMGFKRKE-IKAMTpkIIEFSELG-EFIYQPVKKYS-SGMRA-KLGFSINITVNPD-------------------- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014292979 158 nkqvrLLILDEPTASLTEQETSVLLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13546 164 -----ILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-169 |
9.47e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.37 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 5 LEMKNITKTF-GSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEEIqaSHIRDTERkGI 83
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITS--GEIWIGGRVV--NELEPADR-DI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 84 AIIHQELALVKELTVLENIFLGNEITHngiMDYDLMTLRCQKllAQVSLSISP--DTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLKIRG---MPKAEIEERVAE--AARILELEPllDRKPRELSGGQRQRVAMGRAIVREP 153
|
....*...
gi 1014292979 162 RLLILDEP 169
Cdd:PRK11650 154 AVFLFDEP 161
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
406-512 |
1.24e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELpEVLGLSDRVLVMHEGKLK- 484
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKe 819
|
90 100 110
....*....|....*....|....*....|..
gi 1014292979 485 ----ANLINHNLTQEQVMEAALRSEHHVEKQS 512
Cdd:PLN03232 820 egtfAELSKSGSLFKKLMENAGKMDATQEVNT 851
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-88 |
1.65e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 4 LLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTERKGI 83
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
....*
gi 1014292979 84 AIIHQ 88
Cdd:PRK09580 81 FMAFQ 85
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
406-512 |
2.00e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIY-KLINQLVQQGIAVIVISSE--LPEVlglsDRVLVMHEGK 482
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVLVTNQLhfLSQV----DRIILVHEGM 816
|
90 100 110
....*....|....*....|....*....|....*
gi 1014292979 483 LKA-----NLINHNLTQEQVMEAALRSEHHVEKQS 512
Cdd:PLN03130 817 IKEegtyeELSNNGPLFQKLMENAGKMEEYVEENG 851
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
151-210 |
2.03e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014292979 151 VEIAKALNKQVRLLILDEPTASLTEQETSVLLDIIR-DLQQHGI--ACIYISHKlNEVKAISD 210
Cdd:PRK01156 816 VAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDipQVIMISHH-RELLSVAD 877
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
403-478 |
2.54e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 2.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014292979 403 IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPeVLG-LSDRVLVM 478
Cdd:PRK13409 210 ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLA-VLDyLADNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
399-433 |
3.01e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 3.01e-03
10 20 30
....*....|....*....|....*....|....*
gi 1014292979 399 PDLAIGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:PRK11819 157 WDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-173 |
5.58e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 22 NVCLRLNAGEIVSLCGENGSGKSTLMKVLCGiyphgsyegeiifageEIQASHIRDTERKGIAIIHQElALVKELTVLEN 101
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLS----------------QFEISEGRVWAERSIAYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1014292979 102 IFLGNEITHNGIMDydlmTLRCQKLLAQV-SLSISPDTRVGDLGL----GQQQLVEIAKAL--NKQVRLliLDEPTASL 173
Cdd:PTZ00243 741 ILFFDEEDAARLAD----AVRVSQLEADLaQLGGGLETEIGEKGVnlsgGQKARVSLARAVyaNRDVYL--LDDPLSAL 813
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
35-57 |
6.29e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.21 E-value: 6.29e-03
10 20
....*....|....*....|....*.
gi 1014292979 35 LCGENGSGKSTLMK---VLCGIYPHG 57
Cdd:COG3910 42 FVGENGSGKSTLLEaiaVAAGFNPEG 67
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
406-483 |
7.84e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 406 LSGGnQQKAILARCLLLNP-RILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIS--SELPEVLGLSDRVLVMHEGK 482
Cdd:PLN03140 337 ISGG-QKKRVTTGEMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllQPAPETFDLFDDIILLSEGQ 415
|
.
gi 1014292979 483 L 483
Cdd:PLN03140 416 I 416
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
273-483 |
9.38e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 38.47 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 273 HIKRvnDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVwpgqwE----GKIYIDGKQVdirNCQQAIAQGIAMVPEDRkr 348
Cdd:PRK11000 17 VISK--DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-----EditsGDLFIGEKRM---NDVPPAERGVGMVFQSY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 349 dGIVPVMAVGKNIT----LAALNKftGGISQ-LDDAAEqkcILESIQQLKVKTSSpdlaigrLSGGNQQKAILARCLLLN 423
Cdd:PRK11000 85 -ALYPHLSVAENMSfglkLAGAKK--EEINQrVNQVAE---VLQLAHLLDRKPKA-------LSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014292979 424 PRILILDEPTRGID----IGAKYEIYKLINQLvqqGIAVIVISSELPEVLGLSDRVLVMHEGKL 483
Cdd:PRK11000 152 PSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
398-509 |
9.84e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014292979 398 SPDL---AIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAkyeIYKLINQLVQQGIAVIVIS-------SELPE 467
Cdd:PLN03073 334 TPEMqvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVShareflnTVVTD 410
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1014292979 468 VLGLSDRVLVMHEGK---LKANLINHNLTQEQVMEAALRSEHHVE 509
Cdd:PLN03073 411 ILHLHGQKLVTYKGDydtFERTREEQLKNQQKAFESNERSRSHMQ 455
|
|
| |
